KR20200011955A - 글리칸 분석을 위한 효소 - Google Patents
글리칸 분석을 위한 효소 Download PDFInfo
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- KR20200011955A KR20200011955A KR1020197036845A KR20197036845A KR20200011955A KR 20200011955 A KR20200011955 A KR 20200011955A KR 1020197036845 A KR1020197036845 A KR 1020197036845A KR 20197036845 A KR20197036845 A KR 20197036845A KR 20200011955 A KR20200011955 A KR 20200011955A
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/924—Hydrolases (3) acting on glycosyl compounds (3.2)
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- G—PHYSICS
- G01—MEASURING; TESTING
- G01N—INVESTIGATING OR ANALYSING MATERIALS BY DETERMINING THEIR CHEMICAL OR PHYSICAL PROPERTIES
- G01N2333/00—Assays involving biological materials from specific organisms or of a specific nature
- G01N2333/90—Enzymes; Proenzymes
- G01N2333/914—Hydrolases (3)
- G01N2333/948—Hydrolases (3) acting on peptide bonds (3.4)
- G01N2333/95—Proteinases, i.e. endopeptidases (3.4.21-3.4.99)
- G01N2333/952—Proteinases, i.e. endopeptidases (3.4.21-3.4.99) derived from bacteria
Abstract
본 발명은 당단백질을 연구하는데 유용한 효소 및 이들의 조합, 및 상응하는 이의 사용 방법에 관한 것이다. 특히, 본 발명은 추가적인 프로테아제 및/또는 글리코시다제, 바람직하게는 O-당단백질-특이적인 엔도프로테아제 및/또는 O-글리코시다제를 포함하는 시알리다제 조성물에 관한 것이다.
Description
본 발명은 당단백질을 연구하는데 유용한 효소 및 이들의 조합, 그리고 상응하는 사용 방법에 관한 것이다.
단백질의 당화(glycosylation)는 인간에서 신호 전달, 이송, 단백질분해 활성으로부터의 보호, 접착, 염증 반응, 미생물 군집화 등을 포함하는 많은 생리적인 기능에서 중추적인 역할을 한다. 단백질에 부착된 대부분의 글리칸 사슬은, O- 또는 N-연결과는 무관하게, 말단 시알산(sialic acid)에 의해 수식된다. 당단백질 상의 최외각 글리칸이 있으면, 이들의 존재/부재는 종종 예를 들어 면역글로불린에서 염증 가능성을 포함하는 하류 효과에 매우 중요하다. 단백질 상의 시알산은 소정의 단백질 상에서의 존재/부재, 뿐만 아니라 개별적인 구조적 변형 모두에 대하여 이종적이다. 이들은 또한 일반적으로 음전하를 띄고 있어, 질량 분광분석법 분석을 복잡하게 한다. 이는 당단백질의 연구를 어렵게 할 뿐만 아니라, 제조자가 당단백질 뱃치(batch)가 균일한 방식으로 기능을 할 것인지 확인할 수 있는 능력을 감소시킨다.
이들 문제를 극복하기 위해서, 글리칸의 복잡성을 감소시키도록 CHO 세포를 유전적으로 조작하려는 시도가 있었으나, 이는 기능에 영향을 미칠 수 있다. 화학적 접근법이 또한 사용되었으나, 이들은 종종 단백질을 손상시켰다. 당단백질로부터 시알산을 제거하기 위한 대안적인 접근법이 필요하다. 또한, 일단 시알산이 제거되면, 남아있는 글리칸 사슬, 특히 O-연결된 것들을 연구하기 위한 더 많은 수단이 필요하다.
본 발명의 개요
본 발명은 이하의 것들을 제공하되:
이하의 것들로부터 독립적으로 선택된 제1 시알리다제(sialidase)를 포함하는 조성물:
(a) 서열번호 2의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
(b) 서열번호 2의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
(c) 서열번호 2의 서열의 절편인 아미노산 서열, 또는 서열번호 2의 아미노산 서열과 적어도 85% 동일한 아미노산 서열의 절편을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
선택적으로, 상기 제1 시알리다제는 N 말단에 추가적인 메티오닌 및/또는 C 말단에 히스티딘 태그를 포함하고, 상기 태그는 링커에 의해 C 말단에 연결될 수 있다.
본 발명은 또한 이하의 것들로부터 독립적으로 선택된 제2 시알리다제를 추가로 포함하는, 상기에서 정의한 바와 같은 조성물을 제공하되:
(d) 서열번호 5의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
(e) 서열번호 5의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
(f) 서열번호 5의 서열의 절편인 아미노산 서열, 또는 서열번호 5의 아미노산 서열과 적어도 85% 동일한 아미노산 서열의 절편을 포함하거나 또는 이로써 이루어지는 폴리펩티드.
선택적으로, 상기 제2 시알리다제는 N 말단에서 추가적인 메티오닌, 및/또는 C 말단에서 히스티딘 태그를 포함하고, 상기 태그는 링커에 의해 C 말단에 연결될 수 있다.
조성물은 추가적으로 글리코시다제 및/또는 프로테아제를 포함할 수 있다:
이는 선택적으로 고도로 정제된, 또는 분리된 형태로 존재한다.
본 발명은 또한 당단백질을 변형시키는 방법을 제공하는데, 이는 당단백질을 함유하는 샘플을 상기에서 정의한 바와 같이 접촉시키는 단계를 포함하되, 선택적으로, 생성되는 산물은 분석된다.
도 1: 아커만시아(Akkermansia) 시알리다제의 발현 및 정제. 모든 4개의 시알리다제(본원에서 Am0707 및 Am1757으로 제시됨)는 잘 발현되고, 높은 균일성을 갖도록 정제될 수 있다. 값들(mg/㎖)은 His-정제 이후 얻은 농도를 나타낸다.
도 2: 상이한 시알산 결합에 대한 시알리다제 활성. 2개의 시알리다제 산물[Am1757, 및 혼합물(Am1757 & Am0707)]은 유리된 시알산의 양이 측정된 후, 30분 동안 3개의 상이한 기질(3개의 지정된 타입의 시알산 결합을 나타냄)과 함께 항온 처리되었다(incubated).
도 3: Am0707 및 Am1757에 대한 최적 조건이 결정되었다. 시알리다제의 효소 활성에 영향을 미치는 조건(이온, NaCl 및 pH 포함)은 2-3 시알락토스 기질을 사용하여 조사되었고, 유리된 시알산은 15분 동안 항온 처리 이후 정량화되었다.
도 4: 당단백질(glycoprotein)의 조합된 시알리다제 처리가, 단일 시알리다제를 사용한 경우보다 더욱 효율적이었다. 시알리다제는 이들이 SDS-PAGE를 사용하여 분리된 후 60분 동안 0.5 ㎍ 페투인과 함께 항온처리되었다. Smix는 Am0707 및 Am1757을 모두 함유하였으나, C. 퍼프린겐(perfringens) 시알리다제가 벤치마크 비교로서 사용되었다. 모든 반응은 제조자의 지침에 따라서 항온 처리된 벤치마크 산물을 제외하고는, 37℃에서, 20 mM Tris-HCl pH 6.8 중에서 일어났다.
도 5: GVS_Smix는 시판되는 시알리다제보다 우월하다. New England Biolabs로부터의 몇몇 기존의 상업적인 시알리다제(각 세트에서의 첫번째 3개 컬럼)는 AM1757+Am0707 혼합물(GVS_Smix), 및 Am1757 및 Am0707 효소의 각각에 대해 개별적으로 시험되었다. 각각은 분석되기 전에 30분 동안 37℃에서 특이적인 시알리다제 기질(3개의 지정된 타입의 시알산 결합을 나타냄)과 함께 항온처리되었다. FU(형광 단위)는 유리된 시알산의 양을 나타낸다.
도 6: GVS_Smix는 페투인에서 시알산을 완전히 제거할 수 있다. SDS-PAGE 및 SNA 블로팅은 Smix(AM1757+Am0707 혼합물) 뿐만 아니라 2개의 New England Biolabs 산물(NEB A 및 NEB O)이 페투인 내의 2-3 및 2-6 시알산 결합에서 시알산을 완전히 제거할 수 있다는 것을 보여준다. 2개의 2-3 특이적인 효소 Am1757 및 New England Biolabs NEB S는 페투인에서 시알산을 완전히 제거할 수 없었다(asialylate).
도 7: GVS_Smix(AM1757+Am0707 혼합물; 제 1 세트의 바)는 천연의 단백질로부터 시알산을 모든 3개의 시험된 상업적인 산물과 유사한 수준, 또는 이보다 더 나은 수준으로 방출한다(마지막 3개 세트의 바). Am1757 효소 단독도 또한 도시되었다(제 2 세트의 바). 단백질을 이들의 각각의 버퍼 중의 시알리다제와 혼합하고, 시알산 발생 버퍼의 첨가 이전 15 분 동안 항온처리하였다. 모든 항온 처리는 37℃에서 각각의 버퍼 중에서 실시되었다(GVS-Smix에 대해서는, 이는 20 mM Tris-HCl pH 6.8였다).
도 8: O-글리코시다제의 재조합 발현. (A) S. 오랄리스(oralis) 및 B. 비피둠(bifidum)으로부터의 O-글리코시다제가 발현되고, 친화성 정제되고, SDS-PAGE 상에서 분리되었다. (B) 4℃에서 0-6 일 동안 저장된 S. 오랄리스 O-글리코시다제의 안정성 분석 시험.
도 9: O-글리코시다제는 코어 타입 1, 2 및 3의 pNP-표지된 O-글리칸을 가수분해할 수 있다. S. 오랄리스(S.o) 및 B. 비피둠(B.b)로부터의 상이한 농도의 O-글리코시다제를 (A) 코어 1, (B) 코어 2, 및 (C) 코어 3의 O-글리칸과 함께 항온처리하였고, pNP의 방출은 흡광도 AT 405 nm에서의 변화로서 측정하였다.
도 10: S. 오랄리스 글리코시다제는 MgCl2이 보충된 염기성 pH에서 더 높은 활성을 갖는다. O-글리코시다제는 상이한 pH (A)에서, 상이한 이온 (B), 및 상이한 농도의 MgCl2(C)와 함께 항온 처리되어, 최적 버퍼를 결정하였다.
도 11: O-글리코시다제 활성은 시간 및 투여량-의존적이다. TNFαR(1㎍)은 대조군으로서 GVS_Smix 시알리다제 혼합물 단독[TNFaR(Smix)로 표기된 래인]과 함께, 또는 도시된 S. 오랄리스로부터의 상이한 양의 O-글리코시다제(So)와 조합된 GVS_Smix 시알리다제 혼합물["+5 ㎍ So 등"]과 함께 항온 처리되었다. 지정된 양의 첨가된 O-글리코시다제는 나노드롭으로부터의 값에 의존한다. 그러나, 절편화 때문에, 첨가된 실제량의 전체-길이 단백질은 표기된 값의 ca 10-20%에 더 가깝다. 이들 샘플은 2 mM CaCl2이 보충되었으나 MgCl2은 보충되지 않는 20 mM Tris-HCl pH 8.0 중에서 항온처리되었다.
도 12: O-글리코시다제는 모든 연구된 천연의 당단백질들에 대해 작용할 수 있다. 상이한 천연의 단백질(P)은 시알리다제(Smix)와 S. 오랄리스(So-glyk) 및 B. 비피둠(Bb-glyk)으로부터의 O-글리코시다제의 GVS_Smix 혼합물과 함께 항온 처리되었다. 항온 처리는 밤새 실시되었고, 이후 산물을 SDS-PAGE 상에서 분석하였다.
도 13: S. 오랄리스 O-글리코시다제는 유리하게는 천연의 당단백질에 대한 작용에 대해 시판용 산물과 비교되었다. 천연의 TNFαR은 대조군으로서 GVS_Smix 시알리다제 혼합물 단독[TNFaR (Smix)로 표시된 래인]과 함께, 또는 도시된 S. 오랄리스로부터의 상이한 양의 O-글리코시다제(So)와 조합된 GVS_Smix 시알리다제 혼합물["+ So (0.5 ㎍)" 등]과 함께, 또는 제조자가 이와 함께 공급한, 시알리다제와 조합된 도시된 양의 시판되는 O-글리코시다제(NEB)["+NEB (3ul)" 등]와 함께 항온처리되었다. 모든 효소는 1 시간 또는 16 시간 동안 이들 각각의 버퍼에서 TNFαR과 함께 항온 처리되었다. S. 오랄리스 글리코시다제["So (0.5 ㎍)"]의 최고 투여량은 대략 몰 농도로 상업적인 O-글리코시다제(NEB)의 0.3 ul이다. NEB 처리된 샘플에서의 저 분자량의 분명한 밴드(겔의 상부)는 수반된 시알리다제이다.
도 14: 글리칸 조성물은 활성에 영향을 미친다. O-글리코시다제(So)의 첨가 이전의, 기질과 시알리다제(S) 및/또는 갈락토시다제(G)의 항온 처리; 최적 버퍼(20 mM Tris-HCl pH 8.0) 중에서 밤새 37℃에서 항온 처리함.
도 15: 최종적인 산물은 경쟁적이다. O-글리코시다제의 (효소:기질) 1:40의 비, 뿐만 아니라 시알리다제 혼합물 중의 Am1757+Am0707에 대해서는 1:40+1:40의 효소 기질 비, 20 mM Tris-HCl pH 6.8 중의 모든 3개의 효소(Smix / O-glyk로 표시된 래인)를 사용하여, S. 오랄리스 O-글리코시다제의 활성을 상업적인 O-글리코시다제 + 시알리다제 조합의 경우[NEB(O-glyk 킷트로 표기된 래인]와 비교하였다. S. 오랄리스 O-글리코시다제 + 시알리다제 혼합물("+GVS")에 의한 TNFaR로부터의 O-글리칸 제거는, ConA(N-연결 글리칸) 및 비처리된 TNFaR 대조군으로서 자칼린(O-연결 글리칸)을 사용하여, 렉틴 블로팅에 의해 확인되었다.
도 16: O-글리코시다제 + 시알리다제 다발(Smix/O-glyk)은 매우 다양한 당단백질에 대해 활성을 갖는다. 이들의 최종 농도로, 그리고 20 mM Tris-HCl pH 6.8 중의 제형(1:40)으로 첨가된 효소는, 4시간 동안 37℃에서 당단백질과 함께 항온처리된 후, SDS-PAGE 상에서 분리되었다.
도 17: 특이적인 시알산 결합은 O-글리코시다제 활성에 영향을 미친다. 이들의 최종 농도로, 그리고 20 mM Tris-HCl pH 6.8 중의 제형(1:40)으로 첨가된 효소(Am1757, Am0707 또는 Smix)는 15분~4시간 동안 37℃에서 TNFαR과 함께 항온 처리된 후, SDS-PAGE 상에서 분리되었다.
도 18: S. 오랄리스 O-글리코시다제는 적어도 부분적으로 강력한 시알리다제에 기인하여 탁월하다. S. 오랄리스 O-글리코시다제 (GVS O-glyk) 또는 상업적인 O-글리코시다제(NEB O-glyk)는 GVS_Smix 시알리다제 혼합물(GVS 시알리다제)과 함께, 또는 상업적인 시알리다제(NEB A, NEB S, NEB O)와 함께 항온 처리되었다. 적합한 버퍼(예를 들어, GVS에 대해서는 20 mM Tris-HCl pH 6.8)가 사용되었고, 효소의 각 세트는 산물을 SDS-PAGE 상에서 분리하기 전에, 4시간 동안 37℃에서 엔브렐(Enbrel)(에타너셉트, Etanercept)과 함께 항온 처리되었다.
도 19: 2-3 결합된 시알산은 O-당단백질 특이적인 엔도프로테아제(LS)의 효율성을 제한한다. 당단백질 기질로서 엔브렐을 사용하여 LS와 다양한 시알리다제의 세트를 30분~20시간 동안 동시에 항온 처리하게 되면, 2-3 특이적인 시알디아제 1757의 존재하에, 또는 혼합물(0707 + 1757)에 의해 더 높은 효율성을 나타낸 반면, 광범위한 시알리다제 0707은 겉보기에 LS의 전체 활성에 필수적인 것이 아니고, 따라서 2-6 (및 2-8) 결합이 LS 활성에 대한 염려 사항이 아니라는 것을 암시한다.
도 2: 상이한 시알산 결합에 대한 시알리다제 활성. 2개의 시알리다제 산물[Am1757, 및 혼합물(Am1757 & Am0707)]은 유리된 시알산의 양이 측정된 후, 30분 동안 3개의 상이한 기질(3개의 지정된 타입의 시알산 결합을 나타냄)과 함께 항온 처리되었다(incubated).
도 3: Am0707 및 Am1757에 대한 최적 조건이 결정되었다. 시알리다제의 효소 활성에 영향을 미치는 조건(이온, NaCl 및 pH 포함)은 2-3 시알락토스 기질을 사용하여 조사되었고, 유리된 시알산은 15분 동안 항온 처리 이후 정량화되었다.
도 4: 당단백질(glycoprotein)의 조합된 시알리다제 처리가, 단일 시알리다제를 사용한 경우보다 더욱 효율적이었다. 시알리다제는 이들이 SDS-PAGE를 사용하여 분리된 후 60분 동안 0.5 ㎍ 페투인과 함께 항온처리되었다. Smix는 Am0707 및 Am1757을 모두 함유하였으나, C. 퍼프린겐(perfringens) 시알리다제가 벤치마크 비교로서 사용되었다. 모든 반응은 제조자의 지침에 따라서 항온 처리된 벤치마크 산물을 제외하고는, 37℃에서, 20 mM Tris-HCl pH 6.8 중에서 일어났다.
도 5: GVS_Smix는 시판되는 시알리다제보다 우월하다. New England Biolabs로부터의 몇몇 기존의 상업적인 시알리다제(각 세트에서의 첫번째 3개 컬럼)는 AM1757+Am0707 혼합물(GVS_Smix), 및 Am1757 및 Am0707 효소의 각각에 대해 개별적으로 시험되었다. 각각은 분석되기 전에 30분 동안 37℃에서 특이적인 시알리다제 기질(3개의 지정된 타입의 시알산 결합을 나타냄)과 함께 항온처리되었다. FU(형광 단위)는 유리된 시알산의 양을 나타낸다.
도 6: GVS_Smix는 페투인에서 시알산을 완전히 제거할 수 있다. SDS-PAGE 및 SNA 블로팅은 Smix(AM1757+Am0707 혼합물) 뿐만 아니라 2개의 New England Biolabs 산물(NEB A 및 NEB O)이 페투인 내의 2-3 및 2-6 시알산 결합에서 시알산을 완전히 제거할 수 있다는 것을 보여준다. 2개의 2-3 특이적인 효소 Am1757 및 New England Biolabs NEB S는 페투인에서 시알산을 완전히 제거할 수 없었다(asialylate).
도 7: GVS_Smix(AM1757+Am0707 혼합물; 제 1 세트의 바)는 천연의 단백질로부터 시알산을 모든 3개의 시험된 상업적인 산물과 유사한 수준, 또는 이보다 더 나은 수준으로 방출한다(마지막 3개 세트의 바). Am1757 효소 단독도 또한 도시되었다(제 2 세트의 바). 단백질을 이들의 각각의 버퍼 중의 시알리다제와 혼합하고, 시알산 발생 버퍼의 첨가 이전 15 분 동안 항온처리하였다. 모든 항온 처리는 37℃에서 각각의 버퍼 중에서 실시되었다(GVS-Smix에 대해서는, 이는 20 mM Tris-HCl pH 6.8였다).
도 8: O-글리코시다제의 재조합 발현. (A) S. 오랄리스(oralis) 및 B. 비피둠(bifidum)으로부터의 O-글리코시다제가 발현되고, 친화성 정제되고, SDS-PAGE 상에서 분리되었다. (B) 4℃에서 0-6 일 동안 저장된 S. 오랄리스 O-글리코시다제의 안정성 분석 시험.
도 9: O-글리코시다제는 코어 타입 1, 2 및 3의 pNP-표지된 O-글리칸을 가수분해할 수 있다. S. 오랄리스(S.o) 및 B. 비피둠(B.b)로부터의 상이한 농도의 O-글리코시다제를 (A) 코어 1, (B) 코어 2, 및 (C) 코어 3의 O-글리칸과 함께 항온처리하였고, pNP의 방출은 흡광도 AT 405 nm에서의 변화로서 측정하였다.
도 10: S. 오랄리스 글리코시다제는 MgCl2이 보충된 염기성 pH에서 더 높은 활성을 갖는다. O-글리코시다제는 상이한 pH (A)에서, 상이한 이온 (B), 및 상이한 농도의 MgCl2(C)와 함께 항온 처리되어, 최적 버퍼를 결정하였다.
도 11: O-글리코시다제 활성은 시간 및 투여량-의존적이다. TNFαR(1㎍)은 대조군으로서 GVS_Smix 시알리다제 혼합물 단독[TNFaR(Smix)로 표기된 래인]과 함께, 또는 도시된 S. 오랄리스로부터의 상이한 양의 O-글리코시다제(So)와 조합된 GVS_Smix 시알리다제 혼합물["+5 ㎍ So 등"]과 함께 항온 처리되었다. 지정된 양의 첨가된 O-글리코시다제는 나노드롭으로부터의 값에 의존한다. 그러나, 절편화 때문에, 첨가된 실제량의 전체-길이 단백질은 표기된 값의 ca 10-20%에 더 가깝다. 이들 샘플은 2 mM CaCl2이 보충되었으나 MgCl2은 보충되지 않는 20 mM Tris-HCl pH 8.0 중에서 항온처리되었다.
도 12: O-글리코시다제는 모든 연구된 천연의 당단백질들에 대해 작용할 수 있다. 상이한 천연의 단백질(P)은 시알리다제(Smix)와 S. 오랄리스(So-glyk) 및 B. 비피둠(Bb-glyk)으로부터의 O-글리코시다제의 GVS_Smix 혼합물과 함께 항온 처리되었다. 항온 처리는 밤새 실시되었고, 이후 산물을 SDS-PAGE 상에서 분석하였다.
도 13: S. 오랄리스 O-글리코시다제는 유리하게는 천연의 당단백질에 대한 작용에 대해 시판용 산물과 비교되었다. 천연의 TNFαR은 대조군으로서 GVS_Smix 시알리다제 혼합물 단독[TNFaR (Smix)로 표시된 래인]과 함께, 또는 도시된 S. 오랄리스로부터의 상이한 양의 O-글리코시다제(So)와 조합된 GVS_Smix 시알리다제 혼합물["+ So (0.5 ㎍)" 등]과 함께, 또는 제조자가 이와 함께 공급한, 시알리다제와 조합된 도시된 양의 시판되는 O-글리코시다제(NEB)["+NEB (3ul)" 등]와 함께 항온처리되었다. 모든 효소는 1 시간 또는 16 시간 동안 이들 각각의 버퍼에서 TNFαR과 함께 항온 처리되었다. S. 오랄리스 글리코시다제["So (0.5 ㎍)"]의 최고 투여량은 대략 몰 농도로 상업적인 O-글리코시다제(NEB)의 0.3 ul이다. NEB 처리된 샘플에서의 저 분자량의 분명한 밴드(겔의 상부)는 수반된 시알리다제이다.
도 14: 글리칸 조성물은 활성에 영향을 미친다. O-글리코시다제(So)의 첨가 이전의, 기질과 시알리다제(S) 및/또는 갈락토시다제(G)의 항온 처리; 최적 버퍼(20 mM Tris-HCl pH 8.0) 중에서 밤새 37℃에서 항온 처리함.
도 15: 최종적인 산물은 경쟁적이다. O-글리코시다제의 (효소:기질) 1:40의 비, 뿐만 아니라 시알리다제 혼합물 중의 Am1757+Am0707에 대해서는 1:40+1:40의 효소 기질 비, 20 mM Tris-HCl pH 6.8 중의 모든 3개의 효소(Smix / O-glyk로 표시된 래인)를 사용하여, S. 오랄리스 O-글리코시다제의 활성을 상업적인 O-글리코시다제 + 시알리다제 조합의 경우[NEB(O-glyk 킷트로 표기된 래인]와 비교하였다. S. 오랄리스 O-글리코시다제 + 시알리다제 혼합물("+GVS")에 의한 TNFaR로부터의 O-글리칸 제거는, ConA(N-연결 글리칸) 및 비처리된 TNFaR 대조군으로서 자칼린(O-연결 글리칸)을 사용하여, 렉틴 블로팅에 의해 확인되었다.
도 16: O-글리코시다제 + 시알리다제 다발(Smix/O-glyk)은 매우 다양한 당단백질에 대해 활성을 갖는다. 이들의 최종 농도로, 그리고 20 mM Tris-HCl pH 6.8 중의 제형(1:40)으로 첨가된 효소는, 4시간 동안 37℃에서 당단백질과 함께 항온처리된 후, SDS-PAGE 상에서 분리되었다.
도 17: 특이적인 시알산 결합은 O-글리코시다제 활성에 영향을 미친다. 이들의 최종 농도로, 그리고 20 mM Tris-HCl pH 6.8 중의 제형(1:40)으로 첨가된 효소(Am1757, Am0707 또는 Smix)는 15분~4시간 동안 37℃에서 TNFαR과 함께 항온 처리된 후, SDS-PAGE 상에서 분리되었다.
도 18: S. 오랄리스 O-글리코시다제는 적어도 부분적으로 강력한 시알리다제에 기인하여 탁월하다. S. 오랄리스 O-글리코시다제 (GVS O-glyk) 또는 상업적인 O-글리코시다제(NEB O-glyk)는 GVS_Smix 시알리다제 혼합물(GVS 시알리다제)과 함께, 또는 상업적인 시알리다제(NEB A, NEB S, NEB O)와 함께 항온 처리되었다. 적합한 버퍼(예를 들어, GVS에 대해서는 20 mM Tris-HCl pH 6.8)가 사용되었고, 효소의 각 세트는 산물을 SDS-PAGE 상에서 분리하기 전에, 4시간 동안 37℃에서 엔브렐(Enbrel)(에타너셉트, Etanercept)과 함께 항온 처리되었다.
도 19: 2-3 결합된 시알산은 O-당단백질 특이적인 엔도프로테아제(LS)의 효율성을 제한한다. 당단백질 기질로서 엔브렐을 사용하여 LS와 다양한 시알리다제의 세트를 30분~20시간 동안 동시에 항온 처리하게 되면, 2-3 특이적인 시알디아제 1757의 존재하에, 또는 혼합물(0707 + 1757)에 의해 더 높은 효율성을 나타낸 반면, 광범위한 시알리다제 0707은 겉보기에 LS의 전체 활성에 필수적인 것이 아니고, 따라서 2-6 (및 2-8) 결합이 LS 활성에 대한 염려 사항이 아니라는 것을 암시한다.
서열의 간단한 설명
서열번호 1, 2 및 3은 각각 아커만시아 뮤시니필라(Akkermansia muciniphila)로부터 분리된 시알리다제의 아미노산 서열이다. 서열번호 1은 N 말단에서 신호 모티프를 포함하는 야생형 서열이다. 서열번호 2는 신호 모티프가 제거된 야생형 서열이다. 서열번호 3은 추가적인 N 말단 메티오닌 및 C-말단 링커 + His6 태그를 포함하는 점을 제외하고는, 서열번호 2와 동일하다. 서열번호 2의 서열을 포함하는 어느 서열(서열번호 1 내지 3의 각각을 포함)도, 본원에서 Am0707로 지칭될 수 있다.
서열번호 4, 5 및 6은 각각 아커만시아 뮤시니필라로부터 분리된 다른 시알리다제의 아미노산 서열이다. 서열번호 4는 N 말단에 신호 모티프를 포함하는 야생형 서열이다. 서열번호 5는 신호 모티프가 제거된 야생형 서열이다. 서열번호 6은 추가적인 N 말단 메티오닌 및 C-말단 링커 + His6 태그를 포함하는 점을 제외하고는, 서열번호 5와 동일하다. 서열번호 5의 서열을 포함하는 어느 서열(서열번호 4 내지 6의 각각을 포함)도, 본원에서 Am1757로 지칭될 수 있다.
서열번호 7, 8, 9 및 10은 각각 S. 오랄리스로부터 분리된 O-글리코시다제의 아미노 서열이다. 서열번호 7은 N 말단에서 신호 모티프 및 C 말단에서 LPXTG 벽 앵커 모티프를 포함하는 야생형 서열이다. 서열번호 8은 신호 모티프가 제거된 야생형 서열이다. 서열번호 9는 신호 모티프 및 벽 앵커 모티프가 제거된 야생형 서열이다. 서열번호 10은, 추가적인 N 말단 메티오닌 및 C-말단 링커 + His6 태그를 포함하는 점을 제외하고는, 서열번호 9와 동일하다. 서열번호 9의 서열을 포함하는 어느 서열(서열번호 7 내지 10의 각각을 포함)은, 본원에서 "O-glyk" 또는 "So"로 지칭될 수 있다.
서열번호 11은 O-당단백질-특이적인 엔도프로테아제의 아미노산 서열이다.
서열번호 12는 O-당단백질-특이적인 엔도프로테아제 활성을 갖는 예시적인 폴리펩티드의 아미노산 서열이다. 서열번호 11에 비해, 이는 추가적인 N 말단 메티오닌 및 C-말단 링커 + His6 태그를 포함한다. 이 서열로 이루어지는 폴리펩티드는, 본원에서 LS로 지칭될 수 있다.
서열번호 13은 서열번호 10의 아미노산 서열로 이루어지는 폴리펩티드를 암호화하는 예시적인 핵산 서열이다.
본 발명의 상세한 설명
기재된 산물 및 방법의 상이한 적용은 당업계의 특정 요구에 맞게 맞춤형으로 수행될 수 있는 것으로 이해될 것이다. 또한, 본원에 사용된 용어는 단지 본 발명의 특정 구현예만을 설명하려는 목적을 위한 것이며, 이를 제한하려는 의도가 아니다. 상기 또는 이하에서 본원에 인용된 모든 간행물, 특허 및 특허 출원은, 전체로서 본원에 참고로 포함된다.
본 명세서 및 첨부된 청구항에서 사용될 때, 단수형["a", "an", 및 "the"]은 문맥에서 달리 기재된 바 없는 경우, 복수형을 포함한다. 따라서, 예를 들어, "폴리펩티드"에 대한 언급은 "폴리펩티드들" 등을 포함한다.
본 명세서는 특히 시알리다제, O-글리코시다제 및 O-당단백질-특이적인 엔도프로테아제인 폴리펩티드와 관련된다. 따라서, 용어 폴리펩티드의 일반적 사용은 이들 타입의 효소의 각각에 적용될 수 있다.
일반적인 폴리펩티드 특성들
"폴리펩티드(polypeptide)"는 본원에서 가장 넓은 의미로, 둘 이상의 하위 단위 아미노산, 아미노산 유사체, 또는 다른 펩티드 모방체의 화합물을 지칭하는데 사용된다. 따라서, 용어 "폴리펩티드"는 짧은 펩티드 서열, 및 또한 더 긴 폴리펩티드 및 단백질을 포함한다. 용어 "단백질(protein)", "펩티드(peptide)" 및 "폴리펩티드"는 상호교환적으로 사용할 수 있다. 본원에서 사용된 용어 "아미노산(amino acid)"은, D 또는 L 둘 다의 광학적 이성질체, 및 아미노산 유사체 및 펩티드 모방체를 포함하는 자연적 및/또는 비자연적 또는 합성적 아미노산을 지칭한다.
폴리펩티드는 재조합 또는 합성적 방법을 포함하는 적합한 방법에 의해 제조될 수 있다. 예를 들어, 폴리펩티드는 당업계에 알려진 표준 기술, 예컨대 Fmoc 고체상 화학, Boc 고체상 화학을 사용하여, 또는 용액 상 펩티드 합성에 의해 직접 합성될 수 있다. 대안적으로, 폴리펩티드는 세포, 통상적으로 박테리아 세포를, 상기 폴리펩티드를 암호화하는 핵산 분자 또는 벡터로 형질전환함으로써 제조될 수 있다. 박테리아 숙주 세포에서의 발현에 의한 폴리펩티드의 제조가 이하에 기재되어 있고, 실시예에서 예시되어 있다. 본 발명은 본 발명의 폴리펩티드를 암호화하는 핵산 분자 및 벡터를 제공한다. 본 발명은 또한 이러한 핵산 또는 벡터를 포함하는 숙주 세포를 제공한다. 본원에 기재된 폴리펩티드를 암호화하는 예시적인 폴리뉴클레오티드 분자는, 서열번호 13으로 제공된다. 이 서열은 3' 말단에서 N 말단 메티오닌(ATG)을 위한 코돈을, 그리고 5' 말단에서의 정지 코돈(TAA)에 앞서, GSGLE 링커 및 6×His 태그를 위한 코돈을 포함하며, 이들은 선택적으로 제외될 수 있다. 추가적인 메티오닌 및 태그의 선택적인 포함은 이하에서 더욱 상세히 논의된다.
용어 "핵산 분자(nucleic acid molecule)" 및 "폴리뉴클레오티드(polynucleotide)"는 본원에서 상호교환적으로 사용되며, 데옥시리보뉴클레오티드(deoxyribonucleotide) 또는 리보뉴클레오티드(ribonucleotide) 또는 이들의 유사체이든 간에, 임의의 길이의 뉴클레오티드의 중합체 형태를 지칭한다. 폴리뉴클레오티드의 비-제한적 예는 유전자, 유전자 절편, 메신저 RNA(mRNA), cDNA, 재조합 폴리뉴클레오티드, 플라스미드, 벡터, 어느 서열의 분리된 DNA, 어느 서열의 분리된 RNA, 핵산 프로브, 및 프라이머를 포함한다. 본 발명의 폴리뉴클레오티드는 본 발명의 폴리펩티드를 암호화하고, 분리된 또는 실질적으로 분리된 형태로 제공될 수 있다. 실질적으로 분리된다는 것은, 임의의 주변 매체로부터 폴리펩티드를 실질적으로 그러나 전부가 아니도록 분리될 수 있다는 것을 의미한다. 폴리뉴클레오티드는 이의 의도된 사용을 방해하지 않을 담체 또는 희석제와 혼합될 수 있고, 여전히 실질적으로 분리된 것으로 간주될 수 있다. 선택된 폴리펩티드를 "암호화하는(encode)" 핵산 서열은, 예를 들어 발현 벡터에서, 적합한 조절 서열의 조절 하에 있는 경우 생체 내에서 (DNA의 경우) 전사되고, (mRNA의 경우) 폴리펩티드로 번역되는 핵산 분자이다. 암호화 서열의 경계는 5'(아미노) 말단에서의 개시 코돈 및 3'(카르복시) 말단에서의 번역 정지 코돈에 의해 결정된다. 본 발명의 목적을 위해, 이러한 핵산 서열은, 바이러스, 원핵 또는 진핵 mRNA로부터의 cDNA, 바이러스 또는 원핵 DNA 또는 RNA로부터의 게놈 서열, 및 심지어 합성적 DNA 서열을 포함하나, 이에 제한되지 않는다. 전사 종결 서열은 암호화 서열에서 3' 쪽에서 위치할 수 있다.
폴리뉴클레오티드는 예로서 문헌[Sambrook 등 (1989, Molecular Cloning - a laboratory manual; Cold Spring Harbor Press)]에 기재된 바와 같이, 당업계에 잘 알려진 방법에 따라 합성될 수 있다. 본 발명의 핵산 분자는 삽입된 서열에 작동가능하게 연결된 조절 서열을 포함하여 본 발명의 폴리펩티드의 생체내 발현을 가능하게 하는 발현 카세트의 형태로 제공될 수 있다. 이들 발현 카세트는, 다음으로 벡터(예를 들어, 플라스미드 또는 재조합 바이러스 벡터) 내에 통상적으로 제공된다. 이러한 발현 카세트는 숙주 대상체에 직접 투여될 수 있다. 대안적으로, 본 발명의 폴리뉴클레오티드를 포함하는 벡터는 숙주 대상체에 투여될 수 있다. 바람직하게는, 폴리뉴클레오티드는 유전적 벡터를 사용하여 제조 및/또는 투여된다. 적합한 벡터는 충분한 양의 유전적 정보를 포함하여 본 발명의 폴리펩티드의 발현을 가능하게 할 수 있는 임의의 벡터일 수 있다.
본 발명은 따라서 이러한 폴리뉴클레오티드 서열들을 포함하는 발현 벡터를 포함한다. 이러한 발현 벡터는 분자 생물학 분야에서 일상적으로 제작되며, 예를 들어 플라스미드 DNA 및 적합한 개시자, 프로모터, 인핸서, 및 예컨대 필수적일 수 있고 본 발명의 펩티드의 발현을 허용하기 위해, 정확한 배향으로 위치하는 폴리아데닐화 신호와 같은 다른 요소의 사용과 관련될 수 있다. 다른 적합한 벡터는 당업계의 숙련자들에게 명백할 것이다. 이와 관련된 추가적인 예로서, 본 발명자들은 Sambrook 등에 대해 언급한다.
본 발명은 또한 본 발명의 폴리펩티드를 발현하도록 변형된 세포를 포함한다. 이러한 세포는 통상적으로 원핵 세포, 예컨대 박테리아 세포, 예를 들어 E. coli를 포함한다. 이러한 세포는 본 발명의 폴리펩티드를 제조하기 위한 통상의 방법을 사용하여 배양될 수 있다.
폴리펩티드는 유도 또는 변형되어, 이들의 제조, 분리 또는 정제에 의해 도움을 받을 수 있다. 예를 들어, 본 발명의 폴리펩티드가 박테리아 숙주 세포에서 재조합 발현에 의해 제조되는 경우, 폴리펩티드의 서열은 N 말단에 추가적인 메티오닌(M) 잔기를 포함하여, 발현을 개선시킬 수 있다. 다른 예로서, 본 발명의 폴리펩티드는 분리 수단에 직접 특이적으로 결합할 수 있는 리간드의 첨가에 의해 유도 또는 변형될 수 있다. 대안적으로, 폴리펩티드는 결합쌍의 하나의 구성원의 첨가에 의해 유도 또는 변형될 수 있고, 분리 수단은 결합쌍의 다른 구성원의 첨가에 의해 유도 또는 변형되는 시약을 포함한다. 임의의 적합한 결합쌍이 사용될 수 있다. 본 발명에 사용하기 위한 폴리펩티드가 결합쌍의 한 구성원의 첨가에 의해 유도 또는 변형된 바람직한 구현예에서, 폴리펩티드는 바람직하게 히스티딘-태그화 또는 비오틴-태그화된다. 통상적으로, 히스티딘 또는 비오틴 태그의 아미노산 암호화 서열은 유전자 수준에서 포함되고, 폴리펩티드는 E. coli에서 재조합에 의해 발현된다. 히스티딘 또는 비오틴 태그는 통상적으로 폴리펩티드의 한쪽 말단, 바람직하게 C-말단에 존재한다. 이는 폴리펩티드에 직접 연결될 수 있거나, 또는 임의의 적합한 링커 서열, 예컨대 3, 4 또는 5개 아미노산에 의해 간접적으로 연결될 수 있다. 링커는 통상적으로 대부분 글리신 및 세린 잔기로 이루어질 수 있다. 히스티딘 태그는 통상적으로 6개의 히스티딘 잔기로 이루어지나, 이보다 더 긴, 통상적으로 최대 7, 8, 9, 10 또는 20개 아미노산일 수 있거나, 또는 더 짧은, 예를 들어 5, 4, 3, 2 또는 1개 아미노산일 수 있다.
폴리펩티드는 실질적으로 분리된 또는 정제된 형태로 제공될 수 있다. 즉, 폴리펩티드가 발현된 세포 유래의 세포 추출물에 존재하는 대부분의 다른 성분으로부터 분리된다. 실질적으로 정제된다는 것은, 폴리펩티드가 적어도 50%, 60%, 70%, 80% 또는 바람직하게 적어도 90%의 균일성을 갖도록 정제되는 것으로 이해될 것이다. 순도 수준은 임의의 적합한 수단에 의해 평가될 수 있으나, 통상적으로 샘플의 SDS-PAGE 분석, 및 이후 쿠마시 블루(Coomassie Blue) 탐지와 관련된다. 폴리펩티드는 폴리펩티드의 의도된 목적을 방해하지 않을 담체, 희석제 또는 보존제와 혼합될 수 있고, 여전히 실질적으로 분리된 또는 정제된 것으로 간주될 수 있다. 폴리펩티드가 추가적인 활성 성분, 예컨대 다른 폴리펩티드를 갖는 조성물 중에 제공되는 경우, 각각의 상기 폴리펩티드는 각각의 의도된 목적에 적합한 비로 혼합되기 전에, 높은 수준의 균일성을 갖도록 개별적으로 정제될 것이다. 예를 들어, 2개의 폴리펩티드는 1:1 비로 조합되기 전에 각각 적어도 90% 균일성을 갖도록 정제될 수 있다.
폴리펩티드(또는 이들의 혼합물)는 사용에 앞서 수용액에 재구성하기에 적합한 동결건조된 형태로 제공될 수 있다. 동결 건조된 조성물은 안정성이 개선되어, 폴리펩티드의 더 긴 보관이 가능하게 된다. 폴리펩티드(또는 이들의 혼합물)를 적합한 버퍼, 예컨대 Tris-완충된 염수(TBS) 중의 동결-건조된 상기 폴리펩티드(또는 혼합물)를 포함하는 동결건조된 형태로 제조하는 방법이 본원에 제공된다. 폴리펩티드는 통상적으로 동결-건조에 앞서 실질적으로 정제된다. 생성되는 폴리펩티드(또는 혼합물)는 또한 동결 건조된 형태로도 제공된다. 폴리펩티드(또는 혼합물)의 용액을 제조하는 방법으로서, 폴리펩티드(또는 혼합물)를 동결건조된 형태로 제공하는 단계, 및 적합한 담체 또는 희석제, 예컨대 물에 의해 재구성하는 단계를 포함하는 방법도 또한 제공된다.
폴리펩티드는 예를 들어 문헌[Datta S 등, Enzyme immobilization: an overview on techniques and support materials, 3 Biotech, 3(1):1-9 (2013)]에 기재된 바와 같은 당업계에 알려진 방법을 사용하여 고정될 수 있다. 예를 들어, 폴리펩티드는 흡착, 공유 결합, 친화성 고정화 또는 포획에 의해 고정화될 수 있다. 지지체로서 사용될 수 있는 물질은 예를 들어, 천연 지지체, 예컨대 아가로스, 콜라겐, 젤라틴, 셀룰로스, 펙틴, 세파로스, 무기 물질, 예컨대 세라믹, 실리카, 유리, 활성탄 또는 숯, 또는 합성 중합체를 포함하나, 이에 제한되지 않는다. 예를 들어, 폴리펩티드는 세파로스 상에 고정될 수 있다.
시알리다제
기능적 특성들
글리칸 사슬을 변형하기 위한 화학적 및 유전적 접근법을 사용하는 이외에도, 몇몇 효소(글리코시다제)는 시알산을 다른 글리칸에 연결하는 결합에 대해 작용할 수 있다. 이들 효소[시알리다제 또는 뉴로아미니다제(neuroaminidase)로 지칭됨]는 특정 타입의 시알산 결합에 대해 고도의 특이성을 나타낸다. 3개의 분명한 결합 타입이 인간 당단백질 내에서 공통적으로 발견되는데, 알파(2-3) 결합이 우세한 형태이고, 그 다음으로 알파(2-6) 및 알파(2-8)이 따른다. 이들 결합 타입은 간략성을 위해 본원에서 2-3, 2-6 및 2-8 결합으로 지칭될 수 있다. 2-3 결합은 시알산 6탄당의 위치 번호 2에서의 탄소 원자가 산소 원자를 통해, 연결된 글리칸의 6탄당의 위치 3에서의 탄소에 연결된 것은 의미한다. 이에 따라, 2-6 결합 또는 2-8 결합은 각각 연결된 글리칸의 6탄당의 위치 6 또는 위치 8에 연결된 것을 의미한다.
가장 잘 알려진 시알리다제는 2-3 결합에 대해 특이적이거나(매우 높은 활성으로 이를 절단함), 또는 더 넓은 범위의 결합, 통상적으로 2-3, 2-6 및 2-8 결합 모두를 절단할 수 있다. 이들 상이한 타입의 시알리다제는 각각 좁은 범위의 또는 광범위의 것으로 지칭될 수 있다. 광범위한 시알리다제는 통상 2-3 결합에 대한 높은 활성을 나타내는데, 2-6에 대한 활성은 감소시키고, 2-8 결합에 대해서는 매우 낮은 활성을 갖는다. 2-8 결합을 효율적으로 절단하는 효소는 당업계에서 비교적 드물다(심지어 알려지지 않았다).
시알리다제의 효소 활성은 임의의 적합한 방법, 예컨대 실시예에서 기재된 것들에 의해 평가될 수 있다. 적합한 방법은 알려진 또는 의심되는 시알리다제를 표준 시알리다제 기질, 예컨대 2-3, 2-6 및 2-8 타입 결합을 전체적으로 포함하는 하나 이상의 소분자와 함께 항온 처리하는 단계를 포함할 수 있다. 이러한 소분자는 2-3'-시알락토스, 2-6'-시알락토스, 및 콜로민산(2-8')을 포함한다. 이러한 분자에 대한 시알리다제 활성은 유리된 시알산을 생성할 것이고, 이는 통상의 방법에 의해 정량화될 수 있다. 대안적으로, 시알리다제 활성은 기질로서 당단백질을 사용하여 평가될 수 있다. 생성되는 임의의 절단 산물은 통상의 방법, 예컨대 SDS-PAGE 또는 렉틴 블롯을 사용하여 탐지 및 정량화될 수 있다.
구조적 특징들
본 발명자들은 상업적인 장내 박테리아 아커만시아 뮤시니필라로부터 몇몇 시알리다제를 식별하고 이를 특성화하였다. 본원에서 Am0707로 지칭된 시알리다제 중 하나는, 예기치 않게도 2-8 결합에 대한 높은 활성을 갖지만, 또한 2-3 및 2-6 결합을 절단할 수도 있다. 따라서, 이는 광범위한 시알리다제라고 고려된다. 본원에서 Am1757로 지칭된 다른 시알리다제는, 배타적으로 2-3 결합에 대한 높은 활성을 갖는다. 따라서, 이는 좁은 범위의 시알리다제라고 고려된다.
제1 시알리다제(Am0707)의 전체 야생형 1차 구조(아미노산 서열)는 서열번호 1에 도시되어 있다. 신호 모티프가 제거된 서열은 서열번호 2에 도시되어 있다. 제1 시알리다제는 서열번호 2의 서열을 포함하거나, 이를 본질적으로 포함하거나 또는 이로써 이루어질 수 있으며, 통상 400개 아미노산보다 더 길다.
제2 시알리다제(Am1757)의 전체 야생형 1차 구조(아미노산 서열)는 서열번호 4에 도시되어 있다. 신호 모티프가 제거된 서열은 서열번호 5에 도시되어 있다. 제2 시알리다제는 서열번호 5의 서열을 포함하거나, 이를 본질적으로 포함하거나 또는 이로써 이루어질 수 있으며, 통상 600개 아미노산보다 더 길다.
대안적으로, 상기 제1 및/또는 상기 제2 시알리다제는 각각 이의 각각의 변형체에 의해 독립적으로 대체될 수 있고, 단 효소 활성은 유지된다. 상기 시알리다제의 변형체는 각각 서열번호 2 또는 5의 서열의 아미노산 서열을 포함하거나, 이를 본질적으로 포함하거나 또는 이로써 이루어질 수 있으며, 이는 상기 아미노산 서열에 적어도 50% 동일하다. 변형체 서열은 상기 아미노산 서열에 적어도 60%, 적어도 70%, 적어도 80%, 적어도, 85%, 적어도 90%, 적어도 95%, 적어도 98% 또는 적어도 99% 동일할 수 있다. 동일성 수준은 바람직하게 적어도 85% 이상이다. 서열에 대한 동일성은 서열의 적어도 100, 적어도 200, 적어도 300, 적어도 350, 적어도 400, 또는 적어도 500 개 또는 그 이상의 인접하는 아미노산의 부위에 대해, 또는 더욱 바람직하게는 서열의 전체 길이에 대해 측정될 수 있다. 변형체는 통상 참고 서열보다 더 길거나 또는 더 짧은 50개 이하의 아미노산 길이이며, 바람직하게는 참고 서열과 대략 (또는 정확하게) 동일한 길이의 것이다.
아미노산 동일성은 임의의 적합한 알고리즘을 사용하여 계산될 수 있다. 예를 들어, PILEUP 및 BLAST 알고리즘은 예를 들어 문헌[Altschul S. F. (1993) J Mol Evol 36:290-300; Altschul, S, F 등 (1990) J Mol Biol 215:403-10]에 기재된 바와 같이, (통상적으로 이들의 디폴트 설정 상에서) 동일성을 계산하거나 또는 서열들을 정렬하는데 사용될 수 있다(예컨대 동일 또는 상응하는 서열을 식별한다). BLAST 분석을 수행하기 위한 소프트웨어는 미국 국립생물공학정보센터(National Center for Biotechnology Information)(http://www.ncbi.nlm.nih.gov/)를 통해 공공적으로 이용가능하다. 이 알고리즘은 먼저 데이터베이스 서열에서 동일한 길이의 워드와 정렬된 경우 매치하거나 또는 일부 양의 값의 역치 점수 T를 만족하는 문의 서열(query sequence)에서 길이 W의 짧은 워드를 식별함으로써, 높은 스코어링 서열 쌍(HSP)을 식별하는 것을 포함한다. T는 이웃 워드 스코어링 역치값을 지칭한다(Altschul 등, 상기). 이들 초기의 이웃 워드 히트(word hits)는 이들을 포함하는 HSP를 찾기 위한 초기 연구를 위한 종자 역할을 한다. 워드 히트는 누적된 정렬 점수가 증가할 수 있는 만큼 각 서열을 따라 양 방향으로 확장된다. 각 방향으로의 워드 히트에 대한 확장은 이하의 경우 중단된다: 누적된 정렬 점수가 이의 최대 달성값으로부터의 값 X만큼 감소하는 경우; 누적된 점수가 하나 이상의 음의 스코어링 잔기 정렬의 축적으로 인해, 제로 또는 그 이하로 되는 경우; 또는 한쪽 서열의 말단에 도달하는 경우. BLAST 알고리즘 변수 W, T 및 X는 정렬의 민감도 및 속도를 결정한다. BLAST 프로그램은 디폴트로서, 11의 워드 길이(W), BLOSUM62 스코어링 매트릭스[Henikoff and Henikoff (1992) Proc. Natl. Acad. Sci. USA 89: 10915-10919를 참고하라], 50의 정렬(B), 10의 예측값(E), M=5, N=4, 및 양쪽 가닥의 비교를 이용한다.
BLAST 알고리즘은 2개의 서열들 간의 유사성에 대한 통계적 분석을 수행한다; 예를 들어, 문헌[Karlin and Altschul (1993) Proc. Natl. Acad. Sci. USA 90: 5873-5787]를 참고하라. BLAST 알고리즘에 의해 제공된 유사성의 한 측정은 최소 총 확률[smallest sum probability, (P(N)]인데, 이는 2개의 폴리뉴클레오티드 또는 아미노산 서열들 사이의 매치가 우연히 일어날 확률의 지표로서 제공된다. 예를 들어, 제1 서열 대 제2 서열의 비교시 최소 총 확률이 약 1 미만, 바람직하게 약 0.1 미만, 더욱 바람직하게는 약 0.01 미만, 가장 바람직하게 약 0.001 미만인 경우, 한 서열은 다른 서열에 유사한 것으로 간주된다. 대안적으로, UWGCG 패키지는 동일성을 계산하는데 사용될 수 있는 BESTFIT 프로그램(예를 들어 이의 디폴트 셋팅으로 사용됨)을 제공한다[Devereux 등 (1984) Nucleic acids Research 12, 387-395)].
시알리다제의 서열은, 변형, 예컨대 아미노산 첨가, 결실 또는 치환이 상기 서열번호의 서열에 대해 이루어지는, 각각의 서열번호의 변형체를 포함할 수 있다. 달리 기재된 바 없는 경우, 변형은 바람직하게는 보존적인 아미노산 치환이다. 보존적인 치환은 아미노산을 유사한 화학적 구조, 유사한 화학적 특성, 또는 유사한 측쇄 부피의 다른 아미노산으로 치환한다. 도입되는 아미노산은 이들이 치환하는 아미노산에 대해 유사한 극성, 친수성, 소수성, 염기성, 산성, 중성 또는 전하를 가질 수 있다. 대안적으로, 보존적인 치환은 기존의 방향족 또는 지방족 아미노산 대신에 방향족 또는 지방족인 또 다른 아미노산을 도입할 수 있다. 보존적인 아미노산 변화는 당업계에 잘 알려져 있는데, 이하의 표 A1에서 정의한 바와 같이 20개의 주요 아미노산의 특성에 따라 선택될 수 있다. 아미노산이 유사한 극성을 갖는 경우, 이는 표 A2에서 아미노산 측쇄에 대한 소수성(hydropathy) 스케일과 관련하여 결정될 수 있다. 본 발명의 시알리다제의 서열은 최대 10, 20, 30, 40, 50 또는 60 개의 보존적인 치환이 이루어진, 각각의 서열번호의 변형체를 포함할 수 있다.
표 A1 - 아미노산의 화학적 특성
표 A2 - 소수성 스케일
대안적으로, 시알리다제는 상기에서 기재된 각각의 서열번호 또는 이의 변형체의 더 짧은 절편에 의해 대체될 수 있다. 절편은 효소 활성을 갖는 상기 서열번호의 절단된 형태로 설명될 수 있다. 이러한 절편은 상응하는 서열번호보다 더 짧고, 통상적으로 적어도 100, 150, 200, 250, 300, 350, 400, 450 또는 500개 아미노산 길이이다.
본원에 기재된 임의의 시알리다제는 선택적으로 N 말단에 추가적인 메티오닌, 및/또는 C 말단에 히스티딘 또는 다른 태그를 포함할 수 있다. 이러한 추가적인 서열은 발현 및/또는 정제에 의해 도움을 받을 수 있다. 히스티딘 태그는 바람직하게는 6개의 히스티딘 잔기로 이루어진다. 히스티딘 태그는 바람직하게는 통상적으로 아미노산의 짧은 서열, 예컨대 3~5개 아미노산인 링커에 의해 C 말단에 연결된다. 링커는 통상적으로 대부분 글리신 및 세린 잔기로 이루어지며, 바람직하게 서열 GSG를 포함할 수 있다. 예를 들어 GSG 및 GSGLE는 적합한 링커이다.
따라서, 요약하면, 제1 시알리다제는 이하와 같고:
(a) 서열번호 2의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
(b) 서열번호 2의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
(c) 서열번호 2의 서열의 절편인 아미노산 서열, 또는 서열번호 2의 아미노산 서열과 85% 동일한 아미노산의 절편을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
그리고, 제2 시알리다제는 이하와 같고:
(d) 서열번호 5의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
(e) 서열번호 5의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
(f) 서열번호 5의 서열의 절편인 아미노산 서열, 또는 서열번호 5의 아미노산 서열과 85% 동일한 아미노산의 절편을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
선택적으로, 상기 제1 및/또는 상기 제2 시알리다제는 N 말단에 추가적인 메티오닌, 및/또는 C 말단에 히스티딘 태그를 포함하고, 여기에서 태그는 링커에 의해 C 말단에 연결된다.
예시적인 제 1 시알리다제는 서열번호 3의 아미노산 서열로 이루어지는 폴리펩티드이다. 예시적인 제 2 시알리다제는 서열번호 6의 아미노산 서열로 이루어지는 폴리펩티드이다.
시알리다제 조성물
시알리다제 조성물은 바람직하게 실질적으로 분리된 또는 정제된 형태의 적어도 하나의 시알리다제를 포함한다. 상기 제시된 폴리펩티드와 관련된 전체적인 기재 내에서와 같이, 이것은 통상 시알리다제가 발현된 세포로부터의 세포 추출물 중에 존재하는 다른 대부분의 성분들로부터 분리된 것을 의미한다. 실질적으로 정제된다는 것은, 시알리다제가 적어도 50%, 60%, 70%, 80% 또는 바람직하게 적어도 90% 균일성을 갖도록 정제된다고 이해될 것이다. 순도 수준은 임의의 적합한 수단에 의해 평가될 수 있으나, 통상적으로 샘플의 SDS-PAGE 분석, 및 이후 쿠마시 블루 탐지를 포함한다. 시알리다제는 시알리다제의 의도된 목적을 방해하지 않을 담체, 희석제 또는 방부제와 혼합될 수 있고, 여전히 실질적으로 분리된 또는 정제된 것으로 간주될 수 있다. 시알리다제 조성물은 추가적인 활성 성분, 예컨대 다른 시알리다제 또는 다른 효소를 포함할 수 있는데, 이 경우 상기 각 성분은 각각의 의도된 목적에 적합한 비로 혼합되기 전에 높은 수준의 균일성을 갖도록 개별적으로 정제될 것이다. 본 발명의 바람직한 시알리다제 조성물에서, 조성물은 제1 시알리다제 및 제2 시알리다제를 포함하는데, 이들은 각각 적어도 90% 균일성을 갖도록 정제되고, 서로 1:1 비로 존재한다. 이러한 조성물은 추가적인 활성 성분, 예컨대 시알리다제가 아닌 다른 효소를 포함할 수 있다. 또 다른 효소는 프로테아제 및/또는 글리코시다제일 수 있다. 프로테아제는 바람직하게 O-당단백질-특이적인 엔도프로테아제이다. 글리코시다제는 바람직하게 O-글리코시다제이다. 두 타입의 효소는 이하에서 더욱 상세히 논의된다.
시알리다제 조성물이 시알리다제가 아닌 활성 성분을 포함하는 경우, 다른 효소에 대한 총 시알리다제 함량 (예를 들어 제1 플러스 제2 시알리다제)의 바람직한 비는 1:1일 것이다. 예를 들어, 조성물이 2000 단위의 또 다른 효소를 포함하는 경우, 이는 또한 2000 단위의 시알리다제를 포함할 것이고, 여기에서 2개의 시알리다제가 있는 경우, 이후 상기 2000 단위는 1000 단위의 제1 시알리다제와 1000 단위의 제2 시알리다제를 포함한다.
시알리다제 조성물(일반적으로 폴리펩티드와 같은)은 사용 전에 수용액 중에서 재구성되기에 적합한 동결건조된 형태로 제공될 수 있다. 동결 건조된 조성물은 안정성을 개선시켜, 시알리다제(들)의 더 긴 보관이 가능하게 한다. 동결 건조된 형태의 시알리다제 조성물(적합한 버퍼, 예컨대 Tris-완충된 염수(TBS) 중의 동결-건조한 하나 이상의 시알리다제를 포함)을 제공하는 방법이 본원에 제공된다. 버퍼는 바람직하게 저농도, 통상적으로 최대 300 mM, 250 mM, 200 mM, 또는 150 mM의 NaCl를 포함한다. NaCl 농도는 바람직하게 약 150 mM, 예컨대 125 mM 내지 175 mM이다. 시알리다제는 통상 동결-건조되기 전에 실질적으로 정제된다. 생성되는 조성물의 동결 건조된 형태도 또한 제공된다. 용액인 시알리다제 조성물을 제조하는 방법도 또한 제공되는데, 이는 조성물을 동결건조된 형태로 제공하는 단계, 및 적합한 담체 또는 희석제, 예컨대 물로 재구성하는 단계를 포함한다.
본 발명자들은 제1 시알리다제가 2-8 결합에 대해 비정상적으로 높은 활성을 갖는다고 결정하였다. 따라서, 본 발명은 이하의 것들로부터 독립적으로 선택된 제1 시알리다제를 포함하는 조성물을 제공하되:
(a) 서열번호 2의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
(b) 서열번호 2의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
(c) 서열번호 2의 서열의 절편인 아미노산 서열, 또는 서열번호 2의 아미노산 서열과 85% 동일한 아미노산의 절편을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
선택적으로, 상기 제1 시알리다제는 N 말단에 추가적인 메티오닌, 및/또는 C 말단에 히스티딘 태그를 포함하고, 여기에서 태그는 링커에 의해 C 말단에 연결될 수 있다.
상기 조성물은 2-8 시알산 결합을, 바람직하게는 높은 효율성으로 절단하는 방법에 사용하기 위한 것이다. 이러한 조성물의 예는 서열번호 3의 아미노산 서열로 이루어지는 시알리다제를 포함한다.
본 발명자들은 또한 제1 시알리다제(Am0707) 및 제2 시알리다제(Am1757)의 조합이 2-3, 2-6, 및 2-8 결합을 비정상적으로 높은 효율성으로 가수분해함으로서, 임의의 당단백질의 실질적으로 모든(통상적으로 > 90%의) 시알산의 효율적인 제거를 허용한다고 결정하였다. 조합은 또한 놀랍게도 천연의 (즉, 비-변성된) 상태의 당단백질에 대해 효과적이었다. 따라서, 본 발명은 제1 시알리다제를 포함하는 상기 기재된 조성물을 제공하는데, 이 조성물은 이하의 것들로부터 독립적으로 선택되는 제2 시알리다제를 추가로 포함한다:
(d) 서열번호 5의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
(e) 서열번호 5의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
(f) 서열번호 5의 서열의 절편인 아미노산 서열, 또는 서열번호 5의 아미노산 서열과 85% 동일한 아미노산의 절편을 포함하거나 또는 이로써 이루어지는 폴리펩티드.
선택적으로, 상기 제2 시알리다제는 N 말단에 추가적인 메티오닌, 및/또는 C 말단에 히스티딘 태그를 포함하고, 여기에서 태그는 링커에 의해 C 말단에 연결될 수 있다. 제1 및 제2 시알리다제는 바람직하게 서로에 대해 1:1 비로 존재할 수 있다.
상기 조성물은 당단백질에서 시알산을 완전히 제거하거나, 또는 당단백질 상의 시알산 결합의 >90%를, 바람직하게 높은 효율로 절단하는 방법에서 사용하기 위한 것일 수 있다. 당단백질은 바람직하게는 천연의 상태이다. 즉, 임의의 형태의 변성화 상태로 만들지 않았다.
본 발명의 시알리다제 조성물의 예는 서열번호 3의 아미노산 서열로 이루어지는 시알리다제, 및 서열번호 6의 아미노산 서열로 이루어지는 시알리다제를, 바람직하게는 1:1 비로 포함한다.
시알리다제 조성물의 시알리다제 활성은 개별적인 시알리다제에 대해 상기 기재된 바와 동일한 방법을 사용하여 평가될 수 있다. 그러나 이는 바람직하게 기질로서 비-변성된 당단백질을 사용하여 평가된다. 결과는 기질이 예시적인 시알리다제 또는 이들의 혼합물, 예컨대 서열번호 3의 아미노산 서열로 이루어지는 폴리펩티드와 서열번호 6의 아미노산 서열로 이루어지는 폴리펩티드의 1:1 혼합물과 접촉되는 경우, 동일한 분석 시험에 의해 얻은 것들과 비교될 수 있다. 이러한 시알리다제 혼합물의 단위는 통상적으로 SDS-PAGE에 의해 모니터링될 때, 20 mM Tris pH 6.8 중에, 37℃에서 2시간 동안 항온 처리되는 경우, 1 ㎍ 당단백질(페투인)의 ≥90%로부터 시알산을 가수분해하는데 요구되는 양이다. 이것은 고효율을 나타낸다고 간주된다.
O-글리코시다제
본 발명자들은 또한 포유동물의 성도(oral tract)에 서식하는 공생 박테리아 스트렙토코커스 오랄리스(Streptococcus oralis)로부터의 O-글리코시다제를 식별하고 이를 특성화하였는데, 이는 특히 상기 기재된 시알리다제 조성물과의 조합으로 사용되는 경우, O-연결된 글리칸을 효율적으로 가수분해한다. O-글리코시다제는 본원에서 "O-glyk" 또는 "So"로 지칭될 수 있다. O-glyk의 야생형 서열은 서열번호 7로서 제공되는데, 이는 신호 서열 및 LPTXG 세포벽 앵커 모티프를 포함한다. 신호 서열이 결여된 O-glyk의 야생형 서열은, 서열번호 8로서 제공된다. 신호 서열 및 세포 벽 앵커 모티프의 C 말단 부위가 결여된 O-glyk의 야생형 서열은, 서열번호 9로서 제공된다. 이들 서열은 선택적으로 N 말단에 추가적인 메티오닌, 및/또는 C 말단에 히스티딘 또는 다른 태그를 포함하도록 변형될 수 있다. 이러한 추가적인 서열은 (예를 들어 E. coli에서) 발현 및/또는 정제에 의해 도움을 받을 수 있다. 히스티딘 태그는 바람직하게 6개의 히스티딘 잔기로 이루어진다. 히스티딘 태그는 바람직하게 통상적으로 아미노산의 짧은 서열, 예컨대 3~5개 아미노산인 링커에 의해 C 말단에 연결된다. 링커는 통상적으로 대부분 글리신 및 세린 잔기로 이루어지며, 바람직하게는 서열 GSG를 포함할 수 있다. 예를 들어, GSG 및 GSGLE는 적합한 링커이다. N 말단에 추가적인 메티오닌 및 C 말단에 GSGLE 링커 및 His6 태그를 갖는 예시적인 O-glyk 서열은, 서열번호 10으로서 제공된다. 본 기재 내용에서 "O-glyk" 또는 "So"에 대한 임의의 언급은 서열번호 7, 8, 9 또는 10 중 어느 것을 의미할 수 있으나, 바람직하게 서열번호 9의 아미노산 서열을 포함하거나 또는 이로써 이루어지며, 통상 2070개 아미노산 이하인 폴리펩티드를 지칭한다. 서열번호 10의 아미노산 서열로 이루어지는 폴리펩티드가 가장 바람직하다.
본 발명자들은 또한 상기 기재된 바와 같은 시알리다제 조성물의 작용이 또한 다른 O-글리코시다제의 활성을 강화시킨다는 것을 발견하였다. 따라서, 본 발명은 또한 당단백질을 변경시키는 방법을 제공하는데, 당단백질의 샘플을 상기 기재된 바와 같은 시알리다제 조성물 및 O-글리코시다제 모두와 접촉시키는 단계를 포함한다. 본 발명은 선택적으로 또한 O-글리코시다제를 포함하는, 상기 기재된 시알리다제 조성물도 또한 제공한다. 상기 방법 및 상기 조성물에서, 상기 O-글리코시다제는 서열번호 9의 아미노산 서열을 포함하거나 또는 이로써 이루어질 수 있거나, 또는 예컨대 장내 박테리아, 예를 들어 엔테로코커스 패칼리스(Enterococcus faecalis)로부터 얻은 효소와 같은 임의의 다른 O-글리코시다제일 수 있다. E. 패칼리스(faecalis)로부터의 바람직한 O-글리코시다제는 Uniprot 엔트리 B5UB72 버전 22의 아미노산 서열을 갖는 폴리펩티드이다. 다른 적합한 O-글리코시다제는 WO2009129086에 기재된 것들, 특히 WO2009129086의 페이지 7에 기재되고 도 5에 도시된 EngEF, EngPA 및 절단된 EngAA를 포함한다.
본원의 기재 내용 중 어느 것에서, 서열번호 9의 서열을 포함하는 O-글리코시다제는 이의 변형체에 의해 대체될 수 있는데, 단 효소 활성은 유지된다. O-글리코시다제의 변형체는 서열번호 9의 서열의 아미노산 서열의 변형체를 포함하거나, 이를 본질적으로 포함하거나, 또는 이로써 이루어질 수 있다. 상기 서열번호의 변형체는 유지될 관련 효소 활성이 O-글리칸에 대한 가수분해 활성인 점을 제외하고는, 시알리다제에 대하여 상기 제시된 바와 같이 정의될 수 있다.
대안적으로, O-글리코시다제는 서열번호 9 또는 상기 기재된 이의 변형체의 더 짧은 절편에 의해 대체될 수 있다. 절편은 효소 활성이 유지되는 상기 서열번호의 절단된 형태로서 기재될 수 있다. 이러한 절편은 서열번호 3보다 더 짧고, 통상적으로 적어도 300, 400, 500, 600, 800, 1000, 1200, 1300, 1400 또는 1500개 아미노산 길이이다.
본원에 기재된 임의의 O-글리코시다제는 선택적으로 N 말단에 추가적인 메티오닌, 및/또는 C 말단에 히스티딘 또는 다른 태그를 포함할 수 있다. 이러한 추가적인 서열은 발현 및/또는 정제에 의해 도움을 받을 수 있다. 히스티딘 태그는 바람직하게는 6개의 히스티딘 잔기로 이루어진다. 히스티딘 태그는 바람직하게 통상 아미노산의 짧은 서열, 예컨대 3~5개 아미노산인 링커에 의해 C 말단에 연결된다. 링커는 통상적으로 대부분 글리신 및 세린 잔기로 이루어지는데, 바람직하게 서열 GSG를 포함할 수 있다. 예를 들어, GSG 및 GSGLE는 적합한 링커이다. 이 타입의 예시적인 O-글리코시다제는 서열번호 10의 아미노산 서열로 이루어진다.
O-글리코시다제의 효소 활성은 임의의 적합한 방법, 예컨대 실시예에 기재된 것들에 의해 평가될 수 있다. 적합한 방법은 알려진 또는 의심되는 O-글리코시다제를 표준 기질, 예컨대 전체적으로 O-글리칸 코어 부위를 포함하는 하나 이상의 소분자와 함께 항온 처리하는 단계를 포함할 수 있다. 이러한 소분자는 4-메틸움벨리페론(4MU) 기질 및 pNP-기질을 포함하는데, pNP의 방출은 활성을 나타낸다. 대안적으로, 활성은 기질로서 당단백질을 사용하여 평가될 수 있다. 임의의 생성되는 절단 산물은 통상의 방법, 예컨대 SDS-PAGE 또는 렉틴 블롯을 사용하여 탐지 및 정량화될 수 있다. 당단백질이 기질로서 사용되는 경우, 상기 기재된 바와 같은 시알리다제 조성물에 의한 사전-처리 (또는 동시 처리)가 요구될 수 있다. 그 결과는 기질이 예시적인 O-글리코시다제, 예컨대 산성의 서열번호 10의 서열로 이루어지는 폴리펩티드와 접촉하는 경우, 동일한 분석 시험에서 얻은 것들과 비교될 수 있다. 서열번호 10의 폴리펩티드의 1 단위는 SDS-PAGE에 의해 모니터링될 때 2시간 내에 37℃에서, 20 mM Tris 버퍼 pH 6.8 중의 1 단위의 시알리다제 혼합물과 조합하여, 1 ㎍의 TNFaR의 > 90%로부터 O-글리칸을 제거하는데 요구되는 양으로 정의된다(바람직한 시알리다제 혼합물은 상기에서 기재된 바와 같다). 시험 폴리펩티드는 바람직하게는 동일한 양으로 존재하는 경우 유사한 수준의 활성을 달성한다. 예시적인 분석 시험은 또한 실시예에서 기재된다.
상기 기재된 바와 같이 O-글리코시다제를 포함하는 조성물은 용액 중에 제공되거나, 또는 용액에서 재구성하기 위해 동결건조된 형태로 제공될 수 있다. O-글리코시다제는 Tris 버퍼 염수 pH 7.6 중에서 동결 건조될 수 있다.
O-글리칸 특이적인 엔도프로테아제
본 발명자들은 또한 상기 기재된 시알리다제 조성물의 작용이 O-글리칸 특이적인 엔도프로테아제, 특히 통상 375개 이하의 아미노산이고, 바람직하게는 서열번호 12의 아미노산 서열로 이루어지는 폴리펩티드인, 서열번호 11의 아미노산 서열을 포함하는 O-글리칸 특이적인 엔도프로테아제의 활성을 강화시키는 것을 발견하였다.
따라서, 본 발명은 또한 당단백질을 변형시키는 방법을 제공하는데, 이는 당단백질의 샘플을 상기 기재된 바와 같은 시알리다제 조성물 및 O-글리칸 특이적인 엔도프로테아제 둘 다와 접촉시키는 단계를 포함한다. 본 발명은 선택적으로 또한 O-글리칸 특이적인 엔도프로테아제를 포함하는, 상기 기재된 시알리다제 조성물을 또한 제공한다. 상기 방법 및 상기 조성물에서, 상기 O-글리칸 특이적인 엔도프로테아제는 서열번호 12로 된 것일 수 있다.
본원의 기재 내용 중 어느 것에서, 서열번호 11의 O-글리칸 특이적인 엔도프로테아제는 이의 변형체에 의해 대체될 수 있고, 단 효소 활성은 유지된다. 엔도프로테아제의 변형체는 서열번호 11의 서열의 아미노산 서열의 변형체를 포함하거나, 이를 본질적으로 포함하거나, 또는 이로써 이루어질 수 있다. 상기 서열번호의 변형체는 보유될 관련 효소 활성이 O-당단백질에 대한 가수분해 활성인 경우를 제외하고는, 시알리다제에 대해 상기 제시된 바와 같이 정의될 수 있다.
대안적으로, 엔도프로테아제는 서열번호 3 또는 상기 기재된 이의 변형체의 더 짧은 절편에 의해 대체될 수 있다. 절편은 효소 활성을 유지하는 상기 서열번호의 절단된 형태로서 설명될 수 있다. 이러한 절편은 서열번호 11보다 더 짧고, 통상적으로 적어도 100, 150, 200, 250, 300, 350, 400, 450 또는 500개 아미노산 길이이다.
본원에 기재된 임의의 엔도프로테아제는 선택적으로 N 말단에 추가적인 메티오닌 및/또는 C 말단에 히스티딘 또는 다른 태그를 포함할 수 있다. 이러한 추가적인 서열은 발현 및/또는 정제에 의해 도움을 받을 수 있다. 히스티딘 태그는 바람직하게 6개의 히스티딘 잔기로 이루어진다. 히스티딘 태그는 바람직하게는 통상적으로 짧은 서열의 아미노산, 예컨대 3~5개의 아미노산인 링커에 의해 C 말단에 연결된다. 링커는 통상적으로 대부분 글리신 및 세린 잔기로 이루어지고, 바람직하게는 서열 GSG를 포함할 수 있다. 예를 들어, GSG 및 GSGLE는 적합한 링커이다. 이 타입의 예시적인 엔도프로테아제는 서열번호 12의 아미노산 서열로 이루어진다.
엔도프로테아제의 효소 활성은 임의의 적합한 분석 시험에 의해 평가될 수 있다. 예를 들어, 표준 O-당단백질 기질, 예컨대 IgA 분자는, 시험 폴리펩티드와 함께 항온 처리될 수 있다. 개시 물질 및 반응 산물은 이후 SDS-PAGE 및/또는 질량 분광분석법에 의해 분석되어, 절단된 산물 (존재하는 경우)의 존재를 결정하고, 필요한 경우 이들 산물도 또한 추가로 특성화할 수 있다. O-당화되지 않은 당단백질 기질, 예컨대 IgG1 분자는, 음성 대조군으로서 사용될 수 있다. 결과는 기질이 예시적인 폴리펩티드, 예컨대 서열번호 12의 아미노산 서열로 이루어지는 폴리펩티드와 접촉하는 경우, 동일한 분석 시험으로 얻어질 수 있는 것과 비교될 수 있다.
상기 기재된 바와 같은 O-글리칸 특이적인 엔도프로테아제를 포함하는 조성물은 용액으로, 또는 용액 중에서 재구성하기 위해 동결 건조된 형태로 제공될 수 있다. O-글리칸 특이적인 엔도프로테아제는 Tris 버퍼 염수 pH 7.6 중에 동결 건조될 수 있다.
사용 방법
본 발명은 샘플이 상기 조성물 중의 효소에 적합한 조건 하에서 본 발명의 조성물과 함께 항온 처리되어, 존재하는 임의의 기질에 대해 작용하는 임의의 방법을 제공한다. 상기 방법은 선택적으로는 생성되는 산물의 분석을 포함할 수 있다. 상기 분석은 SDS-PAGE, HPLC, 렉틴 블로팅, ELISA 또는 질량 분광분석법을 포함하는 어느 적합한 수단에 의해 산물을 분리 및/또는 탐지 및/또는 단리하는 것을 포함할 수 있다.
적합한 조건은 적어도 20분, 30분, 40분, 50분, 60분, 70분, 80분, 90분 또는 120분, 3시간, 5시간, 10시간, 12시간 동안, 또는 밤새 본 발명의 조성물과 함께 항온 처리하는 것을 포함한다. 항온 처리는 바람직하게 실온에서, 더욱 바람직하게는 대략 20℃, 25℃, 30℃, 35℃, 40℃ 또는 45℃에서, 가장 바람직하게는 대략 37℃에서 일어난다. 방법은 임의의 적합한 pH 하에 실시될 수 있다. 적합한 pH 값은 예를 들어, 약 3.0, 3.5, 4, 4.5, 5, 5.5, 6, 6.5, 7, 7.5, 8, 8.5, 9 또는 9.5의 pH를 포함한다. 바람직한 pH는 5.6 내지 6.8의 범위에 있다. 방법은 임의의 적합한 버퍼, 예컨대 tris 완충된 염수 (TBS) 또는 인산 완충된 염수 (PBS)에서 실시될 수 있다. 버퍼는 바람직하게 통상 300 mM, 250 mM, 200 mM, 또는 150 mM 이하의 저농도의 NaCl을 포함한다. NaCl 농도는 바람직하게 약 150 mM, 예컨대 125 내지 175 mM이다. 본 발명의 조성물 중의 효소 대 샘플 내의 단백질 함량의 대략적인 비는, 1:1, 2:1, 4:1, 6:1, 10:1, 15:1, 20:1, 1:2, 1:4, 또는 1:6, 1:10, 1:15, 1:20, 1:40, 1:50 또는 1:100일 수 있다.
이하는 본 발명의 특히 바람직한 방법이다:
당단백질을 변형시키는 방법으로서, 상기 방법은 당단백질을 함유하는 샘플을 본 발명의 조성물과 접촉시키는 단계, 및 선택적으로 생성되는 산물을 분석하는 단계를 포함한다. 상기 분석은 SDS-PAGE, HPLC, 렉틴 블로팅, ELISA 또는 질량 분광분석법을 포함하는 임의의 적합한 방법에 의해 산물을 분리 및/또는 탐지 및/또는 단리하는 단계를 포함한다.
특정 구현예에서, 방법은 샘플을 단지 시알리다제만을 포함하는 본 발명의 조성물과 접촉시키는 단계, 선택적으로 산물을 분리시키는 단계, 및 이후 상기 산물을 또 다른 효소, 예컨대 프로테아제 및/또는 글리코시다제와 접촉시키는 단계를 포함할 수 있다. 이 방법은 다른 효소가 첨가되기 전에 시알산을 제거하기 위한 샘플의 "사전-처리(pre-treatment)"로서 설명될 수 있다. 이 구현예의 변형예에서, 다른 효소는 샘플에 별도로 그러나 시알리다제 조성물과 동시에 첨가될 수 있으며, "병용-처리"로 설명될 수 있다. 다른 변형예에서는, 또 다른 효소는 시알리다제 조성물 중에 존재한다. 또 다른 효소는 바람직하게 예를 들어 본원에서 기재한 바와 같은, O-글리칸 특이적인 엔도프로테아제 또는 O-글리코시다제이다.
이하의 실시예는 본 발명을 예시한다:
실시예 1 - 시알리다제
재료 및 방법
시알리다제의 발현 및 정제
아커만시아 뮤시니필라에서 식별된 유전자(Am0705, Am0707, Am1757, Am2058)는, E. coli에서 벡터 pET21a(+)에서 잘 발현되도록 코돈-최적화되었다. 벡터는 BL21(DE3) Star 세포에 형질전환되었다. E. coli는 37℃에서, 200 rpm으로 통상 LB 중에 배양되었다. 플라스미드의 존재 하에, 100 ㎍/㎖ 암피실린을 첨가하였다. 밤새 항온 처리한 이후, 배양액을 신선한 LB(amp) 중에 1:20으로 희석하고, OD620 ~ 0.7-0.8이 될 때까지 생장시킨 후, 1 mM IPTG의 첨가에 의해 재조합 단백질 발현을 유도하고, 세포를 모아서 동결시키기 전에 발현을 5시간 동안 지속하였다. 동결된 세포를 해동하고, His 결합 버퍼(20 mM NaP pH 7.4, 500 mM NaCl, 20 mM 이미다졸)에 재용해하고, 세포 내 단백질의 방출을 위해 초음파 처리하였다. 세포 잔여물을 원심분리에 의해 제거하였다. 멸균 여과된 상청액을 니켈 컬럼 상에서 친화성 정제하고, PD-25 컬럼 상에서 20 mM Tris-HCl pH 8.0로 재-완충화하였다. 단백질의 농도를 나노드롭을 사용하여 결정하고, 순도를 SDS-PAGE를 통하여 추정하였다.
소분자를 사용한 활성 평가
2-3'-시알락토스, 2-6'-시알락토스, 및 콜로민산(2-8'; Sigma-Aldrich)을 효소의 가수분해 특이성을 결정하기 위한 기질로서 사용하였다. 효소(0.05 ㎍)를 20 mM Tris-HCl pH 6.8 중의 기질(25 μM)과 혼합하고, 30분 동안 37℃에서 항온 처리한 후, 혼합물 중의 유리된 시알산을, 제조자의 지침(시알산 정량화 킷트, Abcam)에 따라서 정량화하였다.
단백질 기질을 사용한 활성 평가
TNFαR, EPO, 엔브렐 및 페투인(0.5 ㎍)을 가변 농도의 시험된 시알리다제 (1:40) 또는 상업적인 시알리다제(NEB 사, 제조사에 따라서)와 혼합하고, 30분 동안 항온 처리한 후, 단백질을 4-20% Novex 구배 SDS-PAGE 상에서 분리하고, 및/또는 SNA 렉틴 블롯으로 분석하였다.
렉틴 블롯
분리된 단백질은 Trans-Blot Turbo Transfer System(BioRad)을 사용하여 PVDF 막으로 전달되었다. 막은 렉틴 버퍼로 블로킹된 후, 이어서 제1 결합자(SNA-비오틴) 및 제2 결합자(HRP-스트렙타비딘; VectorLabs)와 함께 항온 처리되고, 그 사이에 세척 단계를 두었다. 화학-형광(Chemi-luminescense)은 West Pico SuperSignal(ThermoFisher) 킷트에 의해 발생되었고, ChemiDoc(BioRad)에서 탐지되었다.
최적 효소 조건
시알리다제는 20 mM Tris-HCl pH 8.0 중에서 2-3' 시알락토스(25 μM)와 함께 항온 처리되어, NaCl(0-1.5 M) 및 이온(2 mM CaCl2, 2 mM ZnCl2, 5 mM EDTA)의 영향을 조사하였다. pH 최적화를 위해, 시알리다제는 아세트산 버퍼(4.6 및 5.6), 및 Tris-HCl 버퍼(6.8, 7.4, 8.0, 및 8.8)에서 항온 처리되었다. 모든 샘플은 15 분 동안 실온에서 항온 처리한 후, 혼합물을 제조자의 지침에 따라서 시알산 정량화 킷트(Abcam)에 1:1로 첨가하였다. 모든 값은 각 그룹 내의 최고 활성에 대한 상대적 활성으로 표현되었다.
기존 생물공학 회사로부터의 알려진 시알리다제와의 비교
A. 뮤시니필라 시알리다제, 시알리다제 혼합물, 및 기존 브랜드(NEB P0743S, P0720S, 및 P0722S)로부터 구입한 시알리다제를 제조자의 지침에 따라서 시알산 정량화 버퍼 및 이들의 각각의 최적 버퍼 중에서 2-3' 및 2-6' 시알-락토스, 및 콜로민산과 함께 (1:1 비로) 20분 동안 항온 처리하였다.
결과
모든 A. 뮤시니필라 시알리다제는 잘 발현되고, His-컬럼에서 정제될 수 있다.
아커만시아 주석이 달린 시알리다제 Am0705, Am0707, Am1758, 및 Am2058은 E. coli에서 재조합에 의해 발현되고, His-컬럼 상에서 고순도로 정제되었다(도 1). 단백질은 잘 발현되고, 그 수준은 E. coli 배양액 1ℓ당 70-150 mg의 정제된 효소로 변화한다. 또한, 시알리다제는 Tris 버퍼 중에 잘 용해되며, 유의한 침전 없이 > 3 mg/㎖로 농축될 수 있다.
시알리다제 중 단지 3개만이 다양한 단백질 기질에 대한 활성을 나타낸다.
상이한 O- 및 N-연결된 당단백질에 대한 정제된 시알리다제의 초기 스크리닝 동안, Am0705을 제외한 모든 시알리다제는 강력한 활성을 나타내었다(데이터 미도시). Am2058의 일관성 없는 활성 때문에, 본 발명자들은 Am0707 및 Am0707/1757의 혼합물(혼합물, 1:1)의 특성화를 계속하였다.
시알리다제는 상이한 특이성을 갖는다.
몇몇 시알리다제는 특정 시알산 결합(예를 들어 2-3, 2-6, 및/또는 2-8)을 가수분해하는 제한된 능력을 갖는 결합 특이성을 나타내었다. 상이한 결합에 대해 4종의 A. 뮤시니필라 시알리다제가 작용하는 능력을 조사하기 위하여, 본 발명자들은 단지 존재하는 결합의 타입들(2-3'-시알락토스, 2-6'-시알락토스, 및 콜로민산) 중 하나만을 갖는 특이적인 기질과 함께 시알리다제를 항온 처리하고, 유리된 시알산을 정량화하였다(도 2). Am1757은 2-3 결합에 대한 높은 특이적인 활성을 갖지만, Am0707은 모든 시험된 결합에 대해 더 낮기는 하지만 더 넓은 활성을 갖는다. Am0707 및 Am1757의 조합(혼합물)은, 더 나은 광범위한 산물을 생성하였다(도 2).
시알리다제는 NaCl 민감성이며, 2가 양이온에 의존한다.
시알리다제 활성을 최적화하는데 필요한 조건을 추가로 조사하기 위하여, 본 발명자들은 시알리다제에 대하여 이온, pH, 및 NaCl에 대한 의존성을 조사하였다. 2개의 시알리다제는 유사하게 거동하는데, EDTA 및 Zn2+에 대한 높은 민감성을 갖지만 Ca2+에는 의존하였다. 효소는 중성 내지 염기성 pH에서 더 높은 활성을 갖고, NaCl의 존재 하에서는 이들 활성의 대부분을 상실하였다(도 3).
시알리다제의 혼합물은 가수분해의 전체 효율을 증가시킨다
특성화된 시알리다제가 높은 2-3 결합 가수분해 활성을 갖는 Am1757, 및 2-6,8 결합에 대해 또한 작용하는 Am0707에 대해 보완적인 활성을 갖기 때문에, 본 발명자들은 2개의 효소의 혼합물이 2개의 효소의 비를 변화시킴으로써, 천연의 당단백질 상의 모든 시알산 결합에 대한 높은 효율성을 입증할 수 있는지를 조사하였다. Am0707과 함께(1:40) Am1757을 1:40 함유하는 혼합물은 신속하게(<15 분) 페투인 상의 모든 시알산 결합을 가수분해하였다(도 4).
소분자 기질에 대한 시알리다제의 벤치마킹
단일 효소, 뿐만 아니라 브랜드 경쟁자에 대한 시알리다제 혼합물(GVS_Smix)의 효율성을 비교하기 위하여, 본 발명자들은 본 발명의 효소를 New England Biolabs(NEB) 사로부터의 3종의 시판되는 시알리다제과와 비교하였다. 이들은 아르트로박터 우레아파시엔스(Arthrobacter ureafaciens) 유래의 광범위한 시알리다제[NEB A, 아르트로박터 우레아파시엔스 유래의 효소 α2-3,6,8,9 뉴로아미니다제A(카탈로그 # P0722S)는 2-3, 2-6, 2-8, 및 2-9 결합을 절단한다], 스트렙토코커스 뉴모니애(Streptococcus pneumoniae) 유래의 좁은 범위의 시알리다제[NEB S, 스트렙토코커스 뉴모니애 유래의 효소 α2-3 뉴로아미니다제 S(카탈로그 # P0743S)는 단지 2-3 결합만을 절단한다], 및 클로스트리디움 퍼프린겐스(Clostridium perfringens) 유래의 일반적인 시알리다제[NEB O, 클로스트리디움 퍼프린겐스로부터의 효소 α2-3,6,8 뉴로아미니다제 O(카탈로그 # P0720S)는 2-3, 2-6, 2-8 결합을 절단한다]이다. 효소는 제조자가 추천한 바와 같이 첨가되었고, 30분 동안 37℃에서 기질과 함께 항온 처리되었다(도 5).
SDS-PAGE로 판단해보면, 상이한 샘플 내의 시알리다제의 양은 NEB에서보다 GVS_Smix에서 더 낮았고, 가능하게는 뉴로아미니다제 A는 예외이다. 뉴로아미니다제 S는 당단백질 상의 모든 시알산 결합을 가수분해할 수 있는 제한된 능력을 보여주는 반면, 뉴로아미니다제 A 및 뉴로아미니다제 O는 페투인 상에 존재하는 모든 시알산을 가수분해하였다(도 6). 마찬가지로, 합성된 소분자 기질에 대한 활성에 대하여 관찰된 바와 같이, Smix는 당단백질에서 모든 시알산 결합을 가수분해하여, 좁은 단백질 밴드를 생성하는데, 이는 완전한 시알산 제거의 지표이다. Am1757 처리된 샘플(2-6 또는 2-8 결합을 가수분해할 수 없음)은 Smix로 처리된 샘플들보다 더 높은 분자량으로 이동하였다. 가수 분해는 SNA 블로팅, 시알산 표지에 의해 확인되었고, 이는 모든 광범위한 시알리다제가 페투인 상에 존재하는 모든 시알산을 효율적으로 제거한 반면, 단지 2-3 특이적인 효소(예를 들어 뉴로아미니다제 S 및 Am1757)만이 시알산의 분획을 제거한다는 것을 암시한다(도 6).
Smix는 천연의 단백질로부터 시알산을 효율적으로 방출시킬 수 있다.
Smix가 NEB 산물과 유사하거나 또는 이보다 나은 효율로 작은 반-합성 기질에 작용할 수 있기는 하지만(도 5), 상이한 시알산 결합을 갖는 천연의 단백질에 대한 이의 활성을 조사하는 것도 시급했다. 모델 단백질로서, 페투인이 선택되었는데, 이는 2-3 및 2-6 결합된 시알산을 모두 갖기 때문이다. SNA 블로팅을 사용하여, 선택된 농도의 Smix가 NEB A 및 O와 유사하게, 페투인으로부터 모든 시알산을 완전히 제거할 수 있다는 것이 명백해졌다(도 6). 2개의 2-3 특이적인 효소 Am1757 및 NEB S는, 기대한 바와 같이, 페투인에서 완전히 시알산을 제거할 수 없었다.
3종의 NEB 시알리다제의 비교시, Smix 및 Am1757이 천연의 단백질 유래의 시알산을 방출하는 능력을 더욱 정량적으로 결정하기 위하여, 본 발명자들은 상이한 당단백질 기질(TNFaR, IgA, 플라스미노겐 및 아바타셉트(Abatacept)[Orencia])를 각각 시알리다제와 함께 15 + 15 분 동안 항온 처리하였고, 방출된 시알산을 정량화하였다. 특정 기질이 다른 것들보다 가수분해하기가 더 어렵다고 판명된 반면, GVS_Smix는 모든 경우에 NEB 산물과 적어도 필적할만하고(도 7), 이것이 모든 기질에 대해 높은 활성을 갖는 점에서 가장 일관성을 나타내었다. Am1757의 개별적인 효소 및 각각의 NEB 산물이 하나 또는 다른 개별적인 기질에 대해 더 높은 활성을 갖기는 하지만, 단지 GVS_Smix만이 모든 기질에 대해 일관성있게 높은 활성을 나타내어, 글리칸 분석을 위한 매우 매력적인 수단이 된다.
실시예 2 - O-글리코시다제
재료 및 방법
엔도-O-글리코시다제의 발현 및 정제
스트렙토코커스 오랄리스 엔도-N-아세틸-갈락토사미니다제는 E. coli에서 벡터 pET21a(+) 내에서 잘 발현되기 위해 코돈-최적화되었다. 벡터를 BL21(DE3) Star 세포로 형질전환시켰다. E. coli는 37℃에서, 200 rpm으로 통상 LB 중에 배양되었다. 플라스미드의 존재 하에서, 100 ㎍/㎖ 암피실린을 첨가하였다. 밤새 항온 처리한 후, 배양액을 신선한 LB(amp) 중에 1:20으로 희석하고, OD620 ~ 0.7-0.8이 될 때까지 생장시킨 후, 1 mM IPTG의 첨가에 의해 재조합 단백질 발현을 유도하고, 세포를 모아서 동결하기 전에 5시간 동안 발현을 지속하였다. 동결된 세포를 해동하고, His 결합 버퍼(20 mM NaP pH 7.4, 500 mM NaCl, 20 mM 이미다졸) 중에 재용해시키고, 세포내 단백질의 방출을 위해 초음파 처리하였다. 세포 잔여물은 원심분리에 의해 제거되었다. 멸균 여과된 상청액을 니켈 컬럼 상에서 친화성 정제하였고, PD-25 컬럼 상에서 PBS 중에서 재-완충화되었다. 단백질의 농도는 나노드롭을 사용하여 결정되었고, 순도는 SDS-PAGE를 통해 추정되었다. 단백질의 서열은 서열번호 3으로 제공되었다.
소분자를 사용한 활성 평가
O-글리칸 코어 부위의 4-메틸움벨리페론(4MU) 기질 및 pNP-기질은, 효소의 가수분해 활성을 결정하기 위한 기질로서 사용되었다. 효소(1 ㎍)를 기질(2 mM)과 혼합하고, 15-120 분 동안 37℃에서 항온 처리하였고, 그동안 시간 형광 및 흡광도(405 nm)를 각각 기록하였다.
단백질 기질을 사용한 활성 평가
TNFαR, EPO, 엔브렐, 페투인, IgA, 오렌시아 및 플라스미노겐(0.5 ㎍)을, 0-24 시간 동안 Smix(1:40 + 1:40) 또는 Am1757(1:40)의 존재 또는 부재 하에 O-글리코시다제(1:40)와 혼합하였다. 단백질을 4-20% Novex 구배 SDS-PAGE 상에서 분리하였다.
최적 효소 조건
효소를 NaCl(0-1.5 M) 및 이온(2 mM CaCl2, 2 mM ZnCl2, 5 mM EDTA) 의존성을 조사하기 위해서, 이들의 각각의 기질(4MU 또는 pNP)과 함께 항온 처리하였다. pH 최적화를 위해, 효소를 아세트산 버퍼(50 mM pH 4.6 및 5.6), 및 Tris-HCl 버퍼(20 mM pH 6.8, 7.4, 8.0, 및 8.8)에서 항온 처리하였다. 모든 샘플을 15분 동안 37℃에서 항온 처리하였다. 모든 값들은 각 그룹 내의 최고 활성에 대한 상대적인 활성으로서 표현되었다.
시판되는 효소와의 비교
식별된 효소, 뿐만 아니라 기존의 브랜드로부터 시판되는 효소[NEB 엔테로코커스 패칼리스(Enterococcus faecalis) 유래의 O-글리코시다제(카탈로그 # P0733S, 다발로서는 #E0540S)]를 또한 이들의 각각의 기질(들) 및 최적화된 버퍼와 함께 항온 처리하였고, SDS-PAGE 상에서 분리하기 전에 천연의 조건 하에 상이한 당단백질들과 함께 0-24 시간 동안 항온 처리하였다.
결과
스트렙토코커스 오랄리스 엔도-α-N-아세틸-갈락토사미니다제 발현/정제
발견 상 동안, S. 오랄리스 및 비피도박테리움 비피둠(Bifidobacterium bifidum)으로부터의 2개의 상이한 엔도-α-N-아세틸-갈락토사미니다제가 고려되는데, 이들 둘다 고분자량 박테리아 단백질(> 200 kDa)이다. B. 비피둠 글리코시다제는 매우 불안정하거나, 또는 적어도 발현 및 친화성 정제 이후 고도로 절편화된 부분을 발생시켰다. 특정 절편화는 또한 S. 오랄리스에 대하여 시각화될 수도 있으나, 훨씬 덜 확연하다(도 8a). 추가로, 이 효소는 4℃에서 최대 1주까지 어떠한 추가적인 분해도 없이 안정하였다(도 8b). 그러나 발현 수준(ca 5-10 mg/L)은 매우 낮다. 추가적인 분석은 절편화가 초음파 처리 때문이라는 것을 암시한다.
O-글리코시다제는 합성적 pNP-표지된 코어 1-3 O-글리칸에 대해 작용할 수 있다.
2개의 O-글리코시다제의 계속적인 분석은 코어 2 및 3에 대해 훨씬 더 낮은 활성을 갖는 코어 1 글리칸의 현저한 선호도를 나타내었다(도 9). 중요하게는, S. 오랄리스 유래의 글리코시다제는 B. 비피둠 유래의 해당 유전자보다 유의하게 더 높은 활성을 나타내므로, 본 발명자들은 S. 오랄리스 O-글리코시다제에 주로 초점을 맞추기로 결정하였다.
MgCl
2
의 첨가는 S. 오랄리스 O-글리코시다제의 활성을 유의하게 증가시킨다.
O-글리코시다제에 대한 최적 조건을 결정하기 위해서, 효소는 다양한 범위의 pH 및 이온 하의 상이한 조건에서 pNP 코어 1 기질과 함께 항온 처리되었다(도 10). O-글리코시다제는 중성 내지 약 염기성 pH에서 높은 활성을 나타내었고, Zn2+의 존재에 의해 완전히 저해되었으나, 최대 8 mM MgCl2의 존재 하에 활성이 증가되었다(도 10c).
S. 오랄리스 O-글리코시다제는 천연의 당단백질로부터 글리칸을 가수분해할 수 있다.
모든 O-글리칸의 가수분해를 매개하는데 필요한 역학 및 투여량을 조사하기 위하여, 천연의 TNFαR을 실시예 1에서 특징화된 시알리다제 혼합물(Am1757:Am0707의 1:1 혼합물)과 조합하여 1-12시간 동안 가변량의 O-글리코시다제와 함께, 또는 시알다제 혼합물 단독과 함께 항온 처리하였다. 도 11에 나타난 바와 같이, 심지어 필적할만하게 낮은 농도(예를 들어 ca 0.1 ㎍, 1:10)의 효소는 1시간 이내에 기질을 가수분해할 수 있었다. 항온 처리 시간을 12 시간까지 상승시키면, 효소가 고농도의 시알리다제와 함께 1:50의 비로 기질을 완전히 가수분해시킬 수 있는 능력을 생성한다. 중요한 것은, 효소가 일부 측면에서는 "양자 택일(nothing or all)" 효소이어서, 거의 반-가수분해된 당단백질은 아니고 비-가수분해되거나 또는 완전히 가수분해된 단백질일 수 있다는 점이다.
S. 오랄리스 O-글리코시다제는 상이한 천연의 당단백질에 대해 작용할 수 있다
단지 O-글리코시다제만이 TNFαR에 작용할 수 있는지, 또는 몇몇 천연의 당단백질에 작용할 수 있는지를 추가로 조사하기 위하여, 본 발명자들은 7개의 상이한 당단백질들을 가수분해 효소의 조합과 함께 항온 처리하였다(도 12). S. 오랄리스 O-글리코시다제, 뿐만 아니라 (시알리다제와 조합된) B. 비피둠 효소는 밤새 항온 처리된 이후 모든 천연의 단백질을 가수분해할 수 있었으나, 플라스모겐에 대한 활성은 단백질의 고분자량 때문에 평가하기 어려웠다. 그러나 양쪽 효소는 시알리다제의 존재에 따라 크게 달라졌으며, 이는 말단 시알산이 활성을 저해하기 때문이다.
S.
오랄리스 O-글리코시다제는 NEB 산물 포트폴리오에 비해 천연의 당단백질을 가수분해하는데 우세하다.
기존의 상업적인 제품에 대한 S. 오랄리스 글리코시다제의 활성을 비교하기 위해, 본 발명자들은 1시간 또는 16시간 동안 가변되는 양의 글리코시다제를 사용하여 TNFαR을 가수분해할 수 있는 이들의 능력으로 비교하였다. ca 1:5의 효소:기질 비를 사용하여, S. 오랄리스 글리코시다제는 1시간 내에 이의 기질을 완전히 가수분해할 수 있었다. 심지어 1:1의 효소:기질 비에서도, NEB O-글리코시다제는 모든 O-연결된 글리칸을 가수분해하지 않지만, 단지 몇몇 용이하게 접근가능한 글리칸에만 작용하였다. 추가적인 항온 처리(예를 들어 16시간)은 1:50의 효소:기질 비에서 허용되나, S. 오랄리스 글리코시다제의 전체 효과를 여전히 유지한다. 그러나, NEB O-글리코시다제는 여전히 산물을 완전히 탈당화시키는데 실패하여, 그 변성이 이의 기능에 중추적인 반면, S. 오랄리스 O-글리코시다제 산물은 또한 천연의 단백질에 대해 높은 활성을 갖는다(도 13). S. 오랄리스 O-글리코시다제는 천연의 단백질에 작용할 뿐만 아니라, 또한 변성된 단백질로부터 글리칸을 가수분해할 수 있다(데이터 미도시).
글리칸 조성물은 O-글리코시다제의 활성에 영향을 미친다
O-글리코시다제 활성을 위한 특이적인 글리칸의 필요성을 추가로 연구하기 위해, TNFαR을 O-글리코시다제의 첨가 이전에, 상이한 효소와 함께 사전-항온처리하여, 개별적인 글리칸을 제거하였다. 말단 시알산의 제거는 갈락토스의 존재에서와 마찬가지로 활성에 매우 중요하며, 이는 O-글리코시다제가 단일의 (말단) GalNAc을 제거할 수 없다는 것을 나타낸다(도 14).
O-글리코시다제는 천연의 단백질로부터 O-글리칸을 제거하는데 매우 효율적이다.
일단 조합된 O-glyk + Smix 조성물의 최종적인 농도가 결정되었을 때(1:40), 본 발명자들은 경쟁자 브랜드 제품(NEB)과의 비교를 반복하였다. 일부 가수 분해가 NEB 산물을 사용하여 TNFαR 상에서 탐지될 수 있는 경우, 가수 분해는 심지어 12시간 이후에도 완전하지 않은 것이 명백하다. 이와는 대조적으로, 조합된 O-glyk + Smix 조성물은 4시간 이내에 당단백질의 완전한 가수분해를 발생시켰고, 이는 렉틴 블롯에 의해 뒷받침되었다(도 15).
유사하게, 엔브렐은 조합된 O-glyk + Smix 조성물이 이를 완전히 가수분해할 수 있는 동일한 패턴을 나타낸 반면, NEB 산물은 그렇지 않았다. 그러나 퓨틴(feutin)에 대해서는, 양쪽 산물은 동일하게 효율적인 것으로 보인다(도 16).
2-3 및 2-6 연결된 시알산은 둘 다 O-글리코시다제의 활성을 저해한다
O-글리코시다제 활성에 대한 2-3 또는 2-6 연결된 시알산의 상호 효과를 평가하기 위해서, 본 발명자들은 O-글리코시다제를 2-3 특이적인, 또는 광범위한 시알리다제(예를 들어, 각각 Am1757 및 Smix) 모두와 함께 항온 처리하였다. 예비 데이터에서 Am1757 및 Am0707이 당단백질로부터 동일한 양의 시알산을 방출할 수 있다고 암시하기는 하지만, 당단백질을 Am1757 (또는 Smix)로 처리하는 것은 기질 (TNFaR)의 더욱 신속한 가수분해를 야기하였다. 그러나, 완전한 가수분해를 위해서는, 당단백질에 광범위한 시알리다제를 처리하여, 또한 2-6 (또는 2-8) 시알산을 제거하는 것이 매우 중요하였다(도 17).
GVS O-글리코시다제 다발의 천연의 활성은 매우 효율적인 시알리다제 활성에 기인한다.
조합된 O-glyk + Smix 조성물에서의 개별적인 성분의 효과를 결정하기 위해, O-glyk 및 NEB를 4개의 상이한 시알리다제 산물(GVS_Smix, NEB A, NEB S, 및 NEB O)과 함께 항온처리하였다. 조합된 O-glyk + Smix 조성물은 엔브렐로부터 모든 O-글리칸을 효율적으로 가수분해하는 반면(도 18), 시알리다제를 NEB 산물 중 임의의 것으로 변화시킴으로서 O-glyk의 활성을 유의하게 낮추었고, NEB 시알리다제 A가 가장 강력하였다. 그러나, NEB O-글리코시다제 다발(NEB O-글리코시다제와 NEB 시알리다제 O)이 엔브렐 또는 TNFαR을 가수분해할 수 없는 반면(도 15, 16), NEB 시알리다제 O 대신에 GVS_Smix를 사용함으로서, 당단백질의 전체 가수분해가 관찰되었고, 이는 조합된 O-glyk + Smix 조성물의 효율이 적어도 부분적으로 시알리다제가 당단백질 상의 모든 2-3 및 2-6 결합을 가수분해하는 능력에 의존한다는 것을 암시한다.
실시예 3 - O-당단백질 특이적인 엔도프로테아제
본 발명자들은 최근 서열번호 12로 이루어지는 폴리펩티드의 엔도프로테아제 활성이 적어도 부분적으로는 특이적인 시알산 결합에 의존하여, 완전한 효과를 위해서는 2-3 및 2-6 연결된 시알산 둘 다의 제거가 필요하다는 것을 결정하였다. 엔도프로테아제 활성에 대한 특이적인 시알산 결합의 개별적인 역할을 결정하기 위해, 본 발명자들은 30분-20시간 동안 에타너셉트를 엔도프로테아제와 조합하여, 상이한 시알리다제와 함께 항온 처리하였다. 2-3 결합의 제거는 엔도프로테아제 활성을 강화하기에 충분한 것으로 보인다(도 19). 사용된 시알리다제는 (1) Am0707 = 서열번호 3의 폴리펩티드; (2) Am1757 = 서열번호 6의 폴리펩티드; 혼합물 = (1)과 (2)의 1:1 조합이다.
서열들
서열번호 1 - 시알리다제, Am0707 - 야생형(밑줄은 신호 서열)
서열번호 2 - 시알리다제, Am0707 - 신호가 없는 야생형
서열번호 3 - 시알리다제, Am0707 - 추가적인 N 말단 메티오닌 및 C 말단 링커+ His6 태그 포함(볼드체 & 밑줄)
서열번호 4 - 시알리다제, Am1757 - 야생형(밑줄은 신호 서열)
서열번호 5 - 시알리다제, Am1757 - 신호가 없는 야생형
서열번호 6 - 시알리다제, Am1757 - 추가적인 N 말단 메티오닌 및 C 말단 링커+ His6 태그 포함(볼드체 & 밑줄)
서열번호 7 - 스트렙토코커스 오랄리스 야생형으로부터의 O-글리코시다제(밑줄은 신호 서열; 볼드체 & 밑줄은 LPXTG 세포 벽 앵커 모티프의 C 말단 요소)
서열번호 8 - 신호 서열이 제거된, 스트렙토코커스 오랄리스 야생형으로부터의 O-글리코시다제(볼드체 & 밑줄은 LPXTG 세포 벽 앵커 모티프의 C 말단 요소)
서열번호 9 - 신호 서열 및 LPXTG 세포 벽 앵커 모티프의 C 말단 요소가 모두 제거된, 스트렙토코커스 오랄리스 야생형으로부터의 O-글리코시다제
서열번호 10 - 추가적인 N 말단 Met, C 말단 GSGLE-His6 태그(볼드체 & 밑줄)을 갖고, 신호 서열 및 LPXTG 세포 벽 앵커 모티프의 C 말단 요소가 제거된, 스트렙토코커스 오랄리스부터의 O-글리코시다제
서열번호 11 - O-당단백질-특이적인 엔도프로테아제
서열번호 12 - O-당단백질-특이적인 엔도프로테아제(LS)
서열번호 13 - 서열번호 10를 암호화함
SEQUENCE LISTING
<110> GENOVIS AB
<120> Tools for Glycan Analysis
<130> N410969WO
<150> GB1708471.6
<151> 2017-05-26
<150> GB1708476.5
<151> 2017-05-26
<150> GB1806655.5
<151> 2018-04-24
<160> 13
<170> PatentIn version 3.5
<210> 1
<211> 419
<212> PRT
<213> Akkermansia muciniphila
<400> 1
Met Thr Trp Leu Leu Cys Gly Arg Gly Lys Trp Asn Lys Val Lys Arg
1 5 10 15
Met Met Asn Ser Val Phe Lys Cys Leu Met Ser Ala Val Cys Ala Val
20 25 30
Ala Leu Pro Ala Phe Gly Gln Glu Glu Lys Thr Gly Phe Pro Thr Asp
35 40 45
Arg Ala Val Thr Val Phe Ser Ala Gly Glu Gly Asn Pro Tyr Ala Ser
50 55 60
Ile Arg Ile Pro Ala Leu Leu Ser Ile Gly Lys Gly Gln Leu Leu Ala
65 70 75 80
Phe Ala Glu Gly Arg Tyr Lys Asn Thr Asp Gln Gly Glu Asn Asp Ile
85 90 95
Ile Met Ser Val Ser Lys Asn Gly Gly Lys Thr Trp Ser Arg Pro Arg
100 105 110
Ala Ile Ala Lys Ala His Gly Ala Thr Phe Asn Asn Pro Cys Pro Val
115 120 125
Tyr Asp Ala Lys Thr Arg Thr Val Thr Val Val Phe Gln Arg Tyr Pro
130 135 140
Ala Gly Val Lys Glu Arg Gln Pro Asn Ile Pro Asp Gly Trp Asp Asp
145 150 155 160
Glu Lys Cys Ile Arg Asn Phe Met Ile Gln Ser Arg Asn Gly Gly Ser
165 170 175
Ser Trp Thr Lys Pro Gln Glu Ile Thr Lys Thr Thr Lys Arg Pro Ser
180 185 190
Gly Val Asp Ile Met Ala Ser Gly Pro Asn Ala Gly Thr Gln Leu Lys
195 200 205
Ser Gly Ala His Lys Gly Arg Leu Val Ile Pro Met Asn Glu Gly Pro
210 215 220
Phe Gly Lys Trp Val Ile Ser Cys Ile Tyr Ser Asp Asp Gly Gly Lys
225 230 235 240
Ser Trp Lys Leu Gly Gln Pro Thr Ala Asn Met Lys Gly Met Val Asn
245 250 255
Glu Thr Ser Ile Ala Glu Thr Asp Asn Gly Gly Val Val Met Val Ala
260 265 270
Arg His Trp Gly Ala Gly Asn Cys Arg Arg Ile Ala Trp Ser Gln Asp
275 280 285
Gly Gly Glu Thr Trp Gly Gln Val Glu Asp Ala Pro Glu Leu Phe Cys
290 295 300
Asp Ser Thr Gln Asn Ser Leu Met Thr Tyr Ser Leu Ser Asp Gln Pro
305 310 315 320
Ala Tyr Gly Gly Lys Ser Arg Ile Leu Phe Ser Gly Pro Ser Ala Gly
325 330 335
Arg Arg Ile Lys Gly Gln Val Ala Met Ser Tyr Asp Asn Gly Lys Thr
340 345 350
Trp Pro Val Lys Lys Leu Leu Gly Glu Gly Gly Phe Ala Tyr Ser Ser
355 360 365
Leu Ala Met Val Glu Pro Gly Ile Val Gly Val Leu Tyr Glu Glu Asn
370 375 380
Gln Glu His Ile Lys Lys Leu Lys Phe Val Pro Ile Thr Met Glu Trp
385 390 395 400
Leu Thr Asp Gly Glu Asp Thr Gly Leu Ala Pro Gly Lys Lys Ala Pro
405 410 415
Val Leu Lys
<210> 2
<211> 381
<212> PRT
<213> Akkermansia muciniphila
<400> 2
Gln Glu Glu Lys Thr Gly Phe Pro Thr Asp Arg Ala Val Thr Val Phe
1 5 10 15
Ser Ala Gly Glu Gly Asn Pro Tyr Ala Ser Ile Arg Ile Pro Ala Leu
20 25 30
Leu Ser Ile Gly Lys Gly Gln Leu Leu Ala Phe Ala Glu Gly Arg Tyr
35 40 45
Lys Asn Thr Asp Gln Gly Glu Asn Asp Ile Ile Met Ser Val Ser Lys
50 55 60
Asn Gly Gly Lys Thr Trp Ser Arg Pro Arg Ala Ile Ala Lys Ala His
65 70 75 80
Gly Ala Thr Phe Asn Asn Pro Cys Pro Val Tyr Asp Ala Lys Thr Arg
85 90 95
Thr Val Thr Val Val Phe Gln Arg Tyr Pro Ala Gly Val Lys Glu Arg
100 105 110
Gln Pro Asn Ile Pro Asp Gly Trp Asp Asp Glu Lys Cys Ile Arg Asn
115 120 125
Phe Met Ile Gln Ser Arg Asn Gly Gly Ser Ser Trp Thr Lys Pro Gln
130 135 140
Glu Ile Thr Lys Thr Thr Lys Arg Pro Ser Gly Val Asp Ile Met Ala
145 150 155 160
Ser Gly Pro Asn Ala Gly Thr Gln Leu Lys Ser Gly Ala His Lys Gly
165 170 175
Arg Leu Val Ile Pro Met Asn Glu Gly Pro Phe Gly Lys Trp Val Ile
180 185 190
Ser Cys Ile Tyr Ser Asp Asp Gly Gly Lys Ser Trp Lys Leu Gly Gln
195 200 205
Pro Thr Ala Asn Met Lys Gly Met Val Asn Glu Thr Ser Ile Ala Glu
210 215 220
Thr Asp Asn Gly Gly Val Val Met Val Ala Arg His Trp Gly Ala Gly
225 230 235 240
Asn Cys Arg Arg Ile Ala Trp Ser Gln Asp Gly Gly Glu Thr Trp Gly
245 250 255
Gln Val Glu Asp Ala Pro Glu Leu Phe Cys Asp Ser Thr Gln Asn Ser
260 265 270
Leu Met Thr Tyr Ser Leu Ser Asp Gln Pro Ala Tyr Gly Gly Lys Ser
275 280 285
Arg Ile Leu Phe Ser Gly Pro Ser Ala Gly Arg Arg Ile Lys Gly Gln
290 295 300
Val Ala Met Ser Tyr Asp Asn Gly Lys Thr Trp Pro Val Lys Lys Leu
305 310 315 320
Leu Gly Glu Gly Gly Phe Ala Tyr Ser Ser Leu Ala Met Val Glu Pro
325 330 335
Gly Ile Val Gly Val Leu Tyr Glu Glu Asn Gln Glu His Ile Lys Lys
340 345 350
Leu Lys Phe Val Pro Ile Thr Met Glu Trp Leu Thr Asp Gly Glu Asp
355 360 365
Thr Gly Leu Ala Pro Gly Lys Lys Ala Pro Val Leu Lys
370 375 380
<210> 3
<211> 393
<212> PRT
<213> Artificial Sequence
<220>
<223> sialidase, Am0707 - with additional N terminal methionine and C
terminal linker + His6 tag
<400> 3
Met Gln Glu Glu Lys Thr Gly Phe Pro Thr Asp Arg Ala Val Thr Val
1 5 10 15
Phe Ser Ala Gly Glu Gly Asn Pro Tyr Ala Ser Ile Arg Ile Pro Ala
20 25 30
Leu Leu Ser Ile Gly Lys Gly Gln Leu Leu Ala Phe Ala Glu Gly Arg
35 40 45
Tyr Lys Asn Thr Asp Gln Gly Glu Asn Asp Ile Ile Met Ser Val Ser
50 55 60
Lys Asn Gly Gly Lys Thr Trp Ser Arg Pro Arg Ala Ile Ala Lys Ala
65 70 75 80
His Gly Ala Thr Phe Asn Asn Pro Cys Pro Val Tyr Asp Ala Lys Thr
85 90 95
Arg Thr Val Thr Val Val Phe Gln Arg Tyr Pro Ala Gly Val Lys Glu
100 105 110
Arg Gln Pro Asn Ile Pro Asp Gly Trp Asp Asp Glu Lys Cys Ile Arg
115 120 125
Asn Phe Met Ile Gln Ser Arg Asn Gly Gly Ser Ser Trp Thr Lys Pro
130 135 140
Gln Glu Ile Thr Lys Thr Thr Lys Arg Pro Ser Gly Val Asp Ile Met
145 150 155 160
Ala Ser Gly Pro Asn Ala Gly Thr Gln Leu Lys Ser Gly Ala His Lys
165 170 175
Gly Arg Leu Val Ile Pro Met Asn Glu Gly Pro Phe Gly Lys Trp Val
180 185 190
Ile Ser Cys Ile Tyr Ser Asp Asp Gly Gly Lys Ser Trp Lys Leu Gly
195 200 205
Gln Pro Thr Ala Asn Met Lys Gly Met Val Asn Glu Thr Ser Ile Ala
210 215 220
Glu Thr Asp Asn Gly Gly Val Val Met Val Ala Arg His Trp Gly Ala
225 230 235 240
Gly Asn Cys Arg Arg Ile Ala Trp Ser Gln Asp Gly Gly Glu Thr Trp
245 250 255
Gly Gln Val Glu Asp Ala Pro Glu Leu Phe Cys Asp Ser Thr Gln Asn
260 265 270
Ser Leu Met Thr Tyr Ser Leu Ser Asp Gln Pro Ala Tyr Gly Gly Lys
275 280 285
Ser Arg Ile Leu Phe Ser Gly Pro Ser Ala Gly Arg Arg Ile Lys Gly
290 295 300
Gln Val Ala Met Ser Tyr Asp Asn Gly Lys Thr Trp Pro Val Lys Lys
305 310 315 320
Leu Leu Gly Glu Gly Gly Phe Ala Tyr Ser Ser Leu Ala Met Val Glu
325 330 335
Pro Gly Ile Val Gly Val Leu Tyr Glu Glu Asn Gln Glu His Ile Lys
340 345 350
Lys Leu Lys Phe Val Pro Ile Thr Met Glu Trp Leu Thr Asp Gly Glu
355 360 365
Asp Thr Gly Leu Ala Pro Gly Lys Lys Ala Pro Val Leu Lys Gly Ser
370 375 380
Gly Leu Glu His His His His His His
385 390
<210> 4
<211> 595
<212> PRT
<213> Akkermansia muciniphila
<400> 4
Met Lys Asn Leu Leu Phe Ala Leu Leu Thr Gly Ser Phe Cys Cys Cys
1 5 10 15
Tyr Ala Gln Gln Lys Ala Ala Pro Val Pro Glu Pro Glu Val Val Ala
20 25 30
Thr Pro Pro Ala Asp Ala Gly Arg Gly Leu Ile Arg Val Asp Ser Arg
35 40 45
Glu Ile Arg His Tyr Ser Gly Thr Arg Lys Glu Pro Asp Tyr Leu Val
50 55 60
Ser Arg Asp Asn Gly Lys Thr Trp Glu Met Lys Ala Ala Pro Ala Gly
65 70 75 80
Tyr Pro Pro Asn Tyr Gly Gly Ile Pro Lys Glu Ser Pro Ala Ile Val
85 90 95
Arg Asn Pro Leu Thr Arg Glu Phe Ile Arg Val Gln Pro Ile Gly Gly
100 105 110
Phe Val Phe Leu Ser Arg Gly Gly Leu Asp Gly Lys Trp Leu Ala Val
115 120 125
Thr Asn Asp Gly Lys Leu Glu Glu Asp Trp Lys Asp Pro Glu Lys Arg
130 135 140
Lys Asn Leu Lys Lys Leu Gly Gly Ile Met Arg Thr Pro Val Phe Val
145 150 155 160
Asn Lys Gly Arg Arg Val Ile Val Pro Phe His Asn Met Gly Gly Gly
165 170 175
Thr Lys Phe His Ile Ser Asp Asp Gly Gly Leu Thr Trp His Val Ser
180 185 190
Arg Asn Gly Val Thr Ser Pro Arg His Glu Ala Arg Pro Pro His Gln
195 200 205
Gly Val Arg Trp Phe Asn Asn Ala Val Glu Ala Thr Val Leu Glu Met
210 215 220
Lys Asp Gly Thr Leu Trp Ala Leu Ala Arg Thr Ser Gln Asp Gln Ala
225 230 235 240
Trp Gln Ala Phe Ser Lys Asp Tyr Gly Glu Thr Trp Ser Lys Pro Glu
245 250 255
Pro Ser Arg Phe Phe Gly Thr Leu Thr Met Asn Thr Leu Gly Arg Leu
260 265 270
Asp Asp Gly Thr Ile Val Ser Leu Trp Thr Asn Thr Met Ala Leu Pro
275 280 285
Glu Asn Ala Thr Ala Gly Asn Gly Thr Trp Glu Asp Val Phe Thr Asn
290 295 300
Arg Asp Ser His His Ile Ala Met Ser Gly Asp Glu Gly Lys Thr Trp
305 310 315 320
Tyr Gly Phe Arg Glu Ile Ile Leu Asp Glu His Arg Asn His Pro Gly
325 330 335
Tyr Ala Thr Leu Asp Gly Pro Glu Asp Arg Gly Lys His Gln Ser Glu
340 345 350
Met Val Gln Leu Asp Lys Asn Arg Ile Leu Ile Ser Leu Gly Gln His
355 360 365
Lys Asn His Arg Arg Leu Val Ile Val Asp Arg Arg Trp Val Gly Ala
370 375 380
Lys Thr Arg Ala Thr Gln Thr Gly Lys Asp Leu Asp Ser Gln Trp Thr
385 390 395 400
Ile His Thr Tyr Ile Pro Gln Lys Lys Gly His Cys Ser Tyr Asn Arg
405 410 415
Lys Pro Ser Ala Glu Leu Val Gln Asp Pro Ser Gly Gly Thr Lys Lys
420 425 430
Val Leu Gln Ile Lys Arg Leu Asp Asp Pro Glu Leu Val Asn Glu Lys
435 440 445
Ser Asn Val Asp Tyr Arg Asn Gly Gly Ala Thr Trp Asn Phe Pro Asn
450 455 460
Gly Thr Thr Gly Leu Val Lys Phe Arg Phe Arg Val Val Asp Gly Glu
465 470 475 480
Gln Ala Asp Asp Ser Gly Leu Gln Val Ser Leu Thr Asp Arg Leu Phe
485 490 495
Asn Ala Cys Asp Ser Thr Thr Lys Asp Tyr Ala Leu Phe Thr Phe Pro
500 505 510
Ile Arg Leu Lys Pro Ala Pro His Leu Leu Leu Gly Met Lys Lys Val
515 520 525
Pro Phe Thr Pro Gly Ala Trp His Glu Ile Ser Leu Leu Trp Gln Gly
530 535 540
Gly Gln Ala Val Val Ser Leu Asp Gly Lys Lys Ala Gly Thr Leu Lys
545 550 555 560
Met Ala Asn Lys Ser Pro Asn Gly Ala Ser Tyr Ile His Phe Ile Ser
565 570 575
Thr Gly Ser Gln Pro Asp Ala Gly Ile Leu Leu Asp Thr Val Asn Ala
580 585 590
Arg Val Lys
595
<210> 5
<211> 577
<212> PRT
<213> Akkermansia muciniphila
<400> 5
Gln Gln Lys Ala Ala Pro Val Pro Glu Pro Glu Val Val Ala Thr Pro
1 5 10 15
Pro Ala Asp Ala Gly Arg Gly Leu Ile Arg Val Asp Ser Arg Glu Ile
20 25 30
Arg His Tyr Ser Gly Thr Arg Lys Glu Pro Asp Tyr Leu Val Ser Arg
35 40 45
Asp Asn Gly Lys Thr Trp Glu Met Lys Ala Ala Pro Ala Gly Tyr Pro
50 55 60
Pro Asn Tyr Gly Gly Ile Pro Lys Glu Ser Pro Ala Ile Val Arg Asn
65 70 75 80
Pro Leu Thr Arg Glu Phe Ile Arg Val Gln Pro Ile Gly Gly Phe Val
85 90 95
Phe Leu Ser Arg Gly Gly Leu Asp Gly Lys Trp Leu Ala Val Thr Asn
100 105 110
Asp Gly Lys Leu Glu Glu Asp Trp Lys Asp Pro Glu Lys Arg Lys Asn
115 120 125
Leu Lys Lys Leu Gly Gly Ile Met Arg Thr Pro Val Phe Val Asn Lys
130 135 140
Gly Arg Arg Val Ile Val Pro Phe His Asn Met Gly Gly Gly Thr Lys
145 150 155 160
Phe His Ile Ser Asp Asp Gly Gly Leu Thr Trp His Val Ser Arg Asn
165 170 175
Gly Val Thr Ser Pro Arg His Glu Ala Arg Pro Pro His Gln Gly Val
180 185 190
Arg Trp Phe Asn Asn Ala Val Glu Ala Thr Val Leu Glu Met Lys Asp
195 200 205
Gly Thr Leu Trp Ala Leu Ala Arg Thr Ser Gln Asp Gln Ala Trp Gln
210 215 220
Ala Phe Ser Lys Asp Tyr Gly Glu Thr Trp Ser Lys Pro Glu Pro Ser
225 230 235 240
Arg Phe Phe Gly Thr Leu Thr Met Asn Thr Leu Gly Arg Leu Asp Asp
245 250 255
Gly Thr Ile Val Ser Leu Trp Thr Asn Thr Met Ala Leu Pro Glu Asn
260 265 270
Ala Thr Ala Gly Asn Gly Thr Trp Glu Asp Val Phe Thr Asn Arg Asp
275 280 285
Ser His His Ile Ala Met Ser Gly Asp Glu Gly Lys Thr Trp Tyr Gly
290 295 300
Phe Arg Glu Ile Ile Leu Asp Glu His Arg Asn His Pro Gly Tyr Ala
305 310 315 320
Thr Leu Asp Gly Pro Glu Asp Arg Gly Lys His Gln Ser Glu Met Val
325 330 335
Gln Leu Asp Lys Asn Arg Ile Leu Ile Ser Leu Gly Gln His Lys Asn
340 345 350
His Arg Arg Leu Val Ile Val Asp Arg Arg Trp Val Gly Ala Lys Thr
355 360 365
Arg Ala Thr Gln Thr Gly Lys Asp Leu Asp Ser Gln Trp Thr Ile His
370 375 380
Thr Tyr Ile Pro Gln Lys Lys Gly His Cys Ser Tyr Asn Arg Lys Pro
385 390 395 400
Ser Ala Glu Leu Val Gln Asp Pro Ser Gly Gly Thr Lys Lys Val Leu
405 410 415
Gln Ile Lys Arg Leu Asp Asp Pro Glu Leu Val Asn Glu Lys Ser Asn
420 425 430
Val Asp Tyr Arg Asn Gly Gly Ala Thr Trp Asn Phe Pro Asn Gly Thr
435 440 445
Thr Gly Leu Val Lys Phe Arg Phe Arg Val Val Asp Gly Glu Gln Ala
450 455 460
Asp Asp Ser Gly Leu Gln Val Ser Leu Thr Asp Arg Leu Phe Asn Ala
465 470 475 480
Cys Asp Ser Thr Thr Lys Asp Tyr Ala Leu Phe Thr Phe Pro Ile Arg
485 490 495
Leu Lys Pro Ala Pro His Leu Leu Leu Gly Met Lys Lys Val Pro Phe
500 505 510
Thr Pro Gly Ala Trp His Glu Ile Ser Leu Leu Trp Gln Gly Gly Gln
515 520 525
Ala Val Val Ser Leu Asp Gly Lys Lys Ala Gly Thr Leu Lys Met Ala
530 535 540
Asn Lys Ser Pro Asn Gly Ala Ser Tyr Ile His Phe Ile Ser Thr Gly
545 550 555 560
Ser Gln Pro Asp Ala Gly Ile Leu Leu Asp Thr Val Asn Ala Arg Val
565 570 575
Lys
<210> 6
<211> 589
<212> PRT
<213> Artificial Sequence
<220>
<223> sialidase, Am1757 - with additional N terminal methionine and C
terminal linker + His6 tag
<400> 6
Met Gln Gln Lys Ala Ala Pro Val Pro Glu Pro Glu Val Val Ala Thr
1 5 10 15
Pro Pro Ala Asp Ala Gly Arg Gly Leu Ile Arg Val Asp Ser Arg Glu
20 25 30
Ile Arg His Tyr Ser Gly Thr Arg Lys Glu Pro Asp Tyr Leu Val Ser
35 40 45
Arg Asp Asn Gly Lys Thr Trp Glu Met Lys Ala Ala Pro Ala Gly Tyr
50 55 60
Pro Pro Asn Tyr Gly Gly Ile Pro Lys Glu Ser Pro Ala Ile Val Arg
65 70 75 80
Asn Pro Leu Thr Arg Glu Phe Ile Arg Val Gln Pro Ile Gly Gly Phe
85 90 95
Val Phe Leu Ser Arg Gly Gly Leu Asp Gly Lys Trp Leu Ala Val Thr
100 105 110
Asn Asp Gly Lys Leu Glu Glu Asp Trp Lys Asp Pro Glu Lys Arg Lys
115 120 125
Asn Leu Lys Lys Leu Gly Gly Ile Met Arg Thr Pro Val Phe Val Asn
130 135 140
Lys Gly Arg Arg Val Ile Val Pro Phe His Asn Met Gly Gly Gly Thr
145 150 155 160
Lys Phe His Ile Ser Asp Asp Gly Gly Leu Thr Trp His Val Ser Arg
165 170 175
Asn Gly Val Thr Ser Pro Arg His Glu Ala Arg Pro Pro His Gln Gly
180 185 190
Val Arg Trp Phe Asn Asn Ala Val Glu Ala Thr Val Leu Glu Met Lys
195 200 205
Asp Gly Thr Leu Trp Ala Leu Ala Arg Thr Ser Gln Asp Gln Ala Trp
210 215 220
Gln Ala Phe Ser Lys Asp Tyr Gly Glu Thr Trp Ser Lys Pro Glu Pro
225 230 235 240
Ser Arg Phe Phe Gly Thr Leu Thr Met Asn Thr Leu Gly Arg Leu Asp
245 250 255
Asp Gly Thr Ile Val Ser Leu Trp Thr Asn Thr Met Ala Leu Pro Glu
260 265 270
Asn Ala Thr Ala Gly Asn Gly Thr Trp Glu Asp Val Phe Thr Asn Arg
275 280 285
Asp Ser His His Ile Ala Met Ser Gly Asp Glu Gly Lys Thr Trp Tyr
290 295 300
Gly Phe Arg Glu Ile Ile Leu Asp Glu His Arg Asn His Pro Gly Tyr
305 310 315 320
Ala Thr Leu Asp Gly Pro Glu Asp Arg Gly Lys His Gln Ser Glu Met
325 330 335
Val Gln Leu Asp Lys Asn Arg Ile Leu Ile Ser Leu Gly Gln His Lys
340 345 350
Asn His Arg Arg Leu Val Ile Val Asp Arg Arg Trp Val Gly Ala Lys
355 360 365
Thr Arg Ala Thr Gln Thr Gly Lys Asp Leu Asp Ser Gln Trp Thr Ile
370 375 380
His Thr Tyr Ile Pro Gln Lys Lys Gly His Cys Ser Tyr Asn Arg Lys
385 390 395 400
Pro Ser Ala Glu Leu Val Gln Asp Pro Ser Gly Gly Thr Lys Lys Val
405 410 415
Leu Gln Ile Lys Arg Leu Asp Asp Pro Glu Leu Val Asn Glu Lys Ser
420 425 430
Asn Val Asp Tyr Arg Asn Gly Gly Ala Thr Trp Asn Phe Pro Asn Gly
435 440 445
Thr Thr Gly Leu Val Lys Phe Arg Phe Arg Val Val Asp Gly Glu Gln
450 455 460
Ala Asp Asp Ser Gly Leu Gln Val Ser Leu Thr Asp Arg Leu Phe Asn
465 470 475 480
Ala Cys Asp Ser Thr Thr Lys Asp Tyr Ala Leu Phe Thr Phe Pro Ile
485 490 495
Arg Leu Lys Pro Ala Pro His Leu Leu Leu Gly Met Lys Lys Val Pro
500 505 510
Phe Thr Pro Gly Ala Trp His Glu Ile Ser Leu Leu Trp Gln Gly Gly
515 520 525
Gln Ala Val Val Ser Leu Asp Gly Lys Lys Ala Gly Thr Leu Lys Met
530 535 540
Ala Asn Lys Ser Pro Asn Gly Ala Ser Tyr Ile His Phe Ile Ser Thr
545 550 555 560
Gly Ser Gln Pro Asp Ala Gly Ile Leu Leu Asp Thr Val Asn Ala Arg
565 570 575
Val Lys Gly Ser Gly Leu Glu His His His His His His
580 585
<210> 7
<211> 2122
<212> PRT
<213> Streptococcus oralis
<400> 7
Met Asp Lys Arg Phe Phe Glu Lys Arg Cys Lys Phe Ser Ile Arg Lys
1 5 10 15
Phe Thr Leu Gly Val Ala Ser Val Met Ile Gly Ala Thr Phe Phe Ala
20 25 30
Ala Ser Pro Val Leu Ala Asp Gln Ala Arg Val Gly Ser Thr Asp Asn
35 40 45
Leu Pro Ser Glu Leu Ala Asp Leu Asp Lys Lys Ala Ser Asp Glu Gly
50 55 60
His Asp Phe Asp Lys Glu Ala Ala Ala Gln Asn Pro Gly Ser Ala Glu
65 70 75 80
Thr Thr Glu Gly Pro Gln Thr Glu Glu Glu Leu Leu Ala Gln Glu Lys
85 90 95
Glu Lys Ser Glu Lys Pro Ser Asn Leu Pro Lys Glu Leu Glu Asp Lys
100 105 110
Leu Glu Lys Ala Glu Asp Asn Gly Arg Glu Val Asp Lys Asp Gln Leu
115 120 125
Ala Gln Asp Thr Gly Lys Leu Val Pro Glu Asp Val Ala Lys Thr Thr
130 135 140
Asn Gly Glu Leu Asn Tyr Gly Ala Thr Val Lys Ile Lys Thr Pro Ser
145 150 155 160
Gly Glu Gly Ser Gly Ile Val Val Ala Lys Asp Leu Val Leu Thr Val
165 170 175
Ser His Asn Phe Ile Lys Asp Ser Gln Glu Gly Asn Ile Arg Lys Val
180 185 190
Val Asp Asn Asp Gln Gly Asp Gly Asp Ile Tyr Ser Ile Ser Tyr Pro
195 200 205
Gly Leu Pro Asp Val Lys Phe Ser Lys Lys Asp Ile Ile His Trp Asp
210 215 220
Arg Glu Gly Tyr Leu Lys Gly Phe Lys Asn Asp Leu Ala Leu Val Arg
225 230 235 240
Leu Arg Thr Val Leu Glu Asn Thr Pro Val Glu Val Thr Lys Lys Pro
245 250 255
Val Val Lys Lys Ile Gly Asp Lys Leu His Val Phe Gly Tyr Pro Glu
260 265 270
Gly Lys Leu Asn Pro Ile Val Asn Thr Thr Val Asp Phe Ala Glu Pro
275 280 285
Tyr Gly Glu Gly Val Gln Gly Ile Gly Tyr Gln Gly Gly Lys Pro Gly
290 295 300
Ala Ser Gly Gly Gly Ile Phe Asp Thr Glu Gly Lys Leu Val Gly Val
305 310 315 320
His Gln Asn Gly Val Val Gly Lys Arg Ser Gly Gly Ile Leu Phe Ser
325 330 335
Pro Ala Gln Leu Lys Trp Ile Gln Asp His Met Gln Gly Ile Ser Ser
340 345 350
Val Lys Pro Ala Asp Leu Glu Glu Lys Glu Lys Pro Ala Glu Glu Lys
355 360 365
Pro Lys Glu Asp Lys Pro Ala Ala Ala Lys Pro Glu Thr Pro Lys Ala
370 375 380
Val Thr Pro Glu Trp Gln Thr Val Ala Asn Lys Glu Gln Gln Gly Thr
385 390 395 400
Val Thr Ile Arg Glu Glu Lys Gly Val Arg Tyr Asn Gln Leu Ser Ser
405 410 415
Thr Ala Gln Asn Asp Asn Asp Gly Lys Pro Ala Leu Phe Glu Lys Gln
420 425 430
Gly Leu Thr Val Asp Ala Asn Gly Asn Ala Thr Val Asp Leu Thr Phe
435 440 445
Lys Asp Asp Ser Glu Lys Gly Lys Ser Arg Phe Gly Val Phe Leu Lys
450 455 460
Phe Lys Asp Thr Lys Asn Asn Val Phe Val Gly Tyr Asp Gln Gly Gly
465 470 475 480
Trp Phe Trp Glu Tyr Lys Thr Pro Gly Asn Ser Thr Trp Tyr Lys Gly
485 490 495
Asn Arg Val Ala Ala Pro Glu Pro Gly Ser Val Asn Arg Leu Ser Ile
500 505 510
Thr Leu Lys Ser Asp Gly Gln Leu Asn Ala Ser Asn Asn Asp Val Asn
515 520 525
Leu Phe Asp Thr Val Thr Leu Pro Gly Ala Val Asn Glu Asn Leu Lys
530 535 540
Asn Glu Lys Lys Ile Leu Leu Lys Ala Gly Thr Tyr Ser Asn Asp Arg
545 550 555 560
Thr Val Val Ser Val Lys Thr Asp Asn Gln Glu Gly Val Lys Ala Asp
565 570 575
Asp Thr Pro Ala Gln Lys Glu Thr Gly Pro Ala Val Asp Asp Ser Lys
580 585 590
Val Thr Tyr Asp Thr Ile Gln Ser Lys Val Leu Lys Ala Val Ile Asp
595 600 605
Gln Ala Phe Pro Arg Val Lys Glu Tyr Thr Leu Asn Gly His Thr Leu
610 615 620
Pro Gly Gln Val Gln Gln Phe Asn Gln Val Phe Ile Asn Asn His Arg
625 630 635 640
Ile Thr Pro Glu Val Thr Tyr Lys Lys Ile Asn Glu Thr Thr Ala Glu
645 650 655
Tyr Leu Met Lys Leu Arg Asp Asp Ala His Leu Ile Asn Ala Glu Met
660 665 670
Thr Val Arg Leu Gln Val Val Asp Asn Gln Leu His Phe Asp Val Thr
675 680 685
Lys Ile Val Asn His Asn Gln Val Thr Pro Gly Gln Lys Ile Asp Asp
690 695 700
Glu Arg Lys Leu Leu Ser Thr Ile Ser Phe Leu Gly Asn Ala Leu Val
705 710 715 720
Ser Val Ser Ser Asp Gln Ala Gly Ala Lys Phe Asp Gly Ala Thr Met
725 730 735
Ser Asn Asn Thr His Val Ser Gly Asp Asp His Ile Asp Val Thr Asn
740 745 750
Pro Met Lys Asp Leu Ala Lys Gly Tyr Met Tyr Gly Phe Val Ser Thr
755 760 765
Asp Lys Leu Ala Ala Gly Val Trp Ser Asn Ser Gln Asn Ser Tyr Gly
770 775 780
Gly Gly Ser Asn Asp Trp Thr Arg Leu Thr Ala Tyr Lys Glu Thr Val
785 790 795 800
Gly Asn Ala Asn Tyr Val Gly Ile His Ser Ser Glu Trp Gln Trp Glu
805 810 815
Lys Ala Tyr Lys Gly Ile Val Phe Pro Glu Tyr Thr Lys Glu Leu Pro
820 825 830
Ser Ala Lys Val Val Ile Thr Glu Asp Ala Asn Ala Asp Asn Lys Val
835 840 845
Asp Trp Gln Asp Gly Ala Ile Ala Tyr Arg Ser Ile Met Asn Asn Pro
850 855 860
Gln Gly Trp Glu Lys Val Lys Asp Ile Thr Ala Tyr Arg Ile Ala Met
865 870 875 880
Asn Phe Gly Ser Gln Ala Gln Asn Pro Phe Leu Met Thr Leu Asp Gly
885 890 895
Ile Lys Lys Ile Asn Leu His Thr Asp Gly Leu Gly Gln Gly Val Leu
900 905 910
Leu Lys Gly Tyr Gly Ser Glu Gly His Asp Ser Gly His Leu Asn Tyr
915 920 925
Ala Asp Ile Gly Lys Arg Ile Gly Gly Val Glu Asp Phe Lys Thr Leu
930 935 940
Ile Glu Lys Ala Lys Lys Tyr Gly Ala His Leu Gly Ile His Val Asn
945 950 955 960
Ala Ser Glu Thr Tyr Pro Glu Ser Lys Tyr Phe Asn Glu Asn Ile Leu
965 970 975
Arg Lys Asn Pro Asp Gly Ser Tyr Ser Tyr Gly Trp Asn Trp Leu Asp
980 985 990
Gln Gly Ile Asn Ile Asp Ala Ala Tyr Asp Leu Ala His Gly Arg Leu
995 1000 1005
Ala Arg Trp Glu Asp Leu Lys Lys Lys Leu Gly Glu Gly Leu Asp
1010 1015 1020
Phe Ile Tyr Val Asp Val Trp Gly Asn Gly Gln Ser Gly Asp Asn
1025 1030 1035
Gly Ala Trp Ala Thr His Val Leu Ala Lys Glu Ile Asn Lys Gln
1040 1045 1050
Gly Trp Arg Phe Ala Ile Glu Trp Gly His Gly Gly Glu Tyr Asp
1055 1060 1065
Ser Thr Phe Gln His Trp Ala Ala Asp Leu Thr Tyr Gly Gly Tyr
1070 1075 1080
Thr Asn Lys Gly Ile Asn Ser Ala Ile Thr Arg Phe Ile Arg Asn
1085 1090 1095
His Gln Lys Asp Ser Trp Val Gly Asp Tyr Arg Ser Tyr Gly Gly
1100 1105 1110
Ala Ala Asn Tyr Pro Leu Leu Gly Gly Tyr Ser Met Lys Asp Phe
1115 1120 1125
Glu Gly Trp Gln Gly Arg Ser Asp Tyr Asn Gly Tyr Val Thr Asn
1130 1135 1140
Leu Phe Ala His Asp Val Met Thr Lys Tyr Phe Gln His Phe Thr
1145 1150 1155
Val Ser Lys Trp Glu Asn Gly Thr Pro Val Thr Met Thr Asp Asn
1160 1165 1170
Gly Ser Thr Tyr Lys Trp Thr Pro Glu Met Lys Val Glu Leu Val
1175 1180 1185
Asp Ala Ala Gly Asn Lys Val Val Val Thr Arg Lys Ser Asn Asp
1190 1195 1200
Val Asn Ser Pro Gln Tyr Arg Glu Arg Thr Val Thr Leu Asn Gly
1205 1210 1215
Arg Val Ile Gln Asp Gly Ser Ala Tyr Leu Thr Pro Trp Asn Trp
1220 1225 1230
Asp Ala Asn Gly Lys Lys Leu Pro Thr Glu Lys Glu Lys Met Tyr
1235 1240 1245
Tyr Phe Asn Thr Gln Ala Gly Ala Thr Thr Trp Thr Leu Pro Ser
1250 1255 1260
Asp Trp Ala Asn Ser Lys Val Tyr Leu Tyr Lys Leu Thr Asp Gln
1265 1270 1275
Gly Lys Thr Glu Glu Gln Glu Leu Thr Val Thr Asp Gly Lys Ile
1280 1285 1290
Thr Leu Asp Leu Leu Ala Asn Gln Pro Tyr Val Leu Tyr Arg Ser
1295 1300 1305
Lys Gln Thr Asn Pro Glu Met Ser Trp Ser Glu Gly Met His Ile
1310 1315 1320
Tyr Asp Gln Gly Phe Asn Ser Gly Thr Leu Lys His Trp Thr Ile
1325 1330 1335
Ser Gly Asp Ala Ser Lys Ala Glu Ile Val Lys Ser Gln Gly Ala
1340 1345 1350
Asn Glu Met Leu Arg Ile Gln Gly Asn Lys Ser Lys Val Ser Leu
1355 1360 1365
Thr Gln Lys Leu Thr Gly Leu Lys Pro Asn Thr Lys Tyr Ala Val
1370 1375 1380
Tyr Val Gly Val Asp Asn Arg Ser Asn Ala Lys Ala Ser Ile Thr
1385 1390 1395
Val Asn Thr Gly Glu Lys Glu Val Thr Thr Tyr Thr Asn Lys Ser
1400 1405 1410
Leu Ala Leu Asn Tyr Ile Lys Ala Tyr Ala His Asn Asn Arg Arg
1415 1420 1425
Glu Asn Ala Thr Val Asp Asp Thr Ser Tyr Phe Gln Asn Met Tyr
1430 1435 1440
Ala Phe Phe Thr Thr Gly Ser Asp Val Ser Asn Val Thr Leu Thr
1445 1450 1455
Leu Ser Arg Glu Ala Gly Asp Glu Ala Thr Tyr Phe Asp Glu Ile
1460 1465 1470
Arg Thr Phe Glu Asn Asn Ser Ser Met Tyr Gly Asp Lys His Asp
1475 1480 1485
Thr Gly Gln Gly Thr Phe Lys Gln Asp Phe Glu Asn Val Ala Gln
1490 1495 1500
Gly Ile Phe Pro Phe Val Val Gly Gly Val Glu Gly Val Glu Asp
1505 1510 1515
Asn Arg Thr His Leu Ser Glu Lys His Asp Pro Tyr Thr Gln Arg
1520 1525 1530
Gly Trp Asn Gly Lys Lys Val Asp Asp Val Ile Glu Gly Asn Trp
1535 1540 1545
Ser Leu Lys Thr Asn Gly Leu Val Ser Arg Arg Asn Leu Val Tyr
1550 1555 1560
Gln Thr Ile Pro Gln Asn Phe Arg Phe Glu Ala Gly Lys Thr Tyr
1565 1570 1575
Arg Val Thr Phe Glu Tyr Glu Ala Gly Ser Asp Asn Thr Tyr Ala
1580 1585 1590
Phe Val Val Gly Lys Gly Glu Phe Gln Ser Gly Arg Arg Gly Thr
1595 1600 1605
Gln Ala Ser Asn Leu Glu Met His Glu Leu Pro Asn Thr Trp Thr
1610 1615 1620
Asp Ser Lys Lys Ala Lys Lys Val Thr Phe Leu Val Thr Gly Ala
1625 1630 1635
Glu Thr Gly Asp Thr Trp Val Gly Ile Tyr Ser Thr Gly Asn Ala
1640 1645 1650
Ser Asn Thr Arg Gly Asp Ala Gly Gly Asn Ala Asn Phe Arg Gly
1655 1660 1665
Tyr Asn Asp Phe Met Met Asp Asn Leu Gln Ile Glu Glu Ile Thr
1670 1675 1680
Leu Thr Gly Lys Met Leu Thr Glu Asn Ala Leu Lys Asn Tyr Leu
1685 1690 1695
Pro Thr Val Ala Met Thr Asn Tyr Thr Lys Glu Ser Met Asp Ala
1700 1705 1710
Leu Lys Glu Ala Val Phe Asn Leu Ser Gln Ala Asp Asp Asp Ile
1715 1720 1725
Ser Val Glu Glu Ala Arg Ala Glu Ile Ala Lys Ile Glu Ala Leu
1730 1735 1740
Lys Asn Ala Leu Val Gln Lys Lys Thr Ala Leu Val Ala Glu Asp
1745 1750 1755
Phe Glu Ser Leu Asp Ala Pro Ala Gln Pro Gly Glu Gly Leu Glu
1760 1765 1770
Asn Ala Phe Asp Gly Asn Val Ser Ser Leu Trp His Thr Ser Trp
1775 1780 1785
Asn Gly Gly Asp Val Gly Lys Pro Ala Thr Met Val Leu Lys Glu
1790 1795 1800
Pro Thr Glu Ile Thr Gly Leu Arg Tyr Val Pro Arg Ala Ser Asp
1805 1810 1815
Ser Asn Gly Asn Leu Arg Asp Val Lys Leu Val Val Thr Asp Glu
1820 1825 1830
Ser Gly Lys Glu His Thr Phe Asn Val Thr Asp Trp Pro Asn Asn
1835 1840 1845
Asn Lys Pro Lys Asp Ile Asp Phe Gly Lys Thr Ile Lys Ala Lys
1850 1855 1860
Lys Ile Val Leu Thr Gly Thr Lys Thr Tyr Gly Asp Gly Gly Asp
1865 1870 1875
Lys Tyr Gln Ser Ala Ala Glu Leu Ile Phe Thr Arg Pro Gln Val
1880 1885 1890
Ala Glu Thr Pro Leu Asp Leu Ser Gly Tyr Glu Ala Ala Leu Ala
1895 1900 1905
Lys Ala Gln Lys Leu Thr Asp Lys Asp Asn Gln Glu Glu Val Ala
1910 1915 1920
Ser Val Gln Ala Ser Met Lys Tyr Ala Thr Asp Asn His Leu Leu
1925 1930 1935
Thr Glu Arg Met Val Ala Tyr Phe Ala Asp Tyr Leu Asn Gln Leu
1940 1945 1950
Lys Asp Ser Ala Thr Lys Pro Asp Ala Pro Thr Ser Ser Lys Gly
1955 1960 1965
Glu Glu Gln Pro Pro Val Leu Asp Val Pro Glu Phe Lys Gly Gly
1970 1975 1980
Val Asn Ala Thr Glu Ala Ala Val His Glu Val Pro Glu Phe Lys
1985 1990 1995
Gly Gly Val Asn Ala Val Gln Ala Leu Val His Glu Leu Pro Glu
2000 2005 2010
Tyr Lys Gly Gly Ala Asn Ala Val Leu Ala Ala Ala Asn Glu Val
2015 2020 2025
Pro Glu Tyr Lys Gly Gly Ala Asn Ala Val Glu Ala Leu Val Asn
2030 2035 2040
Glu Lys Pro Ala Tyr Thr Gly Val Leu Ala Thr Ala Gly Asp Gln
2045 2050 2055
Ala Ala Pro Thr Val Glu Lys Pro Glu Tyr Pro Leu Thr Pro Ser
2060 2065 2070
Pro Val Ala Asp Thr Lys Thr Pro Gly Ala Lys Asp Glu Glu Lys
2075 2080 2085
Leu Pro Ala Thr Gly Glu His Ser Ser Glu Val Ala Leu Phe Leu
2090 2095 2100
Ala Ser Val Ser Ile Ala Leu Ser Ala Ala Val Leu Ala Thr Lys
2105 2110 2115
Arg Lys Glu Glu
2120
<210> 8
<211> 2084
<212> PRT
<213> Streptococcus oralis
<400> 8
Asp Gln Ala Arg Val Gly Ser Thr Asp Asn Leu Pro Ser Glu Leu Ala
1 5 10 15
Asp Leu Asp Lys Lys Ala Ser Asp Glu Gly His Asp Phe Asp Lys Glu
20 25 30
Ala Ala Ala Gln Asn Pro Gly Ser Ala Glu Thr Thr Glu Gly Pro Gln
35 40 45
Thr Glu Glu Glu Leu Leu Ala Gln Glu Lys Glu Lys Ser Glu Lys Pro
50 55 60
Ser Asn Leu Pro Lys Glu Leu Glu Asp Lys Leu Glu Lys Ala Glu Asp
65 70 75 80
Asn Gly Arg Glu Val Asp Lys Asp Gln Leu Ala Gln Asp Thr Gly Lys
85 90 95
Leu Val Pro Glu Asp Val Ala Lys Thr Thr Asn Gly Glu Leu Asn Tyr
100 105 110
Gly Ala Thr Val Lys Ile Lys Thr Pro Ser Gly Glu Gly Ser Gly Ile
115 120 125
Val Val Ala Lys Asp Leu Val Leu Thr Val Ser His Asn Phe Ile Lys
130 135 140
Asp Ser Gln Glu Gly Asn Ile Arg Lys Val Val Asp Asn Asp Gln Gly
145 150 155 160
Asp Gly Asp Ile Tyr Ser Ile Ser Tyr Pro Gly Leu Pro Asp Val Lys
165 170 175
Phe Ser Lys Lys Asp Ile Ile His Trp Asp Arg Glu Gly Tyr Leu Lys
180 185 190
Gly Phe Lys Asn Asp Leu Ala Leu Val Arg Leu Arg Thr Val Leu Glu
195 200 205
Asn Thr Pro Val Glu Val Thr Lys Lys Pro Val Val Lys Lys Ile Gly
210 215 220
Asp Lys Leu His Val Phe Gly Tyr Pro Glu Gly Lys Leu Asn Pro Ile
225 230 235 240
Val Asn Thr Thr Val Asp Phe Ala Glu Pro Tyr Gly Glu Gly Val Gln
245 250 255
Gly Ile Gly Tyr Gln Gly Gly Lys Pro Gly Ala Ser Gly Gly Gly Ile
260 265 270
Phe Asp Thr Glu Gly Lys Leu Val Gly Val His Gln Asn Gly Val Val
275 280 285
Gly Lys Arg Ser Gly Gly Ile Leu Phe Ser Pro Ala Gln Leu Lys Trp
290 295 300
Ile Gln Asp His Met Gln Gly Ile Ser Ser Val Lys Pro Ala Asp Leu
305 310 315 320
Glu Glu Lys Glu Lys Pro Ala Glu Glu Lys Pro Lys Glu Asp Lys Pro
325 330 335
Ala Ala Ala Lys Pro Glu Thr Pro Lys Ala Val Thr Pro Glu Trp Gln
340 345 350
Thr Val Ala Asn Lys Glu Gln Gln Gly Thr Val Thr Ile Arg Glu Glu
355 360 365
Lys Gly Val Arg Tyr Asn Gln Leu Ser Ser Thr Ala Gln Asn Asp Asn
370 375 380
Asp Gly Lys Pro Ala Leu Phe Glu Lys Gln Gly Leu Thr Val Asp Ala
385 390 395 400
Asn Gly Asn Ala Thr Val Asp Leu Thr Phe Lys Asp Asp Ser Glu Lys
405 410 415
Gly Lys Ser Arg Phe Gly Val Phe Leu Lys Phe Lys Asp Thr Lys Asn
420 425 430
Asn Val Phe Val Gly Tyr Asp Gln Gly Gly Trp Phe Trp Glu Tyr Lys
435 440 445
Thr Pro Gly Asn Ser Thr Trp Tyr Lys Gly Asn Arg Val Ala Ala Pro
450 455 460
Glu Pro Gly Ser Val Asn Arg Leu Ser Ile Thr Leu Lys Ser Asp Gly
465 470 475 480
Gln Leu Asn Ala Ser Asn Asn Asp Val Asn Leu Phe Asp Thr Val Thr
485 490 495
Leu Pro Gly Ala Val Asn Glu Asn Leu Lys Asn Glu Lys Lys Ile Leu
500 505 510
Leu Lys Ala Gly Thr Tyr Ser Asn Asp Arg Thr Val Val Ser Val Lys
515 520 525
Thr Asp Asn Gln Glu Gly Val Lys Ala Asp Asp Thr Pro Ala Gln Lys
530 535 540
Glu Thr Gly Pro Ala Val Asp Asp Ser Lys Val Thr Tyr Asp Thr Ile
545 550 555 560
Gln Ser Lys Val Leu Lys Ala Val Ile Asp Gln Ala Phe Pro Arg Val
565 570 575
Lys Glu Tyr Thr Leu Asn Gly His Thr Leu Pro Gly Gln Val Gln Gln
580 585 590
Phe Asn Gln Val Phe Ile Asn Asn His Arg Ile Thr Pro Glu Val Thr
595 600 605
Tyr Lys Lys Ile Asn Glu Thr Thr Ala Glu Tyr Leu Met Lys Leu Arg
610 615 620
Asp Asp Ala His Leu Ile Asn Ala Glu Met Thr Val Arg Leu Gln Val
625 630 635 640
Val Asp Asn Gln Leu His Phe Asp Val Thr Lys Ile Val Asn His Asn
645 650 655
Gln Val Thr Pro Gly Gln Lys Ile Asp Asp Glu Arg Lys Leu Leu Ser
660 665 670
Thr Ile Ser Phe Leu Gly Asn Ala Leu Val Ser Val Ser Ser Asp Gln
675 680 685
Ala Gly Ala Lys Phe Asp Gly Ala Thr Met Ser Asn Asn Thr His Val
690 695 700
Ser Gly Asp Asp His Ile Asp Val Thr Asn Pro Met Lys Asp Leu Ala
705 710 715 720
Lys Gly Tyr Met Tyr Gly Phe Val Ser Thr Asp Lys Leu Ala Ala Gly
725 730 735
Val Trp Ser Asn Ser Gln Asn Ser Tyr Gly Gly Gly Ser Asn Asp Trp
740 745 750
Thr Arg Leu Thr Ala Tyr Lys Glu Thr Val Gly Asn Ala Asn Tyr Val
755 760 765
Gly Ile His Ser Ser Glu Trp Gln Trp Glu Lys Ala Tyr Lys Gly Ile
770 775 780
Val Phe Pro Glu Tyr Thr Lys Glu Leu Pro Ser Ala Lys Val Val Ile
785 790 795 800
Thr Glu Asp Ala Asn Ala Asp Asn Lys Val Asp Trp Gln Asp Gly Ala
805 810 815
Ile Ala Tyr Arg Ser Ile Met Asn Asn Pro Gln Gly Trp Glu Lys Val
820 825 830
Lys Asp Ile Thr Ala Tyr Arg Ile Ala Met Asn Phe Gly Ser Gln Ala
835 840 845
Gln Asn Pro Phe Leu Met Thr Leu Asp Gly Ile Lys Lys Ile Asn Leu
850 855 860
His Thr Asp Gly Leu Gly Gln Gly Val Leu Leu Lys Gly Tyr Gly Ser
865 870 875 880
Glu Gly His Asp Ser Gly His Leu Asn Tyr Ala Asp Ile Gly Lys Arg
885 890 895
Ile Gly Gly Val Glu Asp Phe Lys Thr Leu Ile Glu Lys Ala Lys Lys
900 905 910
Tyr Gly Ala His Leu Gly Ile His Val Asn Ala Ser Glu Thr Tyr Pro
915 920 925
Glu Ser Lys Tyr Phe Asn Glu Asn Ile Leu Arg Lys Asn Pro Asp Gly
930 935 940
Ser Tyr Ser Tyr Gly Trp Asn Trp Leu Asp Gln Gly Ile Asn Ile Asp
945 950 955 960
Ala Ala Tyr Asp Leu Ala His Gly Arg Leu Ala Arg Trp Glu Asp Leu
965 970 975
Lys Lys Lys Leu Gly Glu Gly Leu Asp Phe Ile Tyr Val Asp Val Trp
980 985 990
Gly Asn Gly Gln Ser Gly Asp Asn Gly Ala Trp Ala Thr His Val Leu
995 1000 1005
Ala Lys Glu Ile Asn Lys Gln Gly Trp Arg Phe Ala Ile Glu Trp
1010 1015 1020
Gly His Gly Gly Glu Tyr Asp Ser Thr Phe Gln His Trp Ala Ala
1025 1030 1035
Asp Leu Thr Tyr Gly Gly Tyr Thr Asn Lys Gly Ile Asn Ser Ala
1040 1045 1050
Ile Thr Arg Phe Ile Arg Asn His Gln Lys Asp Ser Trp Val Gly
1055 1060 1065
Asp Tyr Arg Ser Tyr Gly Gly Ala Ala Asn Tyr Pro Leu Leu Gly
1070 1075 1080
Gly Tyr Ser Met Lys Asp Phe Glu Gly Trp Gln Gly Arg Ser Asp
1085 1090 1095
Tyr Asn Gly Tyr Val Thr Asn Leu Phe Ala His Asp Val Met Thr
1100 1105 1110
Lys Tyr Phe Gln His Phe Thr Val Ser Lys Trp Glu Asn Gly Thr
1115 1120 1125
Pro Val Thr Met Thr Asp Asn Gly Ser Thr Tyr Lys Trp Thr Pro
1130 1135 1140
Glu Met Lys Val Glu Leu Val Asp Ala Ala Gly Asn Lys Val Val
1145 1150 1155
Val Thr Arg Lys Ser Asn Asp Val Asn Ser Pro Gln Tyr Arg Glu
1160 1165 1170
Arg Thr Val Thr Leu Asn Gly Arg Val Ile Gln Asp Gly Ser Ala
1175 1180 1185
Tyr Leu Thr Pro Trp Asn Trp Asp Ala Asn Gly Lys Lys Leu Pro
1190 1195 1200
Thr Glu Lys Glu Lys Met Tyr Tyr Phe Asn Thr Gln Ala Gly Ala
1205 1210 1215
Thr Thr Trp Thr Leu Pro Ser Asp Trp Ala Asn Ser Lys Val Tyr
1220 1225 1230
Leu Tyr Lys Leu Thr Asp Gln Gly Lys Thr Glu Glu Gln Glu Leu
1235 1240 1245
Thr Val Thr Asp Gly Lys Ile Thr Leu Asp Leu Leu Ala Asn Gln
1250 1255 1260
Pro Tyr Val Leu Tyr Arg Ser Lys Gln Thr Asn Pro Glu Met Ser
1265 1270 1275
Trp Ser Glu Gly Met His Ile Tyr Asp Gln Gly Phe Asn Ser Gly
1280 1285 1290
Thr Leu Lys His Trp Thr Ile Ser Gly Asp Ala Ser Lys Ala Glu
1295 1300 1305
Ile Val Lys Ser Gln Gly Ala Asn Glu Met Leu Arg Ile Gln Gly
1310 1315 1320
Asn Lys Ser Lys Val Ser Leu Thr Gln Lys Leu Thr Gly Leu Lys
1325 1330 1335
Pro Asn Thr Lys Tyr Ala Val Tyr Val Gly Val Asp Asn Arg Ser
1340 1345 1350
Asn Ala Lys Ala Ser Ile Thr Val Asn Thr Gly Glu Lys Glu Val
1355 1360 1365
Thr Thr Tyr Thr Asn Lys Ser Leu Ala Leu Asn Tyr Ile Lys Ala
1370 1375 1380
Tyr Ala His Asn Asn Arg Arg Glu Asn Ala Thr Val Asp Asp Thr
1385 1390 1395
Ser Tyr Phe Gln Asn Met Tyr Ala Phe Phe Thr Thr Gly Ser Asp
1400 1405 1410
Val Ser Asn Val Thr Leu Thr Leu Ser Arg Glu Ala Gly Asp Glu
1415 1420 1425
Ala Thr Tyr Phe Asp Glu Ile Arg Thr Phe Glu Asn Asn Ser Ser
1430 1435 1440
Met Tyr Gly Asp Lys His Asp Thr Gly Gln Gly Thr Phe Lys Gln
1445 1450 1455
Asp Phe Glu Asn Val Ala Gln Gly Ile Phe Pro Phe Val Val Gly
1460 1465 1470
Gly Val Glu Gly Val Glu Asp Asn Arg Thr His Leu Ser Glu Lys
1475 1480 1485
His Asp Pro Tyr Thr Gln Arg Gly Trp Asn Gly Lys Lys Val Asp
1490 1495 1500
Asp Val Ile Glu Gly Asn Trp Ser Leu Lys Thr Asn Gly Leu Val
1505 1510 1515
Ser Arg Arg Asn Leu Val Tyr Gln Thr Ile Pro Gln Asn Phe Arg
1520 1525 1530
Phe Glu Ala Gly Lys Thr Tyr Arg Val Thr Phe Glu Tyr Glu Ala
1535 1540 1545
Gly Ser Asp Asn Thr Tyr Ala Phe Val Val Gly Lys Gly Glu Phe
1550 1555 1560
Gln Ser Gly Arg Arg Gly Thr Gln Ala Ser Asn Leu Glu Met His
1565 1570 1575
Glu Leu Pro Asn Thr Trp Thr Asp Ser Lys Lys Ala Lys Lys Val
1580 1585 1590
Thr Phe Leu Val Thr Gly Ala Glu Thr Gly Asp Thr Trp Val Gly
1595 1600 1605
Ile Tyr Ser Thr Gly Asn Ala Ser Asn Thr Arg Gly Asp Ala Gly
1610 1615 1620
Gly Asn Ala Asn Phe Arg Gly Tyr Asn Asp Phe Met Met Asp Asn
1625 1630 1635
Leu Gln Ile Glu Glu Ile Thr Leu Thr Gly Lys Met Leu Thr Glu
1640 1645 1650
Asn Ala Leu Lys Asn Tyr Leu Pro Thr Val Ala Met Thr Asn Tyr
1655 1660 1665
Thr Lys Glu Ser Met Asp Ala Leu Lys Glu Ala Val Phe Asn Leu
1670 1675 1680
Ser Gln Ala Asp Asp Asp Ile Ser Val Glu Glu Ala Arg Ala Glu
1685 1690 1695
Ile Ala Lys Ile Glu Ala Leu Lys Asn Ala Leu Val Gln Lys Lys
1700 1705 1710
Thr Ala Leu Val Ala Glu Asp Phe Glu Ser Leu Asp Ala Pro Ala
1715 1720 1725
Gln Pro Gly Glu Gly Leu Glu Asn Ala Phe Asp Gly Asn Val Ser
1730 1735 1740
Ser Leu Trp His Thr Ser Trp Asn Gly Gly Asp Val Gly Lys Pro
1745 1750 1755
Ala Thr Met Val Leu Lys Glu Pro Thr Glu Ile Thr Gly Leu Arg
1760 1765 1770
Tyr Val Pro Arg Ala Ser Asp Ser Asn Gly Asn Leu Arg Asp Val
1775 1780 1785
Lys Leu Val Val Thr Asp Glu Ser Gly Lys Glu His Thr Phe Asn
1790 1795 1800
Val Thr Asp Trp Pro Asn Asn Asn Lys Pro Lys Asp Ile Asp Phe
1805 1810 1815
Gly Lys Thr Ile Lys Ala Lys Lys Ile Val Leu Thr Gly Thr Lys
1820 1825 1830
Thr Tyr Gly Asp Gly Gly Asp Lys Tyr Gln Ser Ala Ala Glu Leu
1835 1840 1845
Ile Phe Thr Arg Pro Gln Val Ala Glu Thr Pro Leu Asp Leu Ser
1850 1855 1860
Gly Tyr Glu Ala Ala Leu Ala Lys Ala Gln Lys Leu Thr Asp Lys
1865 1870 1875
Asp Asn Gln Glu Glu Val Ala Ser Val Gln Ala Ser Met Lys Tyr
1880 1885 1890
Ala Thr Asp Asn His Leu Leu Thr Glu Arg Met Val Ala Tyr Phe
1895 1900 1905
Ala Asp Tyr Leu Asn Gln Leu Lys Asp Ser Ala Thr Lys Pro Asp
1910 1915 1920
Ala Pro Thr Ser Ser Lys Gly Glu Glu Gln Pro Pro Val Leu Asp
1925 1930 1935
Val Pro Glu Phe Lys Gly Gly Val Asn Ala Thr Glu Ala Ala Val
1940 1945 1950
His Glu Val Pro Glu Phe Lys Gly Gly Val Asn Ala Val Gln Ala
1955 1960 1965
Leu Val His Glu Leu Pro Glu Tyr Lys Gly Gly Ala Asn Ala Val
1970 1975 1980
Leu Ala Ala Ala Asn Glu Val Pro Glu Tyr Lys Gly Gly Ala Asn
1985 1990 1995
Ala Val Glu Ala Leu Val Asn Glu Lys Pro Ala Tyr Thr Gly Val
2000 2005 2010
Leu Ala Thr Ala Gly Asp Gln Ala Ala Pro Thr Val Glu Lys Pro
2015 2020 2025
Glu Tyr Pro Leu Thr Pro Ser Pro Val Ala Asp Thr Lys Thr Pro
2030 2035 2040
Gly Ala Lys Asp Glu Glu Lys Leu Pro Ala Thr Gly Glu His Ser
2045 2050 2055
Ser Glu Val Ala Leu Phe Leu Ala Ser Val Ser Ile Ala Leu Ser
2060 2065 2070
Ala Ala Val Leu Ala Thr Lys Arg Lys Glu Glu
2075 2080
<210> 9
<211> 2053
<212> PRT
<213> Streptococcus oralis
<400> 9
Asp Gln Ala Arg Val Gly Ser Thr Asp Asn Leu Pro Ser Glu Leu Ala
1 5 10 15
Asp Leu Asp Lys Lys Ala Ser Asp Glu Gly His Asp Phe Asp Lys Glu
20 25 30
Ala Ala Ala Gln Asn Pro Gly Ser Ala Glu Thr Thr Glu Gly Pro Gln
35 40 45
Thr Glu Glu Glu Leu Leu Ala Gln Glu Lys Glu Lys Ser Glu Lys Pro
50 55 60
Ser Asn Leu Pro Lys Glu Leu Glu Asp Lys Leu Glu Lys Ala Glu Asp
65 70 75 80
Asn Gly Arg Glu Val Asp Lys Asp Gln Leu Ala Gln Asp Thr Gly Lys
85 90 95
Leu Val Pro Glu Asp Val Ala Lys Thr Thr Asn Gly Glu Leu Asn Tyr
100 105 110
Gly Ala Thr Val Lys Ile Lys Thr Pro Ser Gly Glu Gly Ser Gly Ile
115 120 125
Val Val Ala Lys Asp Leu Val Leu Thr Val Ser His Asn Phe Ile Lys
130 135 140
Asp Ser Gln Glu Gly Asn Ile Arg Lys Val Val Asp Asn Asp Gln Gly
145 150 155 160
Asp Gly Asp Ile Tyr Ser Ile Ser Tyr Pro Gly Leu Pro Asp Val Lys
165 170 175
Phe Ser Lys Lys Asp Ile Ile His Trp Asp Arg Glu Gly Tyr Leu Lys
180 185 190
Gly Phe Lys Asn Asp Leu Ala Leu Val Arg Leu Arg Thr Val Leu Glu
195 200 205
Asn Thr Pro Val Glu Val Thr Lys Lys Pro Val Val Lys Lys Ile Gly
210 215 220
Asp Lys Leu His Val Phe Gly Tyr Pro Glu Gly Lys Leu Asn Pro Ile
225 230 235 240
Val Asn Thr Thr Val Asp Phe Ala Glu Pro Tyr Gly Glu Gly Val Gln
245 250 255
Gly Ile Gly Tyr Gln Gly Gly Lys Pro Gly Ala Ser Gly Gly Gly Ile
260 265 270
Phe Asp Thr Glu Gly Lys Leu Val Gly Val His Gln Asn Gly Val Val
275 280 285
Gly Lys Arg Ser Gly Gly Ile Leu Phe Ser Pro Ala Gln Leu Lys Trp
290 295 300
Ile Gln Asp His Met Gln Gly Ile Ser Ser Val Lys Pro Ala Asp Leu
305 310 315 320
Glu Glu Lys Glu Lys Pro Ala Glu Glu Lys Pro Lys Glu Asp Lys Pro
325 330 335
Ala Ala Ala Lys Pro Glu Thr Pro Lys Ala Val Thr Pro Glu Trp Gln
340 345 350
Thr Val Ala Asn Lys Glu Gln Gln Gly Thr Val Thr Ile Arg Glu Glu
355 360 365
Lys Gly Val Arg Tyr Asn Gln Leu Ser Ser Thr Ala Gln Asn Asp Asn
370 375 380
Asp Gly Lys Pro Ala Leu Phe Glu Lys Gln Gly Leu Thr Val Asp Ala
385 390 395 400
Asn Gly Asn Ala Thr Val Asp Leu Thr Phe Lys Asp Asp Ser Glu Lys
405 410 415
Gly Lys Ser Arg Phe Gly Val Phe Leu Lys Phe Lys Asp Thr Lys Asn
420 425 430
Asn Val Phe Val Gly Tyr Asp Gln Gly Gly Trp Phe Trp Glu Tyr Lys
435 440 445
Thr Pro Gly Asn Ser Thr Trp Tyr Lys Gly Asn Arg Val Ala Ala Pro
450 455 460
Glu Pro Gly Ser Val Asn Arg Leu Ser Ile Thr Leu Lys Ser Asp Gly
465 470 475 480
Gln Leu Asn Ala Ser Asn Asn Asp Val Asn Leu Phe Asp Thr Val Thr
485 490 495
Leu Pro Gly Ala Val Asn Glu Asn Leu Lys Asn Glu Lys Lys Ile Leu
500 505 510
Leu Lys Ala Gly Thr Tyr Ser Asn Asp Arg Thr Val Val Ser Val Lys
515 520 525
Thr Asp Asn Gln Glu Gly Val Lys Ala Asp Asp Thr Pro Ala Gln Lys
530 535 540
Glu Thr Gly Pro Ala Val Asp Asp Ser Lys Val Thr Tyr Asp Thr Ile
545 550 555 560
Gln Ser Lys Val Leu Lys Ala Val Ile Asp Gln Ala Phe Pro Arg Val
565 570 575
Lys Glu Tyr Thr Leu Asn Gly His Thr Leu Pro Gly Gln Val Gln Gln
580 585 590
Phe Asn Gln Val Phe Ile Asn Asn His Arg Ile Thr Pro Glu Val Thr
595 600 605
Tyr Lys Lys Ile Asn Glu Thr Thr Ala Glu Tyr Leu Met Lys Leu Arg
610 615 620
Asp Asp Ala His Leu Ile Asn Ala Glu Met Thr Val Arg Leu Gln Val
625 630 635 640
Val Asp Asn Gln Leu His Phe Asp Val Thr Lys Ile Val Asn His Asn
645 650 655
Gln Val Thr Pro Gly Gln Lys Ile Asp Asp Glu Arg Lys Leu Leu Ser
660 665 670
Thr Ile Ser Phe Leu Gly Asn Ala Leu Val Ser Val Ser Ser Asp Gln
675 680 685
Ala Gly Ala Lys Phe Asp Gly Ala Thr Met Ser Asn Asn Thr His Val
690 695 700
Ser Gly Asp Asp His Ile Asp Val Thr Asn Pro Met Lys Asp Leu Ala
705 710 715 720
Lys Gly Tyr Met Tyr Gly Phe Val Ser Thr Asp Lys Leu Ala Ala Gly
725 730 735
Val Trp Ser Asn Ser Gln Asn Ser Tyr Gly Gly Gly Ser Asn Asp Trp
740 745 750
Thr Arg Leu Thr Ala Tyr Lys Glu Thr Val Gly Asn Ala Asn Tyr Val
755 760 765
Gly Ile His Ser Ser Glu Trp Gln Trp Glu Lys Ala Tyr Lys Gly Ile
770 775 780
Val Phe Pro Glu Tyr Thr Lys Glu Leu Pro Ser Ala Lys Val Val Ile
785 790 795 800
Thr Glu Asp Ala Asn Ala Asp Asn Lys Val Asp Trp Gln Asp Gly Ala
805 810 815
Ile Ala Tyr Arg Ser Ile Met Asn Asn Pro Gln Gly Trp Glu Lys Val
820 825 830
Lys Asp Ile Thr Ala Tyr Arg Ile Ala Met Asn Phe Gly Ser Gln Ala
835 840 845
Gln Asn Pro Phe Leu Met Thr Leu Asp Gly Ile Lys Lys Ile Asn Leu
850 855 860
His Thr Asp Gly Leu Gly Gln Gly Val Leu Leu Lys Gly Tyr Gly Ser
865 870 875 880
Glu Gly His Asp Ser Gly His Leu Asn Tyr Ala Asp Ile Gly Lys Arg
885 890 895
Ile Gly Gly Val Glu Asp Phe Lys Thr Leu Ile Glu Lys Ala Lys Lys
900 905 910
Tyr Gly Ala His Leu Gly Ile His Val Asn Ala Ser Glu Thr Tyr Pro
915 920 925
Glu Ser Lys Tyr Phe Asn Glu Asn Ile Leu Arg Lys Asn Pro Asp Gly
930 935 940
Ser Tyr Ser Tyr Gly Trp Asn Trp Leu Asp Gln Gly Ile Asn Ile Asp
945 950 955 960
Ala Ala Tyr Asp Leu Ala His Gly Arg Leu Ala Arg Trp Glu Asp Leu
965 970 975
Lys Lys Lys Leu Gly Glu Gly Leu Asp Phe Ile Tyr Val Asp Val Trp
980 985 990
Gly Asn Gly Gln Ser Gly Asp Asn Gly Ala Trp Ala Thr His Val Leu
995 1000 1005
Ala Lys Glu Ile Asn Lys Gln Gly Trp Arg Phe Ala Ile Glu Trp
1010 1015 1020
Gly His Gly Gly Glu Tyr Asp Ser Thr Phe Gln His Trp Ala Ala
1025 1030 1035
Asp Leu Thr Tyr Gly Gly Tyr Thr Asn Lys Gly Ile Asn Ser Ala
1040 1045 1050
Ile Thr Arg Phe Ile Arg Asn His Gln Lys Asp Ser Trp Val Gly
1055 1060 1065
Asp Tyr Arg Ser Tyr Gly Gly Ala Ala Asn Tyr Pro Leu Leu Gly
1070 1075 1080
Gly Tyr Ser Met Lys Asp Phe Glu Gly Trp Gln Gly Arg Ser Asp
1085 1090 1095
Tyr Asn Gly Tyr Val Thr Asn Leu Phe Ala His Asp Val Met Thr
1100 1105 1110
Lys Tyr Phe Gln His Phe Thr Val Ser Lys Trp Glu Asn Gly Thr
1115 1120 1125
Pro Val Thr Met Thr Asp Asn Gly Ser Thr Tyr Lys Trp Thr Pro
1130 1135 1140
Glu Met Lys Val Glu Leu Val Asp Ala Ala Gly Asn Lys Val Val
1145 1150 1155
Val Thr Arg Lys Ser Asn Asp Val Asn Ser Pro Gln Tyr Arg Glu
1160 1165 1170
Arg Thr Val Thr Leu Asn Gly Arg Val Ile Gln Asp Gly Ser Ala
1175 1180 1185
Tyr Leu Thr Pro Trp Asn Trp Asp Ala Asn Gly Lys Lys Leu Pro
1190 1195 1200
Thr Glu Lys Glu Lys Met Tyr Tyr Phe Asn Thr Gln Ala Gly Ala
1205 1210 1215
Thr Thr Trp Thr Leu Pro Ser Asp Trp Ala Asn Ser Lys Val Tyr
1220 1225 1230
Leu Tyr Lys Leu Thr Asp Gln Gly Lys Thr Glu Glu Gln Glu Leu
1235 1240 1245
Thr Val Thr Asp Gly Lys Ile Thr Leu Asp Leu Leu Ala Asn Gln
1250 1255 1260
Pro Tyr Val Leu Tyr Arg Ser Lys Gln Thr Asn Pro Glu Met Ser
1265 1270 1275
Trp Ser Glu Gly Met His Ile Tyr Asp Gln Gly Phe Asn Ser Gly
1280 1285 1290
Thr Leu Lys His Trp Thr Ile Ser Gly Asp Ala Ser Lys Ala Glu
1295 1300 1305
Ile Val Lys Ser Gln Gly Ala Asn Glu Met Leu Arg Ile Gln Gly
1310 1315 1320
Asn Lys Ser Lys Val Ser Leu Thr Gln Lys Leu Thr Gly Leu Lys
1325 1330 1335
Pro Asn Thr Lys Tyr Ala Val Tyr Val Gly Val Asp Asn Arg Ser
1340 1345 1350
Asn Ala Lys Ala Ser Ile Thr Val Asn Thr Gly Glu Lys Glu Val
1355 1360 1365
Thr Thr Tyr Thr Asn Lys Ser Leu Ala Leu Asn Tyr Ile Lys Ala
1370 1375 1380
Tyr Ala His Asn Asn Arg Arg Glu Asn Ala Thr Val Asp Asp Thr
1385 1390 1395
Ser Tyr Phe Gln Asn Met Tyr Ala Phe Phe Thr Thr Gly Ser Asp
1400 1405 1410
Val Ser Asn Val Thr Leu Thr Leu Ser Arg Glu Ala Gly Asp Glu
1415 1420 1425
Ala Thr Tyr Phe Asp Glu Ile Arg Thr Phe Glu Asn Asn Ser Ser
1430 1435 1440
Met Tyr Gly Asp Lys His Asp Thr Gly Gln Gly Thr Phe Lys Gln
1445 1450 1455
Asp Phe Glu Asn Val Ala Gln Gly Ile Phe Pro Phe Val Val Gly
1460 1465 1470
Gly Val Glu Gly Val Glu Asp Asn Arg Thr His Leu Ser Glu Lys
1475 1480 1485
His Asp Pro Tyr Thr Gln Arg Gly Trp Asn Gly Lys Lys Val Asp
1490 1495 1500
Asp Val Ile Glu Gly Asn Trp Ser Leu Lys Thr Asn Gly Leu Val
1505 1510 1515
Ser Arg Arg Asn Leu Val Tyr Gln Thr Ile Pro Gln Asn Phe Arg
1520 1525 1530
Phe Glu Ala Gly Lys Thr Tyr Arg Val Thr Phe Glu Tyr Glu Ala
1535 1540 1545
Gly Ser Asp Asn Thr Tyr Ala Phe Val Val Gly Lys Gly Glu Phe
1550 1555 1560
Gln Ser Gly Arg Arg Gly Thr Gln Ala Ser Asn Leu Glu Met His
1565 1570 1575
Glu Leu Pro Asn Thr Trp Thr Asp Ser Lys Lys Ala Lys Lys Val
1580 1585 1590
Thr Phe Leu Val Thr Gly Ala Glu Thr Gly Asp Thr Trp Val Gly
1595 1600 1605
Ile Tyr Ser Thr Gly Asn Ala Ser Asn Thr Arg Gly Asp Ala Gly
1610 1615 1620
Gly Asn Ala Asn Phe Arg Gly Tyr Asn Asp Phe Met Met Asp Asn
1625 1630 1635
Leu Gln Ile Glu Glu Ile Thr Leu Thr Gly Lys Met Leu Thr Glu
1640 1645 1650
Asn Ala Leu Lys Asn Tyr Leu Pro Thr Val Ala Met Thr Asn Tyr
1655 1660 1665
Thr Lys Glu Ser Met Asp Ala Leu Lys Glu Ala Val Phe Asn Leu
1670 1675 1680
Ser Gln Ala Asp Asp Asp Ile Ser Val Glu Glu Ala Arg Ala Glu
1685 1690 1695
Ile Ala Lys Ile Glu Ala Leu Lys Asn Ala Leu Val Gln Lys Lys
1700 1705 1710
Thr Ala Leu Val Ala Glu Asp Phe Glu Ser Leu Asp Ala Pro Ala
1715 1720 1725
Gln Pro Gly Glu Gly Leu Glu Asn Ala Phe Asp Gly Asn Val Ser
1730 1735 1740
Ser Leu Trp His Thr Ser Trp Asn Gly Gly Asp Val Gly Lys Pro
1745 1750 1755
Ala Thr Met Val Leu Lys Glu Pro Thr Glu Ile Thr Gly Leu Arg
1760 1765 1770
Tyr Val Pro Arg Ala Ser Asp Ser Asn Gly Asn Leu Arg Asp Val
1775 1780 1785
Lys Leu Val Val Thr Asp Glu Ser Gly Lys Glu His Thr Phe Asn
1790 1795 1800
Val Thr Asp Trp Pro Asn Asn Asn Lys Pro Lys Asp Ile Asp Phe
1805 1810 1815
Gly Lys Thr Ile Lys Ala Lys Lys Ile Val Leu Thr Gly Thr Lys
1820 1825 1830
Thr Tyr Gly Asp Gly Gly Asp Lys Tyr Gln Ser Ala Ala Glu Leu
1835 1840 1845
Ile Phe Thr Arg Pro Gln Val Ala Glu Thr Pro Leu Asp Leu Ser
1850 1855 1860
Gly Tyr Glu Ala Ala Leu Ala Lys Ala Gln Lys Leu Thr Asp Lys
1865 1870 1875
Asp Asn Gln Glu Glu Val Ala Ser Val Gln Ala Ser Met Lys Tyr
1880 1885 1890
Ala Thr Asp Asn His Leu Leu Thr Glu Arg Met Val Ala Tyr Phe
1895 1900 1905
Ala Asp Tyr Leu Asn Gln Leu Lys Asp Ser Ala Thr Lys Pro Asp
1910 1915 1920
Ala Pro Thr Ser Ser Lys Gly Glu Glu Gln Pro Pro Val Leu Asp
1925 1930 1935
Val Pro Glu Phe Lys Gly Gly Val Asn Ala Thr Glu Ala Ala Val
1940 1945 1950
His Glu Val Pro Glu Phe Lys Gly Gly Val Asn Ala Val Gln Ala
1955 1960 1965
Leu Val His Glu Leu Pro Glu Tyr Lys Gly Gly Ala Asn Ala Val
1970 1975 1980
Leu Ala Ala Ala Asn Glu Val Pro Glu Tyr Lys Gly Gly Ala Asn
1985 1990 1995
Ala Val Glu Ala Leu Val Asn Glu Lys Pro Ala Tyr Thr Gly Val
2000 2005 2010
Leu Ala Thr Ala Gly Asp Gln Ala Ala Pro Thr Val Glu Lys Pro
2015 2020 2025
Glu Tyr Pro Leu Thr Pro Ser Pro Val Ala Asp Thr Lys Thr Pro
2030 2035 2040
Gly Ala Lys Asp Glu Glu Lys Leu Pro Ala
2045 2050
<210> 10
<211> 2065
<212> PRT
<213> Artificial Sequence
<220>
<223> O-glycosidase from S. oralis with additional N terminal Met, C
terminal GSGLE-His6tag, and signal sequence and C terminal
element of LPXTG cell wall anchor motif removed
<400> 10
Met Asp Gln Ala Arg Val Gly Ser Thr Asp Asn Leu Pro Ser Glu Leu
1 5 10 15
Ala Asp Leu Asp Lys Lys Ala Ser Asp Glu Gly His Asp Phe Asp Lys
20 25 30
Glu Ala Ala Ala Gln Asn Pro Gly Ser Ala Glu Thr Thr Glu Gly Pro
35 40 45
Gln Thr Glu Glu Glu Leu Leu Ala Gln Glu Lys Glu Lys Ser Glu Lys
50 55 60
Pro Ser Asn Leu Pro Lys Glu Leu Glu Asp Lys Leu Glu Lys Ala Glu
65 70 75 80
Asp Asn Gly Arg Glu Val Asp Lys Asp Gln Leu Ala Gln Asp Thr Gly
85 90 95
Lys Leu Val Pro Glu Asp Val Ala Lys Thr Thr Asn Gly Glu Leu Asn
100 105 110
Tyr Gly Ala Thr Val Lys Ile Lys Thr Pro Ser Gly Glu Gly Ser Gly
115 120 125
Ile Val Val Ala Lys Asp Leu Val Leu Thr Val Ser His Asn Phe Ile
130 135 140
Lys Asp Ser Gln Glu Gly Asn Ile Arg Lys Val Val Asp Asn Asp Gln
145 150 155 160
Gly Asp Gly Asp Ile Tyr Ser Ile Ser Tyr Pro Gly Leu Pro Asp Val
165 170 175
Lys Phe Ser Lys Lys Asp Ile Ile His Trp Asp Arg Glu Gly Tyr Leu
180 185 190
Lys Gly Phe Lys Asn Asp Leu Ala Leu Val Arg Leu Arg Thr Val Leu
195 200 205
Glu Asn Thr Pro Val Glu Val Thr Lys Lys Pro Val Val Lys Lys Ile
210 215 220
Gly Asp Lys Leu His Val Phe Gly Tyr Pro Glu Gly Lys Leu Asn Pro
225 230 235 240
Ile Val Asn Thr Thr Val Asp Phe Ala Glu Pro Tyr Gly Glu Gly Val
245 250 255
Gln Gly Ile Gly Tyr Gln Gly Gly Lys Pro Gly Ala Ser Gly Gly Gly
260 265 270
Ile Phe Asp Thr Glu Gly Lys Leu Val Gly Val His Gln Asn Gly Val
275 280 285
Val Gly Lys Arg Ser Gly Gly Ile Leu Phe Ser Pro Ala Gln Leu Lys
290 295 300
Trp Ile Gln Asp His Met Gln Gly Ile Ser Ser Val Lys Pro Ala Asp
305 310 315 320
Leu Glu Glu Lys Glu Lys Pro Ala Glu Glu Lys Pro Lys Glu Asp Lys
325 330 335
Pro Ala Ala Ala Lys Pro Glu Thr Pro Lys Ala Val Thr Pro Glu Trp
340 345 350
Gln Thr Val Ala Asn Lys Glu Gln Gln Gly Thr Val Thr Ile Arg Glu
355 360 365
Glu Lys Gly Val Arg Tyr Asn Gln Leu Ser Ser Thr Ala Gln Asn Asp
370 375 380
Asn Asp Gly Lys Pro Ala Leu Phe Glu Lys Gln Gly Leu Thr Val Asp
385 390 395 400
Ala Asn Gly Asn Ala Thr Val Asp Leu Thr Phe Lys Asp Asp Ser Glu
405 410 415
Lys Gly Lys Ser Arg Phe Gly Val Phe Leu Lys Phe Lys Asp Thr Lys
420 425 430
Asn Asn Val Phe Val Gly Tyr Asp Gln Gly Gly Trp Phe Trp Glu Tyr
435 440 445
Lys Thr Pro Gly Asn Ser Thr Trp Tyr Lys Gly Asn Arg Val Ala Ala
450 455 460
Pro Glu Pro Gly Ser Val Asn Arg Leu Ser Ile Thr Leu Lys Ser Asp
465 470 475 480
Gly Gln Leu Asn Ala Ser Asn Asn Asp Val Asn Leu Phe Asp Thr Val
485 490 495
Thr Leu Pro Gly Ala Val Asn Glu Asn Leu Lys Asn Glu Lys Lys Ile
500 505 510
Leu Leu Lys Ala Gly Thr Tyr Ser Asn Asp Arg Thr Val Val Ser Val
515 520 525
Lys Thr Asp Asn Gln Glu Gly Val Lys Ala Asp Asp Thr Pro Ala Gln
530 535 540
Lys Glu Thr Gly Pro Ala Val Asp Asp Ser Lys Val Thr Tyr Asp Thr
545 550 555 560
Ile Gln Ser Lys Val Leu Lys Ala Val Ile Asp Gln Ala Phe Pro Arg
565 570 575
Val Lys Glu Tyr Thr Leu Asn Gly His Thr Leu Pro Gly Gln Val Gln
580 585 590
Gln Phe Asn Gln Val Phe Ile Asn Asn His Arg Ile Thr Pro Glu Val
595 600 605
Thr Tyr Lys Lys Ile Asn Glu Thr Thr Ala Glu Tyr Leu Met Lys Leu
610 615 620
Arg Asp Asp Ala His Leu Ile Asn Ala Glu Met Thr Val Arg Leu Gln
625 630 635 640
Val Val Asp Asn Gln Leu His Phe Asp Val Thr Lys Ile Val Asn His
645 650 655
Asn Gln Val Thr Pro Gly Gln Lys Ile Asp Asp Glu Arg Lys Leu Leu
660 665 670
Ser Thr Ile Ser Phe Leu Gly Asn Ala Leu Val Ser Val Ser Ser Asp
675 680 685
Gln Ala Gly Ala Lys Phe Asp Gly Ala Thr Met Ser Asn Asn Thr His
690 695 700
Val Ser Gly Asp Asp His Ile Asp Val Thr Asn Pro Met Lys Asp Leu
705 710 715 720
Ala Lys Gly Tyr Met Tyr Gly Phe Val Ser Thr Asp Lys Leu Ala Ala
725 730 735
Gly Val Trp Ser Asn Ser Gln Asn Ser Tyr Gly Gly Gly Ser Asn Asp
740 745 750
Trp Thr Arg Leu Thr Ala Tyr Lys Glu Thr Val Gly Asn Ala Asn Tyr
755 760 765
Val Gly Ile His Ser Ser Glu Trp Gln Trp Glu Lys Ala Tyr Lys Gly
770 775 780
Ile Val Phe Pro Glu Tyr Thr Lys Glu Leu Pro Ser Ala Lys Val Val
785 790 795 800
Ile Thr Glu Asp Ala Asn Ala Asp Asn Lys Val Asp Trp Gln Asp Gly
805 810 815
Ala Ile Ala Tyr Arg Ser Ile Met Asn Asn Pro Gln Gly Trp Glu Lys
820 825 830
Val Lys Asp Ile Thr Ala Tyr Arg Ile Ala Met Asn Phe Gly Ser Gln
835 840 845
Ala Gln Asn Pro Phe Leu Met Thr Leu Asp Gly Ile Lys Lys Ile Asn
850 855 860
Leu His Thr Asp Gly Leu Gly Gln Gly Val Leu Leu Lys Gly Tyr Gly
865 870 875 880
Ser Glu Gly His Asp Ser Gly His Leu Asn Tyr Ala Asp Ile Gly Lys
885 890 895
Arg Ile Gly Gly Val Glu Asp Phe Lys Thr Leu Ile Glu Lys Ala Lys
900 905 910
Lys Tyr Gly Ala His Leu Gly Ile His Val Asn Ala Ser Glu Thr Tyr
915 920 925
Pro Glu Ser Lys Tyr Phe Asn Glu Asn Ile Leu Arg Lys Asn Pro Asp
930 935 940
Gly Ser Tyr Ser Tyr Gly Trp Asn Trp Leu Asp Gln Gly Ile Asn Ile
945 950 955 960
Asp Ala Ala Tyr Asp Leu Ala His Gly Arg Leu Ala Arg Trp Glu Asp
965 970 975
Leu Lys Lys Lys Leu Gly Glu Gly Leu Asp Phe Ile Tyr Val Asp Val
980 985 990
Trp Gly Asn Gly Gln Ser Gly Asp Asn Gly Ala Trp Ala Thr His Val
995 1000 1005
Leu Ala Lys Glu Ile Asn Lys Gln Gly Trp Arg Phe Ala Ile Glu
1010 1015 1020
Trp Gly His Gly Gly Glu Tyr Asp Ser Thr Phe Gln His Trp Ala
1025 1030 1035
Ala Asp Leu Thr Tyr Gly Gly Tyr Thr Asn Lys Gly Ile Asn Ser
1040 1045 1050
Ala Ile Thr Arg Phe Ile Arg Asn His Gln Lys Asp Ser Trp Val
1055 1060 1065
Gly Asp Tyr Arg Ser Tyr Gly Gly Ala Ala Asn Tyr Pro Leu Leu
1070 1075 1080
Gly Gly Tyr Ser Met Lys Asp Phe Glu Gly Trp Gln Gly Arg Ser
1085 1090 1095
Asp Tyr Asn Gly Tyr Val Thr Asn Leu Phe Ala His Asp Val Met
1100 1105 1110
Thr Lys Tyr Phe Gln His Phe Thr Val Ser Lys Trp Glu Asn Gly
1115 1120 1125
Thr Pro Val Thr Met Thr Asp Asn Gly Ser Thr Tyr Lys Trp Thr
1130 1135 1140
Pro Glu Met Lys Val Glu Leu Val Asp Ala Ala Gly Asn Lys Val
1145 1150 1155
Val Val Thr Arg Lys Ser Asn Asp Val Asn Ser Pro Gln Tyr Arg
1160 1165 1170
Glu Arg Thr Val Thr Leu Asn Gly Arg Val Ile Gln Asp Gly Ser
1175 1180 1185
Ala Tyr Leu Thr Pro Trp Asn Trp Asp Ala Asn Gly Lys Lys Leu
1190 1195 1200
Pro Thr Glu Lys Glu Lys Met Tyr Tyr Phe Asn Thr Gln Ala Gly
1205 1210 1215
Ala Thr Thr Trp Thr Leu Pro Ser Asp Trp Ala Asn Ser Lys Val
1220 1225 1230
Tyr Leu Tyr Lys Leu Thr Asp Gln Gly Lys Thr Glu Glu Gln Glu
1235 1240 1245
Leu Thr Val Thr Asp Gly Lys Ile Thr Leu Asp Leu Leu Ala Asn
1250 1255 1260
Gln Pro Tyr Val Leu Tyr Arg Ser Lys Gln Thr Asn Pro Glu Met
1265 1270 1275
Ser Trp Ser Glu Gly Met His Ile Tyr Asp Gln Gly Phe Asn Ser
1280 1285 1290
Gly Thr Leu Lys His Trp Thr Ile Ser Gly Asp Ala Ser Lys Ala
1295 1300 1305
Glu Ile Val Lys Ser Gln Gly Ala Asn Glu Met Leu Arg Ile Gln
1310 1315 1320
Gly Asn Lys Ser Lys Val Ser Leu Thr Gln Lys Leu Thr Gly Leu
1325 1330 1335
Lys Pro Asn Thr Lys Tyr Ala Val Tyr Val Gly Val Asp Asn Arg
1340 1345 1350
Ser Asn Ala Lys Ala Ser Ile Thr Val Asn Thr Gly Glu Lys Glu
1355 1360 1365
Val Thr Thr Tyr Thr Asn Lys Ser Leu Ala Leu Asn Tyr Ile Lys
1370 1375 1380
Ala Tyr Ala His Asn Asn Arg Arg Glu Asn Ala Thr Val Asp Asp
1385 1390 1395
Thr Ser Tyr Phe Gln Asn Met Tyr Ala Phe Phe Thr Thr Gly Ser
1400 1405 1410
Asp Val Ser Asn Val Thr Leu Thr Leu Ser Arg Glu Ala Gly Asp
1415 1420 1425
Glu Ala Thr Tyr Phe Asp Glu Ile Arg Thr Phe Glu Asn Asn Ser
1430 1435 1440
Ser Met Tyr Gly Asp Lys His Asp Thr Gly Gln Gly Thr Phe Lys
1445 1450 1455
Gln Asp Phe Glu Asn Val Ala Gln Gly Ile Phe Pro Phe Val Val
1460 1465 1470
Gly Gly Val Glu Gly Val Glu Asp Asn Arg Thr His Leu Ser Glu
1475 1480 1485
Lys His Asp Pro Tyr Thr Gln Arg Gly Trp Asn Gly Lys Lys Val
1490 1495 1500
Asp Asp Val Ile Glu Gly Asn Trp Ser Leu Lys Thr Asn Gly Leu
1505 1510 1515
Val Ser Arg Arg Asn Leu Val Tyr Gln Thr Ile Pro Gln Asn Phe
1520 1525 1530
Arg Phe Glu Ala Gly Lys Thr Tyr Arg Val Thr Phe Glu Tyr Glu
1535 1540 1545
Ala Gly Ser Asp Asn Thr Tyr Ala Phe Val Val Gly Lys Gly Glu
1550 1555 1560
Phe Gln Ser Gly Arg Arg Gly Thr Gln Ala Ser Asn Leu Glu Met
1565 1570 1575
His Glu Leu Pro Asn Thr Trp Thr Asp Ser Lys Lys Ala Lys Lys
1580 1585 1590
Val Thr Phe Leu Val Thr Gly Ala Glu Thr Gly Asp Thr Trp Val
1595 1600 1605
Gly Ile Tyr Ser Thr Gly Asn Ala Ser Asn Thr Arg Gly Asp Ala
1610 1615 1620
Gly Gly Asn Ala Asn Phe Arg Gly Tyr Asn Asp Phe Met Met Asp
1625 1630 1635
Asn Leu Gln Ile Glu Glu Ile Thr Leu Thr Gly Lys Met Leu Thr
1640 1645 1650
Glu Asn Ala Leu Lys Asn Tyr Leu Pro Thr Val Ala Met Thr Asn
1655 1660 1665
Tyr Thr Lys Glu Ser Met Asp Ala Leu Lys Glu Ala Val Phe Asn
1670 1675 1680
Leu Ser Gln Ala Asp Asp Asp Ile Ser Val Glu Glu Ala Arg Ala
1685 1690 1695
Glu Ile Ala Lys Ile Glu Ala Leu Lys Asn Ala Leu Val Gln Lys
1700 1705 1710
Lys Thr Ala Leu Val Ala Glu Asp Phe Glu Ser Leu Asp Ala Pro
1715 1720 1725
Ala Gln Pro Gly Glu Gly Leu Glu Asn Ala Phe Asp Gly Asn Val
1730 1735 1740
Ser Ser Leu Trp His Thr Ser Trp Asn Gly Gly Asp Val Gly Lys
1745 1750 1755
Pro Ala Thr Met Val Leu Lys Glu Pro Thr Glu Ile Thr Gly Leu
1760 1765 1770
Arg Tyr Val Pro Arg Ala Ser Asp Ser Asn Gly Asn Leu Arg Asp
1775 1780 1785
Val Lys Leu Val Val Thr Asp Glu Ser Gly Lys Glu His Thr Phe
1790 1795 1800
Asn Val Thr Asp Trp Pro Asn Asn Asn Lys Pro Lys Asp Ile Asp
1805 1810 1815
Phe Gly Lys Thr Ile Lys Ala Lys Lys Ile Val Leu Thr Gly Thr
1820 1825 1830
Lys Thr Tyr Gly Asp Gly Gly Asp Lys Tyr Gln Ser Ala Ala Glu
1835 1840 1845
Leu Ile Phe Thr Arg Pro Gln Val Ala Glu Thr Pro Leu Asp Leu
1850 1855 1860
Ser Gly Tyr Glu Ala Ala Leu Ala Lys Ala Gln Lys Leu Thr Asp
1865 1870 1875
Lys Asp Asn Gln Glu Glu Val Ala Ser Val Gln Ala Ser Met Lys
1880 1885 1890
Tyr Ala Thr Asp Asn His Leu Leu Thr Glu Arg Met Val Ala Tyr
1895 1900 1905
Phe Ala Asp Tyr Leu Asn Gln Leu Lys Asp Ser Ala Thr Lys Pro
1910 1915 1920
Asp Ala Pro Thr Ser Ser Lys Gly Glu Glu Gln Pro Pro Val Leu
1925 1930 1935
Asp Val Pro Glu Phe Lys Gly Gly Val Asn Ala Thr Glu Ala Ala
1940 1945 1950
Val His Glu Val Pro Glu Phe Lys Gly Gly Val Asn Ala Val Gln
1955 1960 1965
Ala Leu Val His Glu Leu Pro Glu Tyr Lys Gly Gly Ala Asn Ala
1970 1975 1980
Val Leu Ala Ala Ala Asn Glu Val Pro Glu Tyr Lys Gly Gly Ala
1985 1990 1995
Asn Ala Val Glu Ala Leu Val Asn Glu Lys Pro Ala Tyr Thr Gly
2000 2005 2010
Val Leu Ala Thr Ala Gly Asp Gln Ala Ala Pro Thr Val Glu Lys
2015 2020 2025
Pro Glu Tyr Pro Leu Thr Pro Ser Pro Val Ala Asp Thr Lys Thr
2030 2035 2040
Pro Gly Ala Lys Asp Glu Glu Lys Leu Pro Ala Gly Ser Gly Leu
2045 2050 2055
Glu His His His His His His
2060 2065
<210> 11
<211> 361
<212> PRT
<213> Akkermansia muciniphila
<400> 11
Glu Val Thr Val Pro Asp Ala Leu Lys Asp Arg Ile Ala Leu Lys Lys
1 5 10 15
Thr Ala Arg Gln Leu Asn Ile Val Tyr Phe Leu Gly Ser Asp Thr Glu
20 25 30
Pro Val Pro Asp Tyr Glu Arg Arg Leu Ser Glu Leu Leu Leu Tyr Leu
35 40 45
Gln Gln Phe Tyr Gly Lys Glu Met Gln Arg His Gly Tyr Gly Ala Arg
50 55 60
Ser Phe Gly Leu Asp Ile Lys Ser Pro Gly Arg Val Asn Ile Ile Glu
65 70 75 80
Tyr Lys Ala Lys Asn Pro Ala Ala His Tyr Pro Tyr Glu Asn Gly Gly
85 90 95
Gly Trp Lys Ala Ala Gln Glu Leu Asp Glu Phe Phe Lys Ala His Pro
100 105 110
Asp Arg Lys Lys Ser Gln His Thr Leu Ile Ile Met Pro Thr Trp Asn
115 120 125
Asp Glu Lys Asn Gly Pro Asp Asn Pro Gly Gly Val Pro Phe Tyr Gly
130 135 140
Met Gly Arg Asn Cys Phe Ala Leu Asp Tyr Pro Ala Phe Asp Ile Lys
145 150 155 160
His Leu Gly Gln Lys Thr Arg Glu Gly Arg Leu Leu Thr Lys Trp Tyr
165 170 175
Gly Gly Met Ala His Glu Leu Gly His Gly Leu Asn Leu Pro His Asn
180 185 190
His Gln Thr Ala Ser Asp Gly Lys Lys Tyr Gly Thr Ala Leu Met Gly
195 200 205
Ser Gly Asn Tyr Thr Phe Gly Thr Ser Pro Thr Phe Leu Thr Pro Ala
210 215 220
Ser Cys Ala Leu Leu Asp Ala Cys Glu Val Phe Ser Val Thr Pro Ser
225 230 235 240
Gln Gln Phe Tyr Glu Gly Lys Pro Glu Val Glu Val Gly Asp Val Ala
245 250 255
Ile Ser Phe Lys Gly Asp Gln Ile Leu Val Ser Gly Asn Tyr Lys Ser
260 265 270
Pro Gln Thr Val Lys Ala Leu Asn Val Tyr Ile Gln Asp Pro Pro Tyr
275 280 285
Ala Val Asn Gln Asp Tyr Asp Ala Val Ser Phe Ser Arg Arg Leu Gly
290 295 300
Lys Lys Ser Gly Lys Phe Ser Met Lys Ile Asp Lys Lys Glu Leu Glu
305 310 315 320
Gly Leu Asn Asn Asn Glu Phe Arg Ile Ser Leu Met Phe Ile Leu Ala
325 330 335
Asn Gly Leu His Met Gln Lys His Phe Thr Phe His Trp Asp Ala Leu
340 345 350
Gln Asp Tyr Arg Asp Gly Ser Lys Ser
355 360
<210> 12
<211> 371
<212> PRT
<213> Artificial Sequence
<220>
<223> O-glycoprotein-specific endoprotease (LS)
<400> 12
Met Glu Val Thr Val Pro Asp Ala Leu Lys Asp Arg Ile Ala Leu Lys
1 5 10 15
Lys Thr Ala Arg Gln Leu Asn Ile Val Tyr Phe Leu Gly Ser Asp Thr
20 25 30
Glu Pro Val Pro Asp Tyr Glu Arg Arg Leu Ser Glu Leu Leu Leu Tyr
35 40 45
Leu Gln Gln Phe Tyr Gly Lys Glu Met Gln Arg His Gly Tyr Gly Ala
50 55 60
Arg Ser Phe Gly Leu Asp Ile Lys Ser Pro Gly Arg Val Asn Ile Ile
65 70 75 80
Glu Tyr Lys Ala Lys Asn Pro Ala Ala His Tyr Pro Tyr Glu Asn Gly
85 90 95
Gly Gly Trp Lys Ala Ala Gln Glu Leu Asp Glu Phe Phe Lys Ala His
100 105 110
Pro Asp Arg Lys Lys Ser Gln His Thr Leu Ile Ile Met Pro Thr Trp
115 120 125
Asn Asp Glu Lys Asn Gly Pro Asp Asn Pro Gly Gly Val Pro Phe Tyr
130 135 140
Gly Met Gly Arg Asn Cys Phe Ala Leu Asp Tyr Pro Ala Phe Asp Ile
145 150 155 160
Lys His Leu Gly Gln Lys Thr Arg Glu Gly Arg Leu Leu Thr Lys Trp
165 170 175
Tyr Gly Gly Met Ala His Glu Leu Gly His Gly Leu Asn Leu Pro His
180 185 190
Asn His Gln Thr Ala Ser Asp Gly Lys Lys Tyr Gly Thr Ala Leu Met
195 200 205
Gly Ser Gly Asn Tyr Thr Phe Gly Thr Ser Pro Thr Phe Leu Thr Pro
210 215 220
Ala Ser Cys Ala Leu Leu Asp Ala Cys Glu Val Phe Ser Val Thr Pro
225 230 235 240
Ser Gln Gln Phe Tyr Glu Gly Lys Pro Glu Val Glu Val Gly Asp Val
245 250 255
Ala Ile Ser Phe Lys Gly Asp Gln Ile Leu Val Ser Gly Asn Tyr Lys
260 265 270
Ser Pro Gln Thr Val Lys Ala Leu Asn Val Tyr Ile Gln Asp Pro Pro
275 280 285
Tyr Ala Val Asn Gln Asp Tyr Asp Ala Val Ser Phe Ser Arg Arg Leu
290 295 300
Gly Lys Lys Ser Gly Lys Phe Ser Met Lys Ile Asp Lys Lys Glu Leu
305 310 315 320
Glu Gly Leu Asn Asn Asn Glu Phe Arg Ile Ser Leu Met Phe Ile Leu
325 330 335
Ala Asn Gly Leu His Met Gln Lys His Phe Thr Phe His Trp Asp Ala
340 345 350
Leu Gln Asp Tyr Arg Asp Gly Ser Lys Ser Gly Ser Gly His His His
355 360 365
His His His
370
<210> 13
<211> 6198
<212> DNA
<213> Artificial Sequence
<220>
<223> Nucleotide encoding O-glycosidase from S. oralis (additional N
terminal Met, C terminal GSGLE-His6tag, and signal sequence and C
terminal element of LPXTG cell wall anchor motif removed)
<400> 13
atggaccaag cgcgtgtggg tagcaccgat aacctgccga gcgagctggc ggatctggac 60
aagaaagcga gcgacgaagg ccacgatttt gacaaagagg cggcggcgca gaacccgggt 120
agcgcggaaa ccaccgaagg tccgcagacc gaggaagagc tgctggcgca agaaaaagag 180
aagagcgaga agccgagcaa cctgccgaaa gaactggagg ataaactgga aaaggcggag 240
gacaacggtc gtgaagtgga taaagaccag ctggcgcaag acaccggcaa gctggtgccg 300
gaggatgttg cgaaaaccac caacggtgaa ctgaactacg gcgcgaccgt taaaattaag 360
accccgagcg gcgagggtag cggtattgtg gttgcgaagg acctggtgct gaccgttagc 420
cacaacttca ttaaggatag ccaggaaggt aatatccgta aagtggttga taacgaccaa 480
ggcgatggtg acatctacag cattagctat ccgggcctgc cggacgttaa gttcagcaag 540
aaagatatca tccactggga ccgtgagggt tacctgaaag gcttcaagaa cgatctggcg 600
ctggtgcgtc tgcgtaccgt tctggaaaac accccggttg aggtgaccaa gaaaccggtg 660
gttaagaaaa ttggtgacaa gctgcacgtg tttggttatc cggagggcaa actgaacccg 720
atcgtgaaca ccaccgttga tttcgcggaa ccgtacggcg agggtgttca gggcattggt 780
tatcaaggtg gcaaaccggg cgcgagcggt ggcggtatct ttgacaccga aggcaagctg 840
gttggcgtgc accagaacgg tgtggttggc aaacgtagcg gcggtattct gttcagcccg 900
gcgcaactga agtggattca ggaccacatg caaggtatca gcagcgtgaa accggcggat 960
ctggaagaga aagagaagcc ggcggaagag aaaccgaagg aagacaagcc ggcggcggcg 1020
aagccggaaa ccccgaaagc ggttaccccg gagtggcaaa ccgtggcgaa caaggaacag 1080
caaggtaccg ttaccatccg tgaagagaaa ggcgtgcgtt acaaccagct gagcagcacc 1140
gcgcaaaacg ataacgacgg caagccggcg ctgtttgaga aacagggtct gaccgttgac 1200
gcgaacggca acgcgaccgt ggatctgacc ttcaaggacg atagcgaaaa aggcaagagc 1260
cgtttcggcg tttttctgaa attcaaggac accaaaaaca acgtttttgt gggttacgat 1320
caaggcggtt ggttctggga gtataagacc ccgggtaaca gcacctggta caagggtaac 1380
cgtgtggcgg cgccggaacc gggtagcgtg aaccgtctga gcattaccct gaaaagcgac 1440
ggccagctga acgcgagcaa caacgatgtg aacctgttcg acaccgttac cctgccgggt 1500
gcggtgaacg aaaacctgaa gaacgagaag aaaatcctgc tgaaagcggg cacctacagc 1560
aacgaccgta ccgtggttag cgttaagacc gataaccagg aaggtgtgaa agcggacgat 1620
accccggcgc aaaaggaaac cggtccggcg gtggacgata gcaaggttac ctacgacacc 1680
attcagagca aagtgctgaa ggcggttatc gatcaagcgt ttccgcgtgt gaaagagtat 1740
accctgaacg gtcacaccct gccgggtcag gttcagcaat ttaaccaagt gttcattaac 1800
aaccaccgta tcaccccgga agtgacctat aagaaaatta acgaaaccac cgcggagtac 1860
ctgatgaagc tgcgtgacga tgcgcacctg atcaacgcgg aaatgaccgt gcgtctgcag 1920
gtggttgata accaactgca cttcgacgtg accaaaattg ttaaccacaa ccaggttacc 1980
ccgggtcaaa agattgacga tgagcgtaaa ctgctgagca ccatcagctt tctgggcaac 2040
gcgctggtta gcgtgagcag cgatcaagcg ggtgcgaagt ttgatggtgc gaccatgagc 2100
aacaacaccc acgttagcgg tgacgatcac atcgatgtga ccaacccgat gaaagacctg 2160
gcgaagggtt acatgtatgg ctttgttagc accgacaagc tggcggcggg tgtgtggagc 2220
aacagccaaa acagctacgg cggtggcagc aacgattgga cccgtctgac cgcgtataaa 2280
gaaaccgttg gtaacgcgaa ctacgtgggc attcacagca gcgaatggca gtgggagaaa 2340
gcgtacaagg gtatcgtgtt cccggaatat accaaggagc tgccgagcgc gaaagtggtt 2400
atcaccgagg atgcgaacgc ggacaacaaa gtggattggc aggacggtgc gattgcgtac 2460
cgtagcatca tgaacaaccc gcaaggctgg gaaaaagtta aggacattac cgcgtatcgt 2520
atcgcgatga actttggtag ccaggcgcaa aacccgttcc tgatgaccct ggacggcatc 2580
aagaaaatta acctgcacac cgatggcctg ggtcagggcg ttctgctgaa gggttatggt 2640
agcgagggtc atgacagcgg tcacctgaac tacgcggata tcggtaaacg tattggtggc 2700
gtggaagact ttaagaccct gattgagaaa gcgaagaaat acggtgcgca cctgggcatc 2760
cacgttaacg cgagcgaaac ctacccggag agcaagtatt tcaacgaaaa cattctgcgt 2820
aaaaacccgg acggtagcta cagctatggc tggaactggc tggatcaggg tatcaacatt 2880
gatgcggcgt acgacctggc gcatggccgt ctggcgcgtt gggaggacct gaagaaaaag 2940
ctgggtgaag gcctggattt tatctatgtt gacgtgtggg gtaacggtca gagcggtgat 3000
aacggtgcgt gggcgaccca tgtgctggcg aaagagatta acaagcaagg ttggcgtttt 3060
gcgatcgaat ggggccacgg tggcgagtac gacagcacct tccagcactg ggcggcggat 3120
ctgacctacg gtggctatac caacaagggt atcaacagcg cgattacccg tttcatccgt 3180
aaccaccaga aagatagctg ggttggcgac taccgtagct atggtggcgc ggcgaactac 3240
ccgctgctgg gtggctatag catgaaggac tttgagggtt ggcaaggccg tagcgattac 3300
aacggttatg ttaccaacct gttcgcgcac gacgtgatga ccaagtactt tcagcacttc 3360
accgttagca aatgggaaaa cggtaccccg gtgaccatga ccgataacgg cagcacctat 3420
aagtggaccc cggaaatgaa agtggagctg gttgacgcgg cgggtaacaa ggtggttgtg 3480
acccgtaaaa gcaacgatgt gaacagcccg cagtaccgtg agcgtaccgt taccctgaac 3540
ggtcgtgtga tccaagacgg cagcgcgtat ctgaccccgt ggaactggga tgcgaacggt 3600
aaaaagctgc cgaccgaaaa agagaagatg tactatttta acacccaagc gggtgcgacc 3660
acctggaccc tgccgagcga ctgggcgaac agcaaggttt acctgtataa actgaccgat 3720
cagggcaaga ccgaggagca agaactgacc gtgaccgatg gcaaaattac cctggacctg 3780
ctggcgaacc agccgtacgt tctgtatcgt agcaagcaaa ccaacccgga aatgagctgg 3840
agcgagggta tgcacatcta cgaccaaggt ttcaacagcg gcaccctgaa acactggacc 3900
attagcggcg atgcgagcaa ggcggagatc gtgaaaagcc agggtgcgaa cgaaatgctg 3960
cgtatccaag gcaacaaaag caaggttagc ctgacccaga agctgaccgg tctgaaaccg 4020
aacaccaagt acgcggttta tgtgggcgtt gacaaccgta gcaacgcgaa agcgagcatt 4080
accgttaaca ccggtgaaaa agaggtgacc acctacacca acaagagcct ggcgctgaac 4140
tacatcaaag cgtatgcgca caacaaccgt cgtgagaacg cgaccgtgga cgataccagc 4200
tacttccaga acatgtatgc gttctttacc accggtagcg acgtgagcaa cgttaccctg 4260
accctgagcc gtgaagcggg cgatgaggcg acctattttg acgaaattcg taccttcgag 4320
aacaacagca gcatgtacgg tgataagcac gacaccggtc agggcacctt taaacaagat 4380
ttcgaaaacg ttgcgcaagg tatcttcccg tttgttgtgg gtggcgtgga aggcgttgag 4440
gacaaccgta cccacctgag cgagaagcac gatccgtaca cccagcgtgg ttggaacggc 4500
aaaaaggtgg acgatgttat tgagggtaac tggagcctga aaaccaacgg cctggttagc 4560
cgtcgtaacc tggtgtacca gaccatcccg caaaacttcc gttttgaggc gggcaagacc 4620
taccgtgtga cctttgaata tgaggcgggc agcgacaaca cctatgcgtt tgttgtgggt 4680
aaaggcgaat tccagagcgg tcgtcgtggc acccaagcga gcaacctgga aatgcacgag 4740
ctgccgaaca cctggaccga tagcaaaaag gcgaaaaagg tgaccttcct ggttaccggt 4800
gcggaaaccg gtgacacctg ggtgggtatc tacagcaccg gcaacgcgag caacacccgt 4860
ggtgatgcgg gtggcaacgc gaactttcgt ggctataacg atttcatgat ggacaacctg 4920
caaatcgaag agattaccct gaccggcaag atgctgaccg aaaacgcgct gaaaaactat 4980
ctgccgaccg ttgcgatgac caactacacc aaggaaagca tggacgcgct gaaagaggcg 5040
gttttcaacc tgagccaggc ggacgatgac atcagcgtgg aagaggcgcg tgcggaaatc 5100
gcgaagattg aggcgctgaa aaacgcgctg gttcagaaaa agaccgcgct ggttgcggaa 5160
gattttgaga gcctggatgc gccggcgcaa ccgggtgaag gcctggagaa cgcgttcgac 5220
ggtaacgtta gcagcctgtg gcacaccagc tggaacggtg gcgatgttgg caagccggcg 5280
accatggtgc tgaaagaacc gaccgagatc accggtctgc gttatgtgcc gcgtgcgagc 5340
gatagcaacg gcaacctgcg tgacgttaag ctggttgtga ccgatgaaag cggtaaagag 5400
cacaccttta acgtgaccga ctggccgaac aacaacaaac cgaaggatat tgacttcggc 5460
aaaaccatta aggcgaaaaa gatcgttctg accggtacca agacctacgg cgatggtggc 5520
gacaaatatc agagcgcggc ggagctgatc tttacccgtc cgcaagtggc ggaaaccccg 5580
ctggatctga gcggttacga agcggcgctg gcgaaagcgc agaagctgac cgataaggac 5640
aaccaggaag aggtggcgag cgttcaagcg agcatgaaat atgcgaccga caaccacctg 5700
ctgaccgaac gtatggttgc gtacttcgcg gattatctga accaactgaa ggatagcgcg 5760
accaaaccgg atgcgccgac cagcagcaag ggtgaagaac agccgccggt gctggatgtt 5820
ccggagttta aaggtggcgt gaacgcgacc gaggcggcgg tgcacgaagt tccggagttc 5880
aagggtggcg tgaacgcggt tcaggcgctg gttcacgaac tgccggagta taaaggtggc 5940
gcgaacgcgg ttctggcggc ggcgaacgaa gtgccggagt acaagggtgg cgcgaacgcg 6000
gtggaagcgc tggttaacga gaaaccggcg tataccggtg ttctggcgac cgcgggcgac 6060
caggcggcgc cgaccgtgga aaaaccggag tacccgctga ccccgagccc ggttgcggac 6120
accaaaaccc cgggtgcgaa agatgaagag aagctgccgg cgggtagcgg cctcgagcac 6180
caccaccacc accactga 6198
Claims (12)
- 이하의 것들로부터 독립적으로 선택되는 제1 시알리다제를 포함하는 조성물로서:
(a) 서열번호 2의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
(b) 서열번호 2의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
(c) 서열번호 2의 서열의 절편인 아미노산 서열, 또는 서열번호 2의 아미노산 서열과 85% 동일한 아미노산의 절편을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
선택적으로, 상기 제1 시알리다제는 N 말단에서의 추가적인 메티오닌, 및/또는 C 말단에서의 히스티딘 태그를 포함하며, 상기 태그는 링커에 의해 C 말단에 연결될 수 있는, 조성물. - 제1항에 있어서, 이하의 것들로부터 독립적으로 선택되는 제2 시알리다제를 추가로 포함하는 조성물로서:
(d) 서열번호 5의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
(e) 서열번호 5의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
(f) 서열번호 5의 서열의 절편인 아미노산 서열, 또는 서열번호 5의 아미노산 서열과 85% 동일한 아미노산의 절편을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
선택적으로, 상기 제2 시알리다제는 N 말단에서의 추가적인 메티오닌 및/또는 C 말단에서의 히스티딘 태그를 포함하고, 상기 태그는 링커에 의해 C 말단에 연결될 수 있는, 조성물. - 제2항에 있어서, 당단백질, 바람직하게는 천연의 비-변성된 상태의 당단백질에서 시알산 결합의 >90%를 가수분해할 수 있는, 조성물.
- 제1항 내지 제3항 중 어느 한 항에 있어서, 서열번호 3의 아미노산 서열로 이루어지는 시알리다제, 및 서열번호 6의 아미노산 서열로 이루어지는 시알리다제를, 바람직하게는 1:1 비로 포함하는, 조성물.
- 제1항 내지 제4항 중 어느 한 항에 있어서, 제1 시알리다제 및/또는 제2 시알리다제는 매우 정제된, 또는 분리된 형태로 존재하며; 및/또는 여기에서 상기 조성물 중 2개 이하의 폴리펩티드는 아커만시아 뮤시니필라(Akkermansia muciniphila)로부터 획득한 시알리다제인, 조성물.
- 제1항 내지 제5항 중 어느 한 항에 있어서, 추가적으로 글리코시다제 및/또는 프로테아제를 포함하되, 선택적으로 매우 정제된 또는 분리된 형태로 존재하는, 조성물.
- 제6항에 있어서, 상기 글리코시다제는 이하의 것들로부터 선택된 O-글리코시다제이며:
a. 서열번호 9의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
b. 서열번호 9와 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
c. 서열번호 9의 서열의 절편, 또는 서열번호 9의 서열과 85% 동일한 서열의 절편인 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
d. 엔테로코커스 패칼리스(Enterococcus faecalis)로부터의 O-글리코시다제, 선택적으로 Uniprot 엔트리 B5UB72 버전 22의 아미노산 서열을 갖는 폴리펩티드;
선택적으로, 상기 글리코시다제는 서열번호 10의 아미노산 서열로 이루어지는, 조성물. - 제6항 또는 제7항에 있어서, 상기 프로테아제는 이하의 것들로부터 선택된 O-당단백질-특이적인 엔도프로테아제이고:
a. 서열번호 11의 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
b. 서열번호 11의 아미노산 서열과 적어도 85% 동일한 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드; 또는
c. 서열번호 11의 서열의 절편, 또는 서열번호 11의 아미노산 서열과 85% 동일한 서열의 절편인 아미노산 서열을 포함하거나 또는 이로써 이루어지는 폴리펩티드;
선택적으로, 상기 프로테아제는 서열번호 12의 아미노산 서열로 이루어지는, 조성물. - 당단백질을 변형시키는 방법으로서, 당단백질을 함유하는 샘플을 제1항 내지 제8항 중 어느 한 항에 의한 조성물과 접촉시키는 단계를 포함하되, 선택적으로 생성되는 산물이 분석되는, 방법.
- 제9항에 있어서, 상기 분석은 SDS-PAGE, HPLC, 렉틴 블로팅, ELISA 또는 질량 분광분석법을 포함하는 임의의 적합한 수단에 의한 산물의 분리(separation) 및/또는 탐지 및/또는 단리(isolation)를 포함하는, 방법.
- 제9항 또는 제10항에 있어서, 상기 조성물은 제1항 내지 제4항 중 어느 한 항에서 정의된 바와 같고, 상기 방법은 당단백질이 상기 조성물과 접촉되기 전 또는 후에, 상기 샘플을 프로테아제 또는 글리코시다제와 동시에 접촉시키는 단계를 포함하는, 방법.
- 제9항에 있어서, 상기 글리코시다제는 선택적으로 제7항에서 정의된 바와 같은 O-글리코시다제이고; 및/또는 상기 프로테아제는 선택적으로 제8항에서 정의된 바와 같은 엔도프로테아제인, 방법.
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