KR101642499B1 - 수용성 파스튜렐라 멀토시다 독소를 포함하는 재조합 융합 단백질, 면역원성 조성물 및 이의 제조방법 - Google Patents
수용성 파스튜렐라 멀토시다 독소를 포함하는 재조합 융합 단백질, 면역원성 조성물 및 이의 제조방법 Download PDFInfo
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- KR101642499B1 KR101642499B1 KR1020140001673A KR20140001673A KR101642499B1 KR 101642499 B1 KR101642499 B1 KR 101642499B1 KR 1020140001673 A KR1020140001673 A KR 1020140001673A KR 20140001673 A KR20140001673 A KR 20140001673A KR 101642499 B1 KR101642499 B1 KR 101642499B1
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Abstract
본 발명은 수용성 파스튜렐라 멀토시다 독소(Pasteurella multocida toxin(PMT))를 포함하는 재조합 융합 단백질, 면역원성 조성물 및 이의 제조방법에 관한 것이다. 본 발명에 따른 재조합 융합 단백질은 수용성일 뿐만 아니라, 기존 PMT 단백질에 비해 독소활성 및 면역원성이 더 높으며, 위축성 비염에 효과적인 면역원성 조성물 또는 유전자 재조합 백신의 첨가제로서 활용될 수 있고, 2차 감염을 더욱 효과적으로 예방할 수 있다.
Description
본 발명은 수용성 파스튜렐라 멀토시다 독소(Pasteurella multocida toxin(PMT))를 포함하는 재조합 융합 단백질, 면역원성 조성물 및 이의 제조방법에 관한 것이다.
돼지의 위축성 비염(Atropic Rhinitis, AR)은 돼지의 3대 호흡기병 중의 하나로 코비틀림, 안면이상, 비출혈 등이 나타나며 전염성이 크고 증체율이 저하되어 경제적 손실이 크다. 이 질병의 원인균인 파스튜렐라 멀토시다 혈청군 A와 B의 캡슐은 숙주의 면역세포에 의한 포식작용에서 벗어날 수 있게 도와주고, 캡슐 타입 A는 보체가 매개하는 용균현상에 저항할 수 있도록 해준다(Chung JY et al., Role of capsule in the pathogenesis of fowl cholera caused by P. multocida serotype A, Infect Immun 2001, 69(4): 2487-2492). 또한, 혈청군 A의 경우 위축성 비염, 마이코플라즈마성 폐렴 등을 포함한 모든 호흡기 질병에 의한 감염이나, 사육 환경, 화학물질에 의한 자극 등 다양한 인자들에 의해 돼지의 면역력이 약해졌을 때, 잠복해 있던 균이 증식하면서 2차 감염균으로 작용하여 병원성을 나타낸다. 위축성 비염을 일으키는 다른 주요 병원체로는 보르데텔라 브론키셉티카(Bordetella bronchiseptica)가 알려져 있다. 보르데텔라 브론키셉티카의 감염에 의해 유발되는 위축성 비염은 파스튜렐라 멀토시다에 의한 것보다 상대적으로 병원성이 약하며, 두 병원균의 복합 감염은 병변을 더욱 악화시키는 것으로 알려져 있다 (Rutter, J.M. et al., Atropic rhinitis in gnobiotic piglets: differences in the pathogenicity of Pasteurella multocida in combined infections with Bordetella bronchiseptica, Vet. Res. 1982, 110, 531-535). 하지만 이 질병을 일으키는 가장 큰 원인은 균체내 독소인 파스튜렐라 멀토시다 독소(PMT)이다. PMT는 Rho GTPases를 활성화시키고, 액틴 스트레스 섬유 (actin stress fiber) 형성에 중요하다. 스트레스 섬유 (stress fiber)의 형성은 파스튜렐라 멀토시다의 엔도시토시스(endocytosis)에 도움을 줄 것으로 보여진다. 따라서 이 독소에 대한 면역항체를 형성시키면 위축성 비염 감염시 더욱 효과적인 방어능을 보인다. 그러나, 이 독소를 얻기 위해 균체를 깨뜨려서 그 안의 독소를 분리하는 방법이 일반적으로 사용되고 있으나, 이러한 방법은 대량생산이 어렵고 순수한 독소를 얻는데 한계가 있다.
이에, 본 발명은 유전자 재조합 기술을 이용하여 위축성 비염의 가장 큰 원인인 파스튜렐라 멀토시다 타입 D의 독소를 생산할 수 있는 기술을 개발하여 순수한 독소를 짧은 시간에 대량생산하고, 이 독소에 파스튜렐라 멀토시다 타입 A 균체를 혼합한 백신을 제공한다.
본 발명의 목적은, 수용성 발현 촉진 단백질 및 외래 단백질을 포함하는 재조합 융합 단백질, 이의 제조방법 및 위축성 비염을 치료 또는 예방하기 위한 상기 재조합 융합 단백질을 포함하는 면역원성 조성물을 제공하는 것이다.
본 발명은 상기 목적을 달성하기 위하여, LysRS (lysyl-tRNA synthetase) 및 파스튜렐라 멀토시다 독소(Pasteurella multocida toxin, PMT)를 포함하는 서열번호 1로 구성된 재조합 융합 단백질을 제공한다.
본 발명의 일 구체예에서, 상기 재조합 융합 단백질은 수용성 발현 촉진 단백질과 외래 단백질 사이에 단백질 절단효소 인식 부위가 존재하는 것을 특징으로 할 수 있다. 또한, 상기 수용성 발현 촉진 단백질은 외래 단백질의 N 말단에 연결되어 있는 것을 특징으로 할 수 있다. 그리고, 단백질의 분리를 위한 태그는 외래 단백질의 C 말단에 연결되어 있는 것을 특징으로 할 수 있다. 또한, 상기 LysRS는 대장균으로부터 유래한 것일 수 있다.
또한, 상기 재조합 융합 단백질은 다른 단백질과 융합되지 않은 PMT에 비해 독소 활성과 면역원성이 증가한 것을 특징으로 할 수 있다. 본 발명에 따른 재조합 융합 단백질은 비융합 PMT에 비해 독소 활성 또는 면역원성이 15% 이상, 바람직하게는 20% 이상 증가할 수 있다.
본 발명의 일 구체예에서, 위축성 비염을 치료 또는 예방하기 위한 상기 재조합 융합 단백질을 포함하는 면역원성 조성물이 제공된다.
또한, 본 발명의 일 구체예에서, LysRS를 코딩하는 유전자 및 파스튜렐라 멀토시다 독소를 코딩하는 유전자를 포함하는 재조합 융합 단백질 생산용 발현벡터 및 상기 벡터로 형질전환된 숙주세포가 제공된다. 본 발명의 일 구체예에서 숙주세포는 대장균 KCTC 12477BP일 수 있다.
본 발명에서 사용된 용어 "외래 단백질"은 당업자가 다량으로 생산하고자 하는 단백질로서, 재조합 발현벡터에 상기 단백질을 코딩하는 뉴클레오티드를 삽입하여 형질전환체에서 발현이 가능한 모든 단백질을 의미한다.
본 발현에서 사용된 용어 "재조합 융합 단백질"은 원래의 외래단백질의 서열의 N 말단 또는 C 말단에 다른 단백질이 연결되거나 다른 아미노산 서열이 부가된 단백질을 의미한다.
본 발명에서 사용된 용어 "발현벡터"는 발현벡터의 전사에 제공되는 추가단편에 작동가능하게 연결된 관심의 폴리펩티드를 암호화하는 단편으로 구성되는 선형 또는 원형의 DNA 분자이다. 그와 같은 추가단편은 프로모터 및 종료암호 서열을 포함한다. 발현벡터는 하나 이상의 복제 개시점, 하나 이상의 선택마커 등을 또한 포함한다. 발현벡터는 일반적으로 플라스미드 또는 바이러스 DNA로부터 유도되거나 또는 둘 다의 요소를 함유한다.
본 발명에서 사용된 용어 "수용성 발현 촉진 단백질"은 융합 단백질을 수용성 형태로 발현시킬 수 있다고 보고된 펩타이드를 말하고 GST(Glutathione S transferase), 말토오스 결합단백질, 유비퀴틴, 티오레독신 등이 포함되며, 본 발명에서는 이에 한정되지 않고 일반적으로 알려진 수용성 발현 촉진 단백질이면 제한 없이 사용된다.
본 발명에 따른 재조합 융합 단백질은 수용성일 뿐만 아니라, 기존 PMT 단백질에 비해 독소활성 및 면역원성이 더 높으며, 위축성 비염에 효과적인 면역원성 조성물 또는 유전자 재조합 백신의 첨가제로서 활용될 수 있고, 2차 감염을 더욱 효과적으로 예방할 수 있다.
도 1은 PMT 융합 단백질의 모식도(LysRS-PMT)을 나타낸 것이다.
도 2는 대장균에서의 LysRS-PMT의 발현 결과를 나타낸 것이다.
도 3은 대장균에서의 PMT의 발현 결과를 나타낸 것이다.
도 4은 LysRS-PMT의 니켈 친화성(affinity) 크로마토그래피를 이용한 정제결과를 확인한 것이다.
도 5는 분리된 LysRS-PMT의 SDS-PAGE 분석결과를 나타낸 것이다.
도 6은 E. coli의 LysRS와 P. multocida의 LysRS의 상동성(homology)를 비교한 것이다.
도 7은 마우스에 PMT 및 LysRS-PMT를 각각 접종하여 면역원성을 비교한 결과를 나타낸 것이다.
도 2는 대장균에서의 LysRS-PMT의 발현 결과를 나타낸 것이다.
도 3은 대장균에서의 PMT의 발현 결과를 나타낸 것이다.
도 4은 LysRS-PMT의 니켈 친화성(affinity) 크로마토그래피를 이용한 정제결과를 확인한 것이다.
도 5는 분리된 LysRS-PMT의 SDS-PAGE 분석결과를 나타낸 것이다.
도 6은 E. coli의 LysRS와 P. multocida의 LysRS의 상동성(homology)를 비교한 것이다.
도 7은 마우스에 PMT 및 LysRS-PMT를 각각 접종하여 면역원성을 비교한 결과를 나타낸 것이다.
재료의 준비
파스튜렐라 멀토시다 독소를 코딩하는 DNA는 중앙백신 연구소로부터 얻었고, DNA 재조합을 위한 제한효소는 NEB(영국)로부터 구매하였다. 분리를 위한 컬럼은 GE Healthcare에서 구매하였다.
단백질 발현
플라스미드의
제작
LysRS-PMT 융합 단백질을 발현시킬 수 있는 pGE-LysRS-PMT 발현 벡터를 각각 특이적인 프라이머를 이용하여 PCR 방법으로 제작하였다. LysRS-PMT의 형태를 위한 프라이머 셋트는 다음과 같다. 5'-GAG CGA GGA TCC ATG AAA ACA AAA CAT TTT TTT-3'(앞부분 프라이머), 5'-GAG CGA GTC GAC TAG TGC TCT TGT TAA GCG AGG-3'(뒷부분 프라이머). PCR 결과물은 BamHI/SalI으로 절단하였고 이 DNA 조각을 pGEMEX-1(promega)로부터 유래된 플라스미드 pGE-LysRS(S.I. Choi et al., Protein solubility and folding enhancement by interaction with RNA, PLoS ONE 3, 2008, e2677, page 7)에 BamHI/SalI 사이트로 넣어 pGE-LysRS-PMT 형태의 플라스미드를 만들었다. 이 플라스미드의 단백질 발현은 T7 프로모터(promoter)에 의하여 조절 받는다.
단백질 발현과 분리정제
플라스미드로 형질전환된 대장균 BL21(DE3)(Novagen) 균주의 단일 콜로니 (colony)를 50㎍/ml농도의 암피실린(ampicillin) 항생제가 포함되어 있는 2ml LB에 접종하여 37℃에서 밤새 배양하였다. 배양액의 1ml을 같은 농도의 항생제가 들어있는 새로운 20ml의 LB에 희석시켰다. PMT 단백질의 발현은 OD600에서의 세포의 밀도 0.5 값에서 1mM IPTG(Isopropyl β-D-1-thiogalactopyranoside)를 넣고 3시간 동안 배양시킴으로써 유도되었다. 10ml의 세포들을 원심분리법을 통하여 수확하였고 0.3ml PBS에 섞어서 풀어주었다. 세포의 초음파 분쇄(sonication)후, 4℃, 12,000g 조건에서 12분간의 원심분리를 통해 단백질을 total(전체), soluble(수용성), insoluble(불수용성) 부분으로 나누었고, SDS-PAGE를 통해 분석하였다(S.I. Choi et al., Protein solubility and folding enhancement by interaction with RNA, PLoS ONE 3, 2008, e2677, page 5).
500ml의 배양으로 얻어진 LysRS-PMT은 니켈 크로마토그래피에 의해 분리 및 정제하였다. 이후 [50mM Tris-HCl (pH 7.5), 300mM NaCl, 10% 글리세롤, 10mM 이미다졸, 2mM 머캅토에탄올 및 0.1% tween-20] 조건의 버퍼로 니켈 컬럼을 미리 적셔 균등하게 해준 후 같은 버퍼 조건의 단백질 수용액을 적용시켰다. 24.5mM의 이미다졸이 포함되어 있는 위 버퍼를 이용하여 세척을 진행한 후 이미다졸을 24.5mM부터 300mM까지 점진적으로 증가시킨 버퍼를 이용하여 단백질을 분리하였다. 분리된 단백질을 모아서 다음의 저장버퍼[50mM Tris-HCl (pH 7.5), 200mM NaCl, 0.1mM EDTA 및 0.1mM DTT]를 이용하여 투석하였다. 저장버퍼로 투석된 단백질을 Centriprep®(Millopore사)을 이용하여 농축하였다.
이하, 본 발명을 하기의 실시예에 의해 상세히 설명한다. 단, 하기 실시예는 본 발명을 예시하는 것일 뿐, 본 발명의 내용이 하기 실기예에 의해 한정되는 것은 아니다.
실시예
1
PMT
융합단백질의
대장균에서의
발현과 정제
대장균 세포질에서의 PMT 단백질의 수용성 발현을 위하여 LysRS의 C-말단에 PMT를 융합시켜 LysRS-PMT 형태로 만들었다. 추가적으로 단백질 절단효소 TEV가 인식하는 사이트를 LysRS와 PMT사이에 연결 펩타이드 형태로 도입하고 6개 히스티딘 태그(histidine tag)를 PMT의 C 말단에 달아 도 1과 같이 디자인하였다. 이 태그는 니켈 친화성(affinity) 크로마토그래피를 이용한 정제를 위해 도입되었다. LysRS-PMT는 37℃에서 발현되었다. 발현된 LysRS-PMT 단백질의 수용성 정도는 SDS-PAGE를 통해 분석되었다. 37℃의 일반적인 온도에서도 LysRS-PMT 융합 단백질은 95% 이상 수용성이었다(도 2). 이러한 결과는 LysRS가 높은 발현 정도를 유지시키는 동안 융합형태로 되어있는 PMT의 수용성을 극적으로 증가시킴을 나타낸다(도 3). 또한 이는 LysRS에 PMT를 융합시키는 방법이 대장균 시스템에서 PMT를 수용성으로 발현시킬 수 있는 효과적인 방법임을 의미한다.
본 발명에서 형질전환된 균주는 2013년 8월 21일자로 부다페스트 조약하의 국제기탁기관인 한국생명공학연구원에 수탁번호 KCTC12477BP로 기탁하였다.
수용성 발현의 확인 후, LysRS-PMT 융합 단백질은 500ml 배양을 통해 발현시켰고 점진적인 이미다졸(imidazole) 농도 (24.5mM~300mM) 환경에서 단일단계 니켈 친화성(affinity) 크로마토그래피를 통하여 정제하였다(도 4). 분리정제 형태는 SDS-PAGE를 통해 분석하였으며 도 4의 SDS-PAGE의 13 내지 17번 레인의 분리 단편(fraction)을 모아 농축 및 저장 수용액(storage buffer)을 이용하여 투석한 후, 30% 글리세롤과 1:1로 섞어 -20℃에 보관하였다. 도 5와 같이 SDS-PAGE를 통해 확인해 본 결과 LysRS-PMT의 순도는 대략 90%였고, 전체적인 분리정제 효율은 대략 10.6mg/3.2ml이었다.
비교실험예
1
1-1:
PMT
단백질의 직접적인 발현
PMT를 어떠한 단백질과도 융합시키지 않고 직접적으로 발현했을 때, 낮은 온도에서는 수용성으로 소량 발현되었지만, 37℃에서는 완전한 불수용성으로 발현되는 것을 볼 수 있었다(도 3).
1-2:
LysRS
-
PMT
와
PMT
단백질의 면역원성 비교
그룹당 10마리의 마우스에 각각 0.2mL의 PMT 및 LysRS-PMT를 접종하여 면역원성을 비교하였다. 1차 접종 후, 2주 후에 2차 접종하였고, 2차 접종 후 2주후에 공격 접종하여 7일간 관찰하였다. 공격 접종은 병원성이 있는 병원성 균주를 실험 동물에 접종하여 방어능력을 측정하기 위한 것이다.
그 결과, 어떠한 단백질과도 융합시키지 않은 PMT 단백질과 LysRS-PMT의 면역원성을 비교하였을 때, P. multocida와 상동성이 높은 E. coli의 LysRS로 인하여 면역원성이 더 높은 것을 볼 수 있었다(도 7).
이상으로 본 발명 내용의 특정한 부분을 상세히 기술하였는바, 당업계의 통상의 지식을 가진 자에게 있어서, 이러한 구체적 기술은 단지 바람직한 실시양태일 뿐이며, 이에 의해 본 발명의 범위가 제한되는 것이 아닌 점은 명백할 것이다. 따라서 본 발명의 실질적인 범위는 첨부된 청구항들과 그것들의 등가물에 의하여 정의된다고 할 것이다.
<110> ChoongAng vaccine
<120> A recombinant fusion protein, an immunogenic composition,
comprising water-soluble Pasteurella multocida toxin (PMT), and a
method for preparing thereof
<130> 1
<160> 1
<170> KopatentIn 2.0
<210> 1
<211> 1818
<212> PRT
<213> Artificial Sequence
<220>
<223> LysRS-PMT
<400> 1
Met Ser Glu Gln His Ala Gln Gly Ala Asp Ala Val Val Asp Leu Asn
1 5 10 15
Asn Glu Leu Lys Thr Arg Arg Glu Lys Leu Ala Asn Leu Arg Glu Gln
20 25 30
Gly Ile Ala Phe Pro Asn Asp Phe Arg Arg Asp His Thr Ser Asp Gln
35 40 45
Leu His Ala Glu Phe Asp Gly Lys Glu Asn Glu Glu Leu Glu Ala Leu
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Asn Ile Glu Val Ala Val Ala Gly Arg Met Met Thr Arg Arg Ile Met
65 70 75 80
Gly Lys Ala Ser Phe Val Thr Leu Gln Asp Val Gly Gly Arg Ile Gln
85 90 95
Leu Tyr Val Ala Arg Asp Asp Leu Pro Glu Gly Val Tyr Asn Glu Gln
100 105 110
Phe Lys Lys Trp Asp Leu Gly Asp Ile Leu Gly Ala Lys Gly Lys Leu
115 120 125
Phe Lys Thr Lys Thr Gly Glu Leu Ser Ile His Cys Thr Glu Leu Arg
130 135 140
Leu Leu Thr Lys Ala Leu Arg Pro Leu Pro Asp Lys Phe His Gly Leu
145 150 155 160
Gln Asp Gln Glu Ala Arg Tyr Arg Gln Arg Tyr Leu Asp Leu Ile Ser
165 170 175
Asn Asp Glu Ser Arg Asn Thr Phe Lys Val Arg Ser Gln Ile Leu Ser
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Gly Ile Arg Gln Phe Met Val Asn Arg Gly Phe Met Glu Val Glu Thr
195 200 205
Pro Met Met Gln Val Ile Pro Gly Gly Ala Ala Ala Arg Pro Phe Ile
210 215 220
Thr His His Asn Ala Leu Asp Leu Asp Met Tyr Leu Arg Ile Ala Pro
225 230 235 240
Glu Leu Tyr Leu Lys Arg Leu Val Val Gly Gly Phe Glu Arg Val Phe
245 250 255
Glu Ile Asn Arg Asn Phe Arg Asn Glu Gly Ile Ser Val Arg His Asn
260 265 270
Pro Glu Phe Thr Met Met Glu Leu Tyr Met Ala Tyr Ala Asp Tyr Lys
275 280 285
Asp Leu Ile Glu Leu Thr Glu Ser Leu Phe Arg Thr Leu Ala Gln Asp
290 295 300
Ile Leu Gly Lys Thr Glu Val Thr Tyr Gly Asp Val Thr Leu Asp Phe
305 310 315 320
Gly Lys Pro Phe Glu Lys Leu Thr Met Arg Glu Ala Ile Lys Lys Tyr
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Arg Pro Glu Thr Asp Met Ala Asp Leu Asp Asn Phe Asp Ser Ala Lys
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Ala Ile Ala Glu Ser Ile Gly Ile His Val Glu Lys Ser Trp Gly Leu
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Gly Arg Ile Val Thr Glu Ile Phe Glu Glu Val Ala Glu Ala His Leu
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Ile Gln Pro Thr Phe Ile Thr Glu Tyr Pro Ala Glu Val Ser Pro Leu
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Ala Arg Arg Asn Asp Val Asn Pro Glu Ile Thr Asp Arg Phe Glu Phe
405 410 415
Phe Ile Gly Gly Arg Glu Ile Gly Asn Gly Phe Ser Glu Leu Asn Asp
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Ala Glu Asp Gln Ala Gln Arg Phe Leu Asp Gln Val Ala Ala Lys Asp
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Ala Gly Asp Asp Glu Ala Met Phe Tyr Asp Glu Asp Tyr Val Thr Ala
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Leu Glu His Gly Leu Pro Pro Thr Ala Gly Leu Gly Ile Gly Ile Asp
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Arg Met Val Met Leu Phe Thr Asn Ser His Thr Ile Arg Asp Val Ile
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Leu Phe Pro Ala Met Arg Pro Val Lys Asp Asp Asp Asp Asp Asp Ser
500 505 510
Gly Glu Asn Leu Tyr Phe Gln Gly Thr Gly Ser Met Lys Thr Lys His
515 520 525
Phe Phe Asn Ser Asp Phe Thr Val Lys Gly Lys Ser Ala Asp Glu Ile
530 535 540
Phe Arg Arg Leu Cys Thr Asp His Pro Asp Lys Gln Leu Asn Asn Val
545 550 555 560
Lys Trp Lys Glu Val Phe Ile Asn Arg Phe Gly Gln Met Met Leu Asp
565 570 575
Thr Pro Asn Pro Arg Lys Ile Val Glu Lys Ile Ile Asn Glu Gly Leu
580 585 590
Glu Lys Gln Gly Leu Lys Asn Ile Asp Pro Glu Thr Thr Tyr Phe Asn
595 600 605
Ile Phe Ser Ser Ser Asp Ser Ser Asp Gly Asn Val Phe His Tyr Asn
610 615 620
Ser Leu Ser Glu Ser Tyr Arg Val Thr Asp Ala Cys Leu Met Asn Ile
625 630 635 640
Phe Val Glu Arg Tyr Phe Asp Asp Trp Asp Leu Leu Asn Ser Leu Ala
645 650 655
Ser Asn Gly Ile Tyr Ser Val Gly Lys Glu Gly Ala Tyr Tyr Pro Asp
660 665 670
His Asp Tyr Gly Pro Glu Tyr Asn Pro Val Trp Gly Pro Asn Glu Gln
675 680 685
Ile Tyr His Ser Arg Val Ile Ala Asp Ile Leu Tyr Ala Arg Ser Val
690 695 700
Trp Asp Glu Phe Lys Lys Tyr Phe Met Glu Tyr Trp Gln Lys Tyr Ala
705 710 715 720
Gln Leu Tyr Thr Glu Met Leu Ser Asp Thr Phe Leu Ala Met Ala Ile
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Gln Gln Tyr Thr Arg Gln Thr Leu Thr Asp Glu Gly Phe Leu Met Val
740 745 750
Cys Asn Thr Tyr Tyr Gly Asn Lys Glu Glu Val Gln Ile Thr Leu Leu
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Asp Ile Tyr Gly Tyr Pro Ser Thr Asp Ile Ile Cys Ile Glu Gln Lys
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Gly Leu Pro Thr Pro Lys Val Ile Leu Tyr Ile Pro Gly Gly Thr Gln
785 790 795 800
Pro Phe Val Glu Phe Leu Asn Thr Asp Asp Leu Lys Gln Trp Ile Ala
805 810 815
Trp His Leu Lys Asp Asn Lys His Met Val Arg Phe Arg Lys His Phe
820 825 830
Ser Leu Lys Gln Arg Gln Glu Gly Glu Thr Phe Thr Gly Ile Asp Lys
835 840 845
Ala Leu Gln Tyr Ile Ala Glu Glu Ser Pro Glu Trp Pro Ala Asn Lys
850 855 860
Tyr Ile Leu Tyr Asn Pro Thr His Leu Glu Thr Glu Asn Leu Phe Asn
865 870 875 880
Ile Met Met Lys Arg Thr Glu Gln Arg Met Leu Glu Asp Ser Asp Val
885 890 895
Gln Ile Arg Ser Asn Ser Glu Ala Thr Arg Asp Tyr Ala Leu Ser Leu
900 905 910
Leu Glu Thr Phe Ile Ser Gln Leu Ser Ala Ile Asp Met Leu Val Pro
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Ala Val Gly Ile Pro Ile Asn Phe Ala Leu Ser Ala Thr Ala Leu Gly
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Leu Ser Ser Asp Ile Val Val Asn Gly Asp Ser Tyr Glu Lys Arg Lys
945 950 955 960
Tyr Gly Ile Gly Ser Leu Val Gln Ser Ala Leu Phe Thr Gly Ile Asn
965 970 975
Leu Ile Pro Val Ile Ser Glu Thr Ala Glu Ile Leu Ser Ser Phe Ser
980 985 990
Arg Thr Glu Glu Asp Ile Pro Ala Phe Phe Thr Glu Glu Gln Ala Leu
995 1000 1005
Ala Gln Arg Phe Glu Ile Val Glu Glu Glu Leu His Ser Ile Ser Pro
1010 1015 1020
Asp Asp Pro Pro Arg Glu Ile Thr Asp Glu Asn Leu His Lys Ile Arg
1025 1030 1035 1040
Leu Val Arg Leu Asn Asn Glu Asn Gln Pro Leu Val Val Leu Arg Arg
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Leu Gly Gly Asn Lys Phe Ile Arg Ile Glu Pro Ile Thr Phe Gln Glu
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Ile Lys Gly Ser Leu Val Ser Glu Val Ile Asn Pro Val Thr Asn Lys
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Thr Tyr Tyr Val Ser Asn Ala Lys Leu Leu Gly Gly Ser Pro Tyr Ser
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Pro Phe Arg Ile Gly Leu Glu Gly Val Trp Thr Pro Glu Val Leu Lys
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Ala Arg Ala Ser Val Ile Gly Lys Pro Ile Gly Glu Ser Tyr Lys Arg
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Ile Leu Ala Lys Leu Gln Arg Ile His Asn Ser Asn Ile Leu Asp Glu
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Arg Gln Gly Leu Met His Glu Leu Met Glu Leu Ile Asp Leu Tyr Glu
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Glu Ser Gln Pro Ser Ser Glu Arg Leu Asn Ala Phe Arg Glu Leu Arg
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Thr Gln Leu Glu Lys Ala Leu Tyr Leu Pro Glu Met Glu Ala Leu Lys
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Lys Gln Ile Leu Gln Ile Pro Asn Lys Gly Ser Gly Ala Ala Arg Phe
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Leu Leu Arg Thr Ala Met Asn Glu Met Ala Gly Lys Thr Ser Glu Ser
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Thr Ala Asp Leu Ile Arg Phe Ala Leu Gln Asp Thr Val Ile Ser Ala
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Pro Phe Arg Gly Tyr Ala Gly Ala Ile Pro Glu Ala Ile Asp Phe Pro
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Val Lys Tyr Val Ile Glu Asp Ile Ser Val Phe Asp Lys Ile Gln Thr
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Asn Tyr Trp Glu Leu Pro Ala Tyr Glu Ser Trp Asn Glu Gly Ser Asn
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Ser Arg Leu Leu Pro Gly Leu Leu Arg Glu Ser Gln Ser Lys Gly Met
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Leu Ser Lys Cys Arg Ile Ile Glu Asn Ser Leu Tyr Ile Gly His Ser
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Tyr Glu Glu Met Phe Tyr Ser Ile Ser Pro Tyr Ser Asn Gln Val Gly
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Gly Pro Tyr Glu Leu Tyr Pro Phe Thr Phe Phe Ser Met Leu Gln Glu
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Val Gln Gly Asp Leu Gly Phe Glu Gln Ala Phe Ala Thr Arg Asn Phe
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Phe Asn Thr Leu Val Ser Asp Arg Leu Ser Leu Met Glu Asn Thr Met
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Leu Leu Thr Glu Ser Phe Asp Tyr Thr Pro Trp Asp Ala Ile Tyr Gly
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Asp Ile Asn Tyr Asp Glu Gln Phe Ala Ala Met Ser Ile Asn Glu Arg
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Ile Glu Lys Cys Met Asn Thr Tyr Arg Gly Val Ala Phe Gln Asn Ser
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Ser Lys Ser Ile Asp Phe Phe Leu Asn Asn Leu Thr Thr Phe Ile Asp
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Asn Gly Leu Thr Glu Ile Ala Ile Ser Asp Leu Pro Tyr Asp Ile Val
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Gln Gln Glu Ile Ser Gln Phe Leu Gln Gly Ser Asn Glu Trp Lys Thr
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Leu Asp Ala Met Leu Phe Asn Leu Asp Lys Gly Asp Ile Asn Gly Ala
1490 1495 1500
Phe Arg Lys Leu Leu Gln Ser Ala Lys Asp Asn Asn Ile Lys Phe Arg
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Ala Ile Gly His Ser Asp Asn Ser Val Pro Pro Phe Asn Asn Pro Tyr
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Lys Ser Leu Tyr Tyr Lys Gly Asn Ile Ile Ala Glu Ala Ile Glu Lys
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Leu Asp Arg Glu Gly Gln Lys Phe Val Val Phe Ala Asp Ser Ser Leu
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Leu Asn Ser Thr Pro Gly Thr Gly Arg Pro Met Pro Gly Leu Val Gln
1570 1575 1580
Tyr Leu Lys Ile Pro Ala Thr Val Val Asp Ser Asp Gly Ala Trp Gln
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Phe Leu Pro Asp Val Ala Ser Ser Arg Val Pro Ile Glu Val Thr Glu
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Leu Glu Asn Trp Gln Val Leu Thr Pro Pro Gln Gly Lys Ile Leu Gly
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Leu Lys Gln Phe Lys Leu Thr Ala Gly Phe Pro Thr Glu Gln Ser Arg
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Leu Pro Leu Leu Glu Asn Ser Val Ser Glu Asp Leu Arg Glu Glu Leu
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Met Gln Lys Ile Asp Ala Ile Lys Asn Asp Val Lys Met Asn Ser Leu
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Val Cys Met Glu Ala Gly Ser Cys Asp Ser Val Ser Pro Lys Val Ala
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Ala Arg Leu Lys Asp Met Gly Leu Glu Ala Gly Met Gly Ala Ser Ile
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Thr Trp Trp Arg Arg Glu Gly Gly Met Glu Phe Ser His Gln Met His
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Thr Thr Ala Ser Phe Lys Phe Ala Gly Lys Glu Phe Ala Val Asp Ala
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Ser His Leu Gln Phe Val His Asp Gln Leu Asp Thr Thr Ile Leu Ile
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Leu Pro Val Asp Asp Trp Ala Leu Glu Ile Ala Gln Arg Asn Arg Ala
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Ile Asn Pro Phe Val Glu Tyr Val Ser Lys Thr Gly Asn Met Leu Ala
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Leu Phe Met Pro Pro Leu Phe Thr Lys Pro Arg Leu Thr Arg Ala Leu
1795 1800 1805
Val Asp Lys Leu His His His His His His
1810 1815
Claims (9)
- LysRS (lysyl-tRNA synthetase) 및 파스튜렐라 멀토시다 독소(Pasteurella multocida toxin, PMT)를 포함하는 서열번호 1로 구성된 재조합 융합 단백질.
- 제 1항에 있어서, 상기 재조합 융합 단백질은 LysRS와 PMT 사이에 단백질 절단효소 인식 부위가 존재하는 것을 특징으로 하는 재조합 융합 단백질.
- 제 1항에 있어서, 상기 LysRS는 대장균으로부터 유래한 것을 특징으로 하는 재조합 융합 단백질.
- 삭제
- 삭제
- 위축성 비염을 치료 또는 예방하기 위한, 제 1항 내지 제 3항 중 어느 한 항에 따른 재조합 융합 단백질을 포함하는 면역원성 조성물.
- LysRS를 코딩하는 유전자 및 파스튜렐라 멀토시다 독소를 코딩하는 유전자를 포함하는 제 1항 내지 제 3항 중 어느 한 항에 따른 재조합 융합 단백질 생산용 발현벡터.
- 제 7항에 따른 발현벡터로 형질전환된 대장균(E. coli) KCTC 12477BP.
- LysRS를 코딩하는 유전자 및 파스튜렐라 멀토시다 독소를 코딩하는 유전자를 포함하는 발현벡터를 대장균에 도입하여 형질전환체를 제조하는 단계를 포함하는, 제 1항 내지 제 3항 중 어느 한 항에 따른 재조합 융합 단백질을 제조하는 방법.
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