KR102427948B1 - 다발성 골수종에서 m-단백질 반응의 임상 평가 - Google Patents
다발성 골수종에서 m-단백질 반응의 임상 평가 Download PDFInfo
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- KR102427948B1 KR102427948B1 KR1020187026496A KR20187026496A KR102427948B1 KR 102427948 B1 KR102427948 B1 KR 102427948B1 KR 1020187026496 A KR1020187026496 A KR 1020187026496A KR 20187026496 A KR20187026496 A KR 20187026496A KR 102427948 B1 KR102427948 B1 KR 102427948B1
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Abstract
출원인은, 인간 알부민에 융합될 때 IFE에서 항체를 이동시켜 M-단백질 임상 평가에서 MOR202의 임의의 잠재적 간섭을 경감시키는, MOR202에 대한 항-이디오타입 항체를 개시한다.
Description
본 발명은 다발성 골수종에서 M-단백질 반응의 임상 평가에 관한 것이다.
다발성 골수종(Multiple myeloma, MM)은 악성 형질 세포의 클론 확장을 포함하는 혈액 암이다. MM은 미국에서 가장 흔한 악성 형질 세포 종양이고 두 번째로 흔한 혈액 암이다. 미국의 연령-보정 발생률은 100,000명 당 5.5사례이고 영국에서 연간 발생률은 100,000명 당 대략 6 내지 7명에 달한다.
형질 세포는 면역글로불린(감마글로불린으로도 불림)을 생산하는데, 이는 함께 연결된 중쇄(IgG, IgA, IgM, IgD 또는 IgE) 및 경쇄(카파 또는 람다)로 구성된다. 하나의 형질 세포는 한 가지 유형의 면역글로불린(예를 들어, IgA 카파 또는 IgG 카파)을 생산한다. 정상적으로 신체는 다양한 다른 형질 세포("다클론")를 포함하여, 혈청에서 면역글로불린은 또한 광범위한 다른 구성 방식(format) 및 특이성(다클론)을 나타낸다. 다발성 골수종의 경우, 악성 종양 세포는 단 하나 또는 단지 몇 안 되는 별개의 형질 세포(들)의 복제이고 이것 또는 이들 세포(들)에 의해 분비되는 면역글로불린은 단클론으로 간주된다.
이 단클론 면역글로불린은 M-단백질 또는 파라단백질로 불리고 또한 중쇄(가장 흔하게는 IgG 또는 IgA뿐 아니라 IgM, IgD 또는 IgE) 및 경쇄(카파 또는 람다) 또는 이들 면역글로불린의 절단된 형태로 구성될 수 있다. 혈청에서 M 단백질의 증가는 MM과 같은 B-세포 악성 종양을 확인하기 위해 사용된다.
다발성 골수종에서 반응의 모니터링 및 진단을 위해 현재 다수의 병기 분류 시스템이 사용된다: a) Durie 및 Salmon 병기 분류 시스템(Durie and Salmon Staging System), b) 국제 병기 분류 시스템(International Staging System, ISS), 및 국제 골수종 작업 그룹(International Myeloma Working Group, IMWG). Durie 및 Salmon 병기 분류 시스템은 종양 세포 매스, 상승된 혈청 면역글로불린(Ig)G 수준, 말단-기관 손상, 및 골용해성 골 병변을 평가하는 특성을 포함한다. ISS는 β2-마이크로글로불린 수준 및 혈청 알부민 수준을 기반으로 하는 질환 부담에 더 역점을 둔다. IMWG는 분자적 및 세포유전학적 이상 둘 다를 고려하는데, 구체적으로 시간 경과에 따른 M-단백질 감소가 가장 중요한 인자의 하나이고 질환의 진행 및 치료 성공을 평가하기 위해 사용된다.
다발성 골수종의 단백질 징후 특징은 단클론(M)-단백질 농도(IgG, IgA, IgA, IgD), 경쇄 농도(카파[κ] 및 람다[λ]를 포함함), 비정상 β2-마이크로글로불린, 혈청 알부민, 크레아티닌, 및 헤모글로빈 수준의 증가, 그리고 골수 형질 세포(5%보다 크거나 이와 동일한)의 발견을 포함한다. 환자에 의해 생산된 단백질 징후(예를 들어, M 단백질)의 측정은 많은 방법에 의해 달성될 수 있다. M-단백질을 측정하는 검사는 24-시간 소변 수집 검사, 소변 단백질 전기영동(UPEP), 혈청 단백질 전기영동(SPEP), 면역고정 전기영동(IFE), 및 혈청 유리 경쇄(serum free light chain, sFLC) 분석이다.
CD38은 악성 종양 형질 세포 및 다른 림프구에서 발현되는 항원의 예이고, 따라서 다발성 골수종 및 다른 감마글로불린병증의 처치에서 치료 표적을 나타낸다. CD38에 부여된 기능은 부착 및 신호전달 이벤트에서 수용체 매개 및 (엑토-) 효소 활성 둘 다를 포함한다. 엑토효소로서, CD38은 NAD+를 사이클릭 ADP-리보오스(cADPR) 및 ADPR, 또한 니코틴아미드 및 니코틴산-아데닌 디뉴클레오티드 포스페이트(NAADP)의 형성을 위한 기질로서 사용한다. cADPR 및 NAADP는 Ca2+ 동원을 위한 제2 메신저로서 작동하는 것을 보여주었다. NAD+를 cADPR로 전환시킴으로써, CD38은 세포외 NAD+ 농도를 조절하고, 이에 따라 NAD-유도 세포 사멸(NCID)의 조정에 의해 세포 생존을 조절한다. Ca2+를 통한 신호 전달에 추가하여, CD38 신호 전달은 T 세포 및 B 세포에서의 항원-수용체 복합체 또는 다른 유형의 수용체 복합체, 예를 들어 MHC 분자와의 크로스-토크(cross-talk)를 통해 일어나고, 이 방식으로 몇 가지 세포 반응뿐 아니라 IgG의 분비 및 전환(switching)에 관여한다.
CD38에 특이적인 항체가 다발성 골수종의 치료를 위해 개발 중이다. CD38에 특이적인 항체는 WO1999/62526(Mayo Foundation); WO200206347(Crucell Holland); US2002164788(Jonathan Ellis)(그 전체가 참조로 포함됨); WO2005/103083(MorphoSys AG), US 출원번호 10/588,568(그 전체가 참조로 포함됨), WO2006/125640(MorphoSys AG), US 출원번호 11/920,830(그 전체가 참조로 포함됨), 및 WO2007/042309(MorphoSys AG), US 출원번호 12/089,806(그 전체가 참조로 포함됨); WO2006099875(Genmab), US 출원번호 11/886,932(그 전체가 참조로 포함됨); WO2011154453A1(Genmab), US 출원번호 13/702,857(그 전체가 참조로 포함됨); WO08/047242(Sanofi-Aventis), US 출원번호 12/441,466(그 전체가 참조로 포함됨); WO2015066450(Sanofi), US 출원번호 14/529,719(그 전체가 참조로 포함됨); WO2012092616A1, 및 WO2012092612A1(Takeda), US 출원번호 13/341,860 및 13/977,207(둘 다 그 전체가 참조로 포함됨), 그리고 WO2014178820A1(Teva)에 기술되어있다.
MM 환자에서 항-CD38 항체 처치는 다발성 골수종 세포에 의해 생산되는 M-단백질의 부분적 또는 완전한 청소를 초래할 수 있다. 혈청 단백질 전기영동(SPEP) 및 면역고정 전기영동(IFE)은 둘 다 다발성 골수종 환자에서 단클론 단백질을 확인 및 면역분류(immunotyping)하기 위해 사용되는 필수적인 분석이다. 최근의 연구에서는 다발성 골수종의 치료를 위한 개발에서 특정 치료 항체가 혈청 IFE에서 용이하게 검출되고 M 단백질 수준의 검출 및 모니터링에 간섭할 수 있음을 보여주었다(McCudden et al., Clinical Chemistry, 56:12; 1897-1904 (2010), 또한 Genzen et al., British Journal of Haematology (2011) 155(1) 123-125 참고). McCudden 등은 실툭시맙(항-IL-6 항체)과 항-약물 항체를 함께 인큐베이션함으로써, 치료 항체 실툭시맙이 내인성 M-단백질로부터 구분될 수 있도록 약물 전기영동 패턴을 이동시킨 것을 발견하였다. Janssen에서는 또한, 유사한 접근법을 사용하여 IFE에서 다라투무맙의 M-단백질 간섭을 경감시키는 임상 분석의 개발을 최근 발표하였는데, 이는 IFE에서 복합체를 이동시키기 위해 비오틴 또는 알렉사-플루오르(Alexa-fluor) 태그로 이상적으로 표지된 마우스 항-다라투무맙 항체를 이용하였다. Axel, et al., Development of a Clinical Assay to Mitigate Daratumumab, an IgG1k Monoclonal Antibody, Interference with Serum Immunofixation and Clinical Assessement of M-protein Response in Multiple Myeloma Poster Presented at the 105th Annual Meeting of the American Association for Cancer Research (AACR), April 5-9, 2014, San Diego, California, USA; 또한 van de Donk et al., Monoclonal antibodies targeting CD38 in hematological malignancies and beyond, Immunological Reviews, 270:95-112 (2016) 참고.
그러나, 이들 접근법은 모든 치료 항체에 대하여 충분하지는 않다. 국제 골수종 작업 그룹(IMWG) 기준에 부합하는 유효한 임상 반응 기술을 보장하기 위해 SPEP 및 IFE에서의 이러한 잠재적 간섭을 회피하기 위한 각각의 치료 항체에 특이적인 신규의 경감 전략이 요구된다.
출원인은 본원에서, 인간 알부민에 융합될 때 IFE에서 항체를 이동시켜 M-단백질 기반 임상 평가에서 MOR202의 임의의 잠재적 간섭을 경감시키는, MOR202에 대한 항-이디오타입 항체를 개시한다.
항-이디오타입 항체, 알부민 융합은 M-단백질 반응의 임상 평가를 향상시키기 위해 MOR202의 임상 개발 디자인으로 통합될 것이다.
일 양태는 MOR202에 대한 항-이디오타입 항체이다. 일 양태에서 항-이디오타입 항체는 인간 알부민에 융합된다. 구현예에서 항-이디오타입 항체는,
아미노산 서열 YSFSNYWIS(서열번호: 18)의 HCDR1,
아미노산 서열 WMGIIDPASSKTRYSPSFQG(서열번호: 19)의 HCDR2,
아미노산 서열 SRGAGMDY(서열번호: 20)의 HCDR3를 포함하는 가변 중쇄, 및
아미노산 서열 TGSSSNIGAGYDVH(서열번호: 21)의 LCDR1,
아미노산 서열 LLIYADNNRPS(서열번호: 22)의 LCDR2,
아미노산 서열 GSYDESSNSM(서열번호: 23)의 LCDR3를 포함하는 가변 경쇄를 포함한다.
일 구현예에서, 항-이디오타입 항체는 인간 항체이다.
구현예에서, 항-이디오타입 항체 융합체는 다음 아미노산 서열의 중쇄를 포함한다.
구현예에서, 항-이디오타입 항체 융합체는 다음 아미노산 서열의 경쇄를 포함한다.
일 양태는 다발성 골수종 또는 다른 감마글로불린병증에 대한 처치를 받는 중인 환자로부터 얻은 혈액 샘플을 평가하는 방법으로, 이 방법은
a) 상기 환자로부터 혈액 샘플을 얻고,
b) 혈액 샘플을 항-이디오타입 항체와 인큐베이션하고,
c) 면역고정 전기영동(IFE)을 수행하고, 그리고
d) IFE의 결과를 보고하는 단계를 포함한다.
구현예에서, 환자는 MOR202로 처치를 받는 중이다.
구현예에서, 샘플은 총 M-단백질 수준에 대하여 평가된다.
일 양태는 예시된 항-이디오타입 항체 또는 예시된 항-이디오타입 항체 알부민 융합체를 암호화하는 핵산이다.
정의
"항-이디오타입"이라는 용어는 항체의 가변 영역에 결합하는 단백질 또는 펩티드를 기술한다. 항-이디오타입 단백질은 항체일 수 있다. 예를 들어, 항체 MOR09292는 MOR202의 가변 영역에 결합한다.
"항체"라는 용어는 항체 단편을 포함한다. 항체는 임의의 동형의 단클론 항체, 예를 들어, IgG, IgM, IgA, IgD 및 IgE를 포함한다. IgG 항체는 이황화 결합에 의해 연결된 2개의 동일한 중쇄 및 2개의 동일한 경쇄로 구성된다. 항체의 중쇄 및 경쇄는 불변 영역 및 가변 영역을 포함한다. 각각의 가변 영역은 "상보성-결정 영역"("CDRs") 또는 "초가변 영역"으로 불리는 3개의 절편을 포함하는데, 이들은 일차적으로 항원의 에피토프와 결합하는 원인이 된다. 이들은 N-말단으로부터 순차적으로 번호를 붙여 CDR1, CDR2, 및 CDR3로 언급된다. CDRs의 바깥쪽 더욱 고도로 보존된 부분의 가변 영역은 "프레임워크 영역"으로 불린다. "항체 단편"은 Fv, scFv, dsFv, Fab, Fab' F(ab')2 단편, 또는 각각 CDRs 및 프레임워크 영역을 포함하는 적어도 하나의 가변 중쇄 또는 가변 경쇄를 포함하는 다른 단편을 의미한다.
본원에서 "CDRs"은 초티아 등(Chothia et al.), 카바트 등(Kabat et al.)에 의하거나, 또는 국제 넘버링 협약에 의해 정의된다. 그 전체가 참조로 포함되는 Chothia C, Lesk AM. (1987) Canonical structures for the hypervariable regions of immunoglobulins. J Mol Biol., 196(4):901-17 참고. 그 전체가 참조로 포함되는 Kabat E.A, Wu T.T., Perry H.M., Gottesman K.S. and Foeller C. (1991). Sequences of Proteins of Immunological Interest. 5th edit., NIH Publication no. 91-3242, US Dept. of Health and Human Services, Washington, DC 참고.
"VH"는 항체 또는 항체 단편의 면역글로불린 중쇄의 가변 영역을 말한다. "VL"은 항체 또는 항체 단편의 면역글로불린 경쇄의 가변 영역을 말한다.
"Fc 영역"은 항체의 불변 영역을 의미하는데, 이는 인간에서 IgG1, 2, 3, 4 서브클래스 등일 수 있다. 인간 Fc 영역의 서열은 IMGT, Human IGH C-REGIONs, http://www.imgt.org/ligmdb/(2016년 2월 22일 검색됨)에서 이용 가능하다.
본원에서 사용되는 바와 같은 "인간 항체" 또는 "인간 항체 단편"은 프레임워크 및 CDR 영역이 둘 다 인간 기원의 서열로부터 유래되는 가변 영역을 갖는 항체 및 항체 단편을 포함한다. 더욱이, 항체가 불변 영역을 포함할 경우, 불면 영역 또한 이러한 서열로부터 유래된다.
"특이적"은 항원을 인식하고 이러한 항원과 하나 이상의 비교 항원(들) 사이를 식별할 수 있는 단백질을 기술한다. 이 능력은 표준 ELISA 분석에 의해 확인될 수 있다. 전형적으로, 특이성의 결정은 단일 비교 항원을 사용하는 것이 아니라, 분유, BSA, 트랜스페린 등과 같은, 대략 3개 내지 5개의 비관련 항원의 세트를 사용하여 수행된다.
"혈액 샘플을 평가하는 것"은 그 방법에 대하여 가장 관련 있는 혈액 샘플의 일부 또는 혈액을 평가하는 것을 의미한다. 현재, 면역고정 전기영동은 혈액의 혈청 성분에 대하여 행하여진다. 그러나, 후일에 상이한 혈액 성분이 평가될 경우, 본 발명은 그 혈액 성분을 평가하는 방법에 관련될 것이다. 혈액 성분은, 예를 들어 혈장, 혈청, 세포, 예를 들어 적혈구 및 백혈구, 그리고 혈소판을 포함한다. 혈장은 단백질, 예를 들어 글로불린, 및 응고 인자, 및 염, 당, 지방, 호르몬 및 비타민을 포함한다.
감마글로불린병증은 혈청 면역글로불린 수준이 크게 증가한 병태이다. 이들은 다클론성(모든 주 면역글로불린 클래스에서의 증가) 또는 단클론성(단일 균질 면역글로불린에서의 증가)으로 분류될 수 있다.
다클론성 감마글로불린병증은 면역계의 만성적 자극으로부터 야기된다. 따라서, 이들은 만성 농피증; 만성 바이러스, 박테리아, 또는 진균 감염; 육아종성 박테리아 질환; 농양; 만성 기생충 감염; 만성 리케차 질환, 예를 들어 열대성 견 범혈구감소증; 만성 면역 질환, 예를 들어 전신성 홍반성 루푸스, 류마티스성 관절염, 및 근염; 또는 일부 종양에 의해 야기될 수 있다. 많은 사례에서, 명백한 소인적 원인이 없다. 일부 동물에서, 감마글로불린병증은 초기에 단일 면역글로불린 클래스(보통 IgG)의 우세로 인해 단클론성일 수 있다.
단클론성 감마글로불린병증은 대량의 단일 면역글로불린 단백질의 생산을 특징으로 한다. 단클론성 감마글로불린병증은 양성(즉, 원질환과 관련되지 않음)이거나, 보다 일반적으로는, 면역글로불린-분비 종양과 관련된다. 단클론 항체를 분비하는 종양은 형질 세포로부터 기원한다(골수종). 골수종은 임의 면역글로불린 클래스 또는 면역글로불린 서브유닛 또는 단편(경쇄 또는 중쇄)의 온전한 단백질을 분비할 수 있다. 단클론성 감마글로불린병증의 예는 다음을 포함한다: 호지킨 병(Hodgkin's disease); 다발성 골수종의 변이형, 예를 들어 뼈의 고립성 형질세포종, 골수외 형질세포종, 형질 세포성 백혈병, 및 비-분비성 골수종, 림프구증식성 장애, 예를 들어 발덴스트롬 거대글로불린혈증 (Waldenstrom's macroglobulinemia), 및 림프종; 중쇄 질환(γ, α, μ); 및 아밀로이드증.
인간 CD38은 다음 아미노산 서열을 갖는다:
아미노산 서열이 도 1에 제공되는 항-CD38 항체인 "MOR202". "MOR202" 및 "MOR03087"은 도 1에 나타낸 항체를 기술하는 동의어로서 사용된다.
MOR202 가변 중쇄 도메인을 암호화하는 DNA 서열은 다음과 같다:
MOR202 가변 경쇄 도메인을 암호화하는 DNA 서열은 다음과 같다:
MOR202는 WO2007/042309, US 출원번호 제12/089,806호(그 전체가 참조로 포함됨)에 개시된다. US 출원번호 제12/089,806호에서, MOR202는 서열번호: 21에 상응하는 가변 중쇄 및 서열번호: 51에 상응하는 가변 경쇄를 포함하는 항체이고, MOR202를 암호화하는 핵산은 가변 중쇄 서열번호: 6 및 가변 경쇄 서열번호: 36이다.
MOR202는 현재 재발성/난치성 골수종 환자에서 단계 1/2 임상 시험 중이다. 이 연구는 단독요법으로서, 그리고 포말리도마이드 및 레날리도마이드와 추가로 덱사메타손과의 병용에서 MOR202의 안전성 및 예비 효능을 평가하는 것이다.
항체 MOR09292는 MOR202에 대한 항-이디오타입 항체이고 다음 핵산 서열에 의해 암호화된다:
MOR09292-VH-CH1_HSA_6His(리더 서열 없음)(MOR09292-hAlb 중쇄)를 암호화하는 DNA:
MOR09292-VL-람다(리더 서열 없음)(MOR09292-hAlb 경쇄)를 암호화하는 DNA:
인간 알부민은 다음 아미노산 서열을 갖는다(신호 서열을 포함함):
다발성 골수종에 대한 국제 골수종 작업 그룹(IMWG) 일정 반응 기준은 다음과 같다:
전기영동은 생화학적 특성을 기반으로 단백질을 분리하는 방법이다. 혈청을 특정 배지에 놓고 전하를 적용한다. 순전하(양 또는 음) 및 단백질의 크기와 형상이 보통 다양한 혈청 단백질을 구별하는 데 사용된다.
혈청 단백질 전기영동의 몇 가지 서브세트가 이용 가능하다. 이들 서브세트의 명칭은 다양한 혈청 성분을 분리하고 구별하는 데 사용되는 방법을 기반으로 한다. 구역 전기영동에서는, 예를 들어 상이한 단백질 서브타입이 한천, 셀룰로오스, 또는 다른 식물 재료로 만들어진 겔 상에서 분리된 물리적 위치에 놓인다. 단백질은 염색되고, 이들의 밀도가 컴퓨터로 계산되어 다양한 단백질의 절대적 및 상대적 양에 대한 그래프 데이터를 제공한다. 단백질 서브타입의 추가적 분리는 면역고정 및/또는 면역형광을 야기하는 면역학적 활성제로 염색함으로써 달성된다.
혈청 단백질 전기영동 결과의 패턴은 두 가지 주요 유형의 단백질: 알부민 및 글로불린의 분율에 의존한다. 혈청의 주요 단백질 성분인 알부민은 정상 생리적 조건 하에 간에서 생산된다. 글로불린은 총 혈청 단백질 함량의 더 작은 분율을 포함한다. 이들 단백질 및 이들의 상대적 양의 서브세트는 대체로 혈청 단백질 전기영동의 해석의 일차적 초점이다.
혈청 단백질 전기영동에서 관찰되는 최대 피크인 알부민은 양극에 가장 가깝게 위치한다. 다음의 5개 성분(글로불린)은 알파1, 알파2, 베타1, 베타2, 및 감마로 표시된다. 이들 성분의 피크는 음극을 향하여 나타나고, 감마 피크가 음극에 가장 가깝다.
도 3은 혈청 단백질 전기영동으로 결정된 단백질의 분포에 대한 전형적인 정규 패턴을 보여준다.
알부민 밴드는 인간 혈청의 최대 단백질 성분을 나타낸다. 알부민 수준은 이 단백질의 간에 의한 생산이 더 적거나 이 단백질의 손실 또는 분해가 증가된 환경 하에서 저하된다. 영양실조, 중대한 간 질환, 신장 손실(예를 들어, 신증후군), 호르몬 요법, 및 임신은 낮은 알부민 수준의 이유가 될 수 있다. 화상 또한 낮은 알부민 수준을 야기할 수 있다. 알부민의 수준은, 예를 들어 혈청 수분에서의 상대적 감소가 있는(예를 들어, 탈수) 환자에서 증가한다.
겔의 음성 부분(즉, 음극)으로 이동하면, 다음 피크는 알파1 및 알파2 성분을 포함한다. 알파1-단백질 부분은 알파1-항트립신, 갑상선-결합 글로불린, 및 트랜스코르틴으로 구성된다. 악성 종양 및 급성 염증(급성기 반응 물질로부터 초래됨)은 알파1-단백질 밴드를 증가시킬 수 있다. 저하된 알파1-단백질 밴드는 간 질환의 결과로서 글로불린의 저하된 생산 또는 알파1-항트립신 결핍으로 인해 일어날 수 있다. 세룰로플라스민, 알파2-거대글로불린, 및 합토글로빈은 알파2-단백질 밴드에 기여한다. 알파2 성분은 급성기 반응 물질로서 증가된다.
베타 부분은 베타1 및 베타2로 표시된 2개의 피크를 갖는다. 베타1은 주로 트랜스페린으로 구성되고, 베타2는 베타-리포단백질을 함유한다. IgA, IgM, 그리고 때때로 IgG는, 보완 단백질과 함께 베타 부분에서 확인될 수도 있다.
많은 임상적 흥미가 혈청 단백질 스펙트럼의 감마 영역에 초점을 두는데, 면역글로불린이 이 영역으로 이동하기 때문이다. 면역글로불린은 종종 전기영동 스펙트럼 전체에 걸쳐 발견될 수 있음이 주목되어야 한다. C-반응성 단백질 (CRP)은 베타와 감마 성분 사이의 지역에 위치한다.
비록 많은 병태가 감마 영역에서의 증가를 야기할 수 있다 하더라도, 몇 가지 질환 상태는 감마-글로불린 구역의 중심 영역에서 균질 스파이크-같은 피크를 야기한다(도 4). 이들 소위 말하는 "단클론성 감마글로불린병증"은, 각각 MM과 같은 균질 M 단백질을 생산하는 형질 세포의 단일 또는 매우 적은 클론(들)의 증식을 특징으로 하는 일군의 장애를 구성한다.
면역고정 전기영동(IFE)은 단백질이 첨가된 단클론 또는 다클론 검출 항체 시약과 불용성 복합체를 형성함으로써 전기영동 이후 고정되도록 허용한다. 이는 다음 4단계로 수행된다:
1) 전기영동에 의한 단백질의 분리.
2) 전기영동된 단백질의 면역고정(면역침전) - 적절한 전기영동 이동 트랙이 개별 항혈청과 중첩된다. 항혈청이 겔로 확산되고, 존재시 상응하는 항원을 침전시킨다. 단백질은 참고 트랙에서 고정제로 고정된다.
3) 침전되지 않은 가용성 단백질을 빨아들이고 세척함으로써 겔로부터 제거한다. 항원-항체 복합체의 침전을 겔 매트릭스 내로 포집한다.
4) 침전된 단백질을 염색(예를 들어, 산 바이올렛 염색)에 의해 가시화시킨다.
의심되는 단클론 성분을 검출 및 확인하기 위해, 샘플을 몇 개의 트랙에서 병렬로 동시에 전기영동시킨다(도면 참고). 전기영동 이후, ELP 트랙은 (총 단백질 고정을 포함하는) 비교 역할을 하여 혈청 샘플의 단백질의 완전한 전기영동 패턴을 제공한다. 나머지 트랙은 보통 인간 IgG, IgA 및 IgM 중쇄에 대한 항혈청, 그리고 유리 및 결합 카파 및 람다 경쇄에 대한 항혈청과의 반응, 또는 이의 결여로부터 단클론 성분의 특성화를 허용한다. 다른 항-혈청(예를 들어, 항-IgD 등) 또한 가능하다. 면역고정된 밴드는 다음에 비교 패턴에서 의심되는 밴드와 비교하는데 - 상응하는 밴드는 동일한 이동 위치를 가질 것이다.
도 5는 혈청 면역고정 전기영동 이후 겔의 예를 보여준다. 건강한 공여자로부터의 혈청 샘플을 겔 전기영동을 통해 병렬로 6회 분리한 한편, 각각의 레인을 상이한 시약으로 염색하였다. 염색 후 비복합체 단백질을 빨아들이고 세척하여 제거하였다. 레인 ELP = 총 단백질 염색; 레인 G = 항-IgG 염색; 레인 A = 항-IgA 염색; 레인 M = 항-IgM 염색; 레인 K = 항-카파 염색; 레인 L = 항-람다 염색.
도 1은 MOR202의 아미노산 서열을 보여준다.
도 2a 및 2b는 MOR09292(MOR202에 대한 항-이디오타입 항체) 인간 알부민 융합 단백질의 아미노산 서열을 보여준다.
도 3은 혈청 단백질 전기영동으로 결정된 단백질의 분포에 대한 전형적인 정규 패턴을 보여준다.
도 4는 단클론성 감마글로불린병증으로 알려진 장애에 통상적인 감마-글로불린 구역의 초점 영역에서 균질 스파이크-양 피크를 갖는 단백질의 혈청 단백질 전기영동 분포를 보여준다. 이 피크는 균질 M 단백질을 생산하는 단일 클론의 형질 세포를 나타낸다.
도 5는 건강한 공여자의 혈청 면역고정 전기영동 이후 겔의 예를 보여준다. 레인 ELP = 총 단백질 염색; 레인 G = 항-IgG 염색; 레인 A = 항-IgA 염색; 레인 M = 항-IgM 염색; 레인 K = 항-카파 염색; 레인 L = 항-람다 염색.
도 6은 약물 비처치 건강한 공여자(A 및 B) 및 약물 비처치 MM 환자(C 및 D)로부터의 샘플의 혈청 면역고정 전기영동을 보여준다. 샘플은 상이한 농도로 MOR202를 첨가하거나 첨가하지 않고 시험하였다. (레인 1 = MOR202 첨가하지 않음; 레인 2 = MOR202를 200 μg/mL로 첨가; 레인 3 = MOR202를 400 μg/mL로 첨가; 레인 4 = MOR202를 800 μg/mL로 첨가; 레인 5 = MOR202를 1200 로 μg/mL 첨가). 점선으로 둘러싼 밴드는 MOR202 첨가 후에만 가시적으로 되고 각각의 분자를 나타낸다. 화살표로 표시된 밴드는 내인성 M-단백질을 나타낸다.
도 7은 MOR202 +/- MOR0929 IgG1 및 MOR09292 IgM의 식염수 중 예비 배양의 혈청 면역고정 전기영동을 보여준다. MOR202를 식염수 중 고정 농도 1200 μg/mL(A 및 B) 또는 560 μg/mL(C)로 이의 이디오타입 항체 MOR09292와 상이한 구성 방식으로 예비 배양하고 조제된 샘플을 IFE를 통해 분석하였다. A) + B): MOR202 및 MOR09292 IgG1(항-IgG 염색(A) 및 항-람다 염색(B) 사용)(레인 1 = MOR202; 레인 2 = MOR09292 IgG1 2400 μg/mL; 레인 3 = MOR202 + MOR09292 IgG1 600 μg/mL; 레인 4 = MOR202 + MOR09292 IgG1 1200 μg/mL; 레인 5 = MOR202 + MOR09292 IgG1 2400 μg/mL). C): MOR202 및 MOR09292 IgM(항-IgG 염색(레인 2 내지 4), 항-람다 염색(레인 5 내지 7) 및 항-IgM 염색(레인 8 내지 10) 사용)(레인 2/5/8 = MOR202; 레인 3/6/9 = MOR09292 IgM 560 μg/mL; 레인 4/7/10 = MOR202 + MOR09292 IgM 560 μg/mL; 레인 1 = 혈청 샘플에서 일반 배경 신호전달을 평가하기 위해 총 단백질에 대하여 염색된 건강한 공여자로부터의 인간 혈청).
도 8은 MOR202 +/- MOR09292-인간 알부민 융합체(MOR09292-hAlb)의 식염수 및 인간 혈청 중 예비 배양의 혈청 면역고정 전기영동을 보여준다. MOR202를 식염수(레인 2 내지 3) 또는 혈청(레인 4 내지 13) 중 고정 농도 1200 μg/mL로 상이한 비율의 이의 이디오타입 항체 MOR09292-hAlb와 함께 또는 없이 예비 배양하고 조제된 샘플을 IFE를 통해 항-IgG 염색(레인 2 내지 8) 또는 항-람다 염색(레인 9 내지 13)을 사용하여 분석하였다. (레인 2 = MOR202; 레인 3 = MOR202 + MOR09292-hAlb 2400 μg/mL; 레인 4 = MOR202; 레인 5 = MOR202 + MOR09292-hAlb 1200 μg/mL; 레인 6 = MOR202 + MOR09292-hAlb 1800 μg/mL; 레인 7 = MOR202 + MOR09292-hAlb 2400 μg/mL; 레인 8 = MOR202 + MOR09292-hAlb 3600 μg/mL; 레인 9 = MOR202; 레인 10 = MOR202 + MOR09292-hAlb 1200 μg/mL; 레인 11 = MOR202 + MOR09292-hAlb 1800 μg/mL; 레인 12 = MOR202 + MOR09292-hAlb 2400 μg/mL; 레인 13 = MOR202 + MOR09292-hAlb 3600 μg/mL; 레인 1 = 일반 배경 신호전달을 평가하기 위해 총 단백질에 대하여 염색된 건강한 공여자로부터의 인간 혈청).
도 2a 및 2b는 MOR09292(MOR202에 대한 항-이디오타입 항체) 인간 알부민 융합 단백질의 아미노산 서열을 보여준다.
도 3은 혈청 단백질 전기영동으로 결정된 단백질의 분포에 대한 전형적인 정규 패턴을 보여준다.
도 4는 단클론성 감마글로불린병증으로 알려진 장애에 통상적인 감마-글로불린 구역의 초점 영역에서 균질 스파이크-양 피크를 갖는 단백질의 혈청 단백질 전기영동 분포를 보여준다. 이 피크는 균질 M 단백질을 생산하는 단일 클론의 형질 세포를 나타낸다.
도 5는 건강한 공여자의 혈청 면역고정 전기영동 이후 겔의 예를 보여준다. 레인 ELP = 총 단백질 염색; 레인 G = 항-IgG 염색; 레인 A = 항-IgA 염색; 레인 M = 항-IgM 염색; 레인 K = 항-카파 염색; 레인 L = 항-람다 염색.
도 6은 약물 비처치 건강한 공여자(A 및 B) 및 약물 비처치 MM 환자(C 및 D)로부터의 샘플의 혈청 면역고정 전기영동을 보여준다. 샘플은 상이한 농도로 MOR202를 첨가하거나 첨가하지 않고 시험하였다. (레인 1 = MOR202 첨가하지 않음; 레인 2 = MOR202를 200 μg/mL로 첨가; 레인 3 = MOR202를 400 μg/mL로 첨가; 레인 4 = MOR202를 800 μg/mL로 첨가; 레인 5 = MOR202를 1200 로 μg/mL 첨가). 점선으로 둘러싼 밴드는 MOR202 첨가 후에만 가시적으로 되고 각각의 분자를 나타낸다. 화살표로 표시된 밴드는 내인성 M-단백질을 나타낸다.
도 7은 MOR202 +/- MOR0929 IgG1 및 MOR09292 IgM의 식염수 중 예비 배양의 혈청 면역고정 전기영동을 보여준다. MOR202를 식염수 중 고정 농도 1200 μg/mL(A 및 B) 또는 560 μg/mL(C)로 이의 이디오타입 항체 MOR09292와 상이한 구성 방식으로 예비 배양하고 조제된 샘플을 IFE를 통해 분석하였다. A) + B): MOR202 및 MOR09292 IgG1(항-IgG 염색(A) 및 항-람다 염색(B) 사용)(레인 1 = MOR202; 레인 2 = MOR09292 IgG1 2400 μg/mL; 레인 3 = MOR202 + MOR09292 IgG1 600 μg/mL; 레인 4 = MOR202 + MOR09292 IgG1 1200 μg/mL; 레인 5 = MOR202 + MOR09292 IgG1 2400 μg/mL). C): MOR202 및 MOR09292 IgM(항-IgG 염색(레인 2 내지 4), 항-람다 염색(레인 5 내지 7) 및 항-IgM 염색(레인 8 내지 10) 사용)(레인 2/5/8 = MOR202; 레인 3/6/9 = MOR09292 IgM 560 μg/mL; 레인 4/7/10 = MOR202 + MOR09292 IgM 560 μg/mL; 레인 1 = 혈청 샘플에서 일반 배경 신호전달을 평가하기 위해 총 단백질에 대하여 염색된 건강한 공여자로부터의 인간 혈청).
도 8은 MOR202 +/- MOR09292-인간 알부민 융합체(MOR09292-hAlb)의 식염수 및 인간 혈청 중 예비 배양의 혈청 면역고정 전기영동을 보여준다. MOR202를 식염수(레인 2 내지 3) 또는 혈청(레인 4 내지 13) 중 고정 농도 1200 μg/mL로 상이한 비율의 이의 이디오타입 항체 MOR09292-hAlb와 함께 또는 없이 예비 배양하고 조제된 샘플을 IFE를 통해 항-IgG 염색(레인 2 내지 8) 또는 항-람다 염색(레인 9 내지 13)을 사용하여 분석하였다. (레인 2 = MOR202; 레인 3 = MOR202 + MOR09292-hAlb 2400 μg/mL; 레인 4 = MOR202; 레인 5 = MOR202 + MOR09292-hAlb 1200 μg/mL; 레인 6 = MOR202 + MOR09292-hAlb 1800 μg/mL; 레인 7 = MOR202 + MOR09292-hAlb 2400 μg/mL; 레인 8 = MOR202 + MOR09292-hAlb 3600 μg/mL; 레인 9 = MOR202; 레인 10 = MOR202 + MOR09292-hAlb 1200 μg/mL; 레인 11 = MOR202 + MOR09292-hAlb 1800 μg/mL; 레인 12 = MOR202 + MOR09292-hAlb 2400 μg/mL; 레인 13 = MOR202 + MOR09292-hAlb 3600 μg/mL; 레인 1 = 일반 배경 신호전달을 평가하기 위해 총 단백질에 대하여 염색된 건강한 공여자로부터의 인간 혈청).
실시예
IFE 재료 및 방법
면역고정은 Sebia의 반-자동화된 아가로오스 겔 전기영동 시스템 Hydrasys 및 Hydrasys2를 사용하고 Sebia의 Maxikit Hydragel 9IF를 사용하여 수행되었다. 키트는 면역고정 전기영동에 의해 인간 혈청에서 면역글로불린의 검출을 위해 고안되었고 모든 필요한 시약 및 재료, 즉 아가로오스 겔, 완충 스트립, 희석제, 산 바이올렛 염료, 항혈청(예를 들어, IgG, IgA, IgM, 카파 및 람다), 고정 용액 및 주입기를 포함한다.
M-단백질 분석에서 MOR202의 영향을 평가하기 위해, 건강한 공여자 및 MM 환자로부터의 혈청 샘플에 MOR202를 상이한 농도로 첨가하고 실온(RT)에서 적어도 15분 동안 인큐베이션하였다. 이후 샘플을 MOR202 첨가 또는 비첨가 중 하나로 IFE를 사용하여 분석하고 겔을 항-IgG 또는 항-람다 항혈청(두 염색 시약은 모두 MOR202에 결합할 수 있음)으로 염색하였다. 두 염색 다 MOR202가 시험된 최저 농도 200 μg/mL에서 이미 검출되어, 이 약물 혈청 수준에서나 그 아래에서의 IFE 간섭을 시사하였다(도 6).
IFE에서 MOR202 관련 분석 신호 대 내인성 M-단백질 스파이크 사이를 구별하기 위해 MOR202 함유 샘플을 MOR202 특이적 항-이디오타입 항체 (MOR09292)와 예비 배양하는 방법을 시험하였다. 이 방법의 목적은 MOR202 관련 IFE 분석 신호가 MOR09292의 예비 배양이 있거나 없는 샘플과 비교하여 이동할 수 있음을 입증하는 것이고 이에 따라 MOR202 관련 분석 신호를 명확하게 확인하는 것이다. 이동 거리가 검출될 정도로 충분히 큰지를 평가하기 위해 식염수 중 MOR202를 함유하는 샘플을 조제하고 MOR09292와 함께 또는 MOR09292 없이 예비 배양하였다. 항-이디오타입 항체를 생산하고 IgG1뿐 아니라 IgM 항체 구성 방식에서 시험하였다. 시험 샘플을 1200 μg/mL MOR202의 일정 농도로 조제하고 다양한 농도의 2개 MOR09292 변이형과 함께 또는 이들 없이 60분 동안 예비 배양하였다. 이후, 샘플을 분석하고 IFE 겔을 항-IgG 또는 항-람다 항혈청으로 염색하였다. 결과는 시험 샘플을 다양한 형태의 MOR09292와 함께 예비 배양시 임상 샘플 평가에 적합한 허용 가능한 MOR202 약물 첨가의 이동 거리가 관찰될 수 없다는 것이었다(도 7). 이 놀라운 발견은 약물/항체 복합체의 크기를 약물 항체 단독과 비교하여 대략 3배(MOR09292-IgG) 또는 7배(MOR09292-IgM) 증가 시에도 복합체의 분자량 변화가 분석 신호에서 관련된 이동(즉, 변화된 이동 패턴)을 초래하지 않음을 입증한다.
이들 결과를 기반으로 이디오타입 항체의 추가적인 변이형이 MOR09292-Fab 단편을 인간 인슐린에 유전적으로 융합시켜 생성되었다(MOR09292-hAlb). 새로운 변이형은 약물 항체 단독과 비교하여 약물-항체 복합체의 크기가 2.6배까지 증가하였다. 더욱 중요하게는, 인간 혈청 알부민의 포함이 복합체의 전체 순전하를 저하시켰다. 샘플 조제 및 시험은 위에 기술된 바와 같이 수행하였다. 결과적으로 MOR202 단독의 분석 신호와 비교할 때 MOR202/MOR09292-huAlb 복합체의 명확한 이동이 관찰될 수 있었다. 도 8 참고.
샘플 전처리를 위해 MOR09292-hAlb를 사용한 변형 IFE 분석은 MOR202의 임상 개발로 포함되었다. 이에 따라, 분석은 M-단백질 분석 책임이 있는 중앙 실험실에서 검증되었고 "면역고정(IFE) 반사 분석(Reflex Assay)"으로서 시험 전략으로 도입되었다. MOR202와 M-단백질 관련 신호 사이를 구별하기 위해, 예를 들어 다음 2가지 조건이 만족될 때, 정규 혈청 IFE 및 혈청 단백질 전기영동(SPE)에 추가하여 IFE 반사 분석을 수행하였다:
a) M-단백질 농도 전처리와 비교하여 혈청 M-단백질 수준에서 적어도 = 40% 감소, 및
b) 적어도 하나의 남은 M-단백질 스파이크가 약물 항체 MOR202의 특징과 동일함(즉, IFE에서 IgG / 람다 양성 염색).
MOR202C101 임상 연구 내에서 IFE 반사 분석의 사용 및 결과에 대한 사례 연구
다발성 골수종 환자에 MOR202(MOR202C101)를 처치하는 최초 임상 연구 내에서 IFE 반사 분석을 환자 19007에 혈청 M-단백질 수준에서 ≥86%의 감소가 관찰된 이후 적용하였다. 이 환자에서, 확인된 M-단백질 스파이크는 IFE에 의해 MOR202에서 알려진 동일한 분자적 특성인 IgG / 람다 양성으로 기술되었다. SPE를 수행하여 잠재적 M-단백질의 잔존 농도가 1 또는 2 g/L로 2106년 1월 12일 및 2016년 2월 19일에 검출되었다. IFE 반사 분석은 이 분석 신호가 MOR202 간섭에 의해서만 야기된 것이고, 따라서 M-단백질과 관련이 없음을 입증할 수 있었다(실험실 결과 요약 표 1 참고). 결과는 새로 확립된 IFE 반사 분석이 M-단백질 및 이에 따른 질환 관련 분석 신호 대 MOR202 처치 관련 분석 신호 사이를 명확하게 식별할 수 있음을 입증한다.
표 1: MOR09292-hAlb 샘플 전처리 단계를 적용한 변형 IFE 분석의 임상 용도를 위한 사례 연구 - 환자 19007 실험실 보고서 요약
MOR202 처치 개시 전 환자 19007은 혈청 M-단백질 양성으로 검사받았다 (2016년 7월 27일 접수된 샘플 16 g/L - IFE에서 IgG / 람다에 대한 양성 염색). 혈청 M-단백질 수준에서 ≥86% 감소가 관찰된 후(2015년 12월 14일) IFE 반사 분석이 IFE 및 SPE에 추가하여 수행되었다. 2016년 1월 12일 및 2016년 2월 19일에 각각 잔존 M-단백질 농도 1 또는 2 g/L이 MOR202 분석 간섭에 의해서만 야기되었음을 보여주었다(즉, M-단백질에 대한 면역고정 반사 분석 결과 "음성").
구현예
일 양태는 알부민에 융합된 항-이디오타입 항체이다. 일 구현예에서, 알부민은 서열번호: 6의 아미노산 서열을 갖는 인간 알부민이다. 일 구현예에서, 인간 알부민은 인간 알부민 또는 인간 알부민의 부분 서열의 단편이다.
일 구현예에서, 알부민은 알부민의 기능적 단편이다. 다른 구현예에서, 인간 알부민은 인간 알부민의 기능적 단편이다. 이 문맥에서, 알부민 또는 인간 알부민의 "기능적 단편"이라는 용어는 천연 알부민 또는 인간 알부민의 단편 또는 변이형이지만, 여전히 알부민의 생리적 역할을 수행할 수 있다는 의미에서 여전히 기능적 활성인 알부민을 의미한다.
일 구현예는 아미노산 서열
을 포함하는 가변 중쇄 도메인, 및
아미노산 서열
을 포함하는 가변 경쇄 도메인을 갖는 항체에 특이적인 항-이디오타입 항체이다.
일 양태는 아미노산 서열
을 포함하는 가변 중쇄 도메인, 및
아미노산 서열
을 포함하는 가변 경쇄 도메인을 갖는 항체에 특이적인 항-이디오타입 항체이다. 일 구현예에서 항-이디오타입 항체는 알부민에 융합된다. 일 구현예에서, 알부민은 서열번호: 6의 아미노산 서열을 갖는 인간 알부민이다. 일 구현예에서, 인간 알부민은 인간 알부민 또는 인간 알부민의 부분 서열의 단편이다. 일 구현예에서, 인간 알부민은 인간 알부민 또는 인간 알부민의 부분 서열의 기능적 단편이다.
구현예에서, 항-이디오타입 항체는,
아미노산 서열 YSFSNYWIS(서열번호: 18)의 HCDR1,
아미노산 서열 WMGIIDPASSKTRYSPSFQG(서열번호: 19)의 HCDR2,
아미노산 서열 SRGAGMDY(서열번호: 20)의 HCDR3를 포함하는 가변 중쇄, 및
아미노산 서열 TGSSSNIGAGYDVH(서열번호: 21)의 LCDR1,
아미노산 서열 LLIYADNNRPS(서열번호: 22)의 LCDR2,
아미노산 서열 GSYDESSNSM(서열번호: 23)의 LCDR3를 포함하는 가변 경쇄를 포함한다.
일 구현예에서, 항-이디오타입 항체는 인간 항체이다.
구현예에서, 항-이디오타입 항체는 아미노산 서열
의 가변 중쇄, 및
아미노산 서열
의 가변 경쇄를 포함한다.
구현예에서, 항-이디오타입 항체 알부민 융합체는 다음 중쇄 아미노산 서열을 포함한다.
구현예에서, 항-이디오타입 항체 알부민 융합체는 다음 경쇄 아미노산 서열을 포함한다.
일 양태는 다발성 골수종 또는 다른 감마글로불린병증에 대한 처치를 받는 중인 환자로부터 얻은 혈액 샘플을 평가하는 방법으로, 이 방법은
e) 상기 환자로부터 혈액 샘플을 얻고,
f) 혈액 샘플을 항-이디오타입 항체와 인큐베이션하고,
g) 면역고정 전기영동(IFE)을 수행하고, 그리고
h) IFE의 결과를 보고하는 단계를 포함한다.
방법의 구현예에서, 환자는 아미노산 서열
을 포함하는 가변 중쇄 도메인, 및
아미노산 서열
을 포함하는 가변 경쇄 도메인을 갖는 항체로 처치를 받는 중이다.
방법의 일 구현예에서, 항-이디오타입 항체는 알부민에 융합된다. 방법의 일 구현예에서, 알부민은 서열번호: 6의 아미노산 서열을 갖는 인간 알부민이다. 방법의 일 구현예에서, 인간 알부민은 인간 알부민 또는 인간 알부민의 부분 서열의 단편이다.
예시된 항-이디오타입 항체 MOR09292는 MOR202에 대하여 특이적이다. MOR202에 대한 항-이디오타입 항체는, 인간 알부민에 융합될 때, IFE에서 항체를 이동시켜 M-단백질 기반 임상 평가에서 MOR202의 임의의 잠재적 간섭을 경감시킨다. 다발성 골수종 또는 다른 감마글로불린병증에서의 요법에 사용되는 다른 항체에 대하여 특이적인 다른 항-이디오타입 항체의 융합이 유사한 결과를 가질 것으로 예상된다. 다른 항-이디오타입 항체 알부민 융합은 IFE에서 항체를 이동시켜 M-단백질 기반 임상 평가에서 그 항체의 임의의 잠재적 간섭을 경감시키는 데 유용할 것임을 의미한다.
방법의 구현예에서, 항-이디오타입 항체는,
아미노산 서열 YSFSNYWIS(서열번호: 18)의 HCDR1,
아미노산 서열 WMGIIDPASSKTRYSPSFQG(서열번호: 19)의 HCDR2,
아미노산 서열 SRGAGMDY(서열번호: 20)의 HCDR3를 포함하는 가변 중쇄, 및
아미노산 서열 TGSSSNIGAGYDVH(서열번호: 21)의 LCDR1,
아미노산 서열 LLIYADNNRPS(서열번호: 22)의 LCDR2,
아미노산 서열 GSYDESSNSM(서열번호: 23)의 LCDR3를 포함하는 가변 경쇄를 포함한다.
방법의 구현예에서, 항-이디오타입 항체는 인간 항체이다.
방법의 구현예에서, 항-이디오타입 항체는 아미노산 서열
의 가변 중쇄, 및
아미노산 서열
의 가변 경쇄를 포함한다.
방법의 구현예에서, 항-이디오타입 항체 알부민 융합체는 다음 중쇄 아미노산 서열을 포함한다.
방법의 구현예에서, 항-이디오타입 항체 알부민 융합체는 다음 경쇄 아미노산 서열을 포함한다.
방법의 구현예에서, 샘플은 다발성 골수종 또는 다른 감마글로불린병증에 대한 처치를 받는 중인 환자로부터 얻는다. 추가의 구현예에서, 감마글로불린병증은 단클론성 감마글로불린병증이다. 추가의 구현예에서, 단클론성 감마글로불린병증은 다음을 포함한다: 호지킨 병(Hodgkin's disease); 다발성 골수종의 변이형, 예를 들어 뼈의 고립성 형질세포종, 골수외 형질세포종, 형질 세포성 백혈병, 및 비-분비성 골수종, 림프구증식성 장애, 예를 들어 발덴스트롬 거대글로불린혈증(Waldenstrom's macroglobulinemia), 및 림프종; 중쇄 질환(γ, α, μ); 및 아밀로이드증.
방법의 구현예에서, 샘플은 총 M-단백질 수준에 대하여 평가된다.
일 양태는 예시된 항-이디오타입 항체 또는 항-이디오타입 항체 알부민 융합체를 암호화하는 핵산이다. 일 구현예에서, 항-이디오타입 항체는 MOR09292이다. 일 구현예에서 항-이디오타입 항체는 도 2a 및 2b에 나타낸 아미노산 서열을 암호화하는 핵산 서열에 의해 암호화된다.
일 구현예에서 항-이디오타입 항체는 핵산 서열 서열번호: 26(VH) 및 서열번호: 27(VL)에 의해 암호화된다.
SEQUENCE LISTING
<110> MORPHOSYS AG
<120> CLINICAL ASSESSMENT OF M-PROTEIN RESPONSE IN MULTIPLE MYELOMA
<130> MS241/PCT
<140> EP 16158714.2
<141> 2016-03-04
<160> 28
<170> PatentIn version 3.5
<210> 1
<211> 300
<212> PRT
<213> Homo sapiens
<400> 1
Met Ala Asn Cys Glu Phe Ser Pro Val Ser Gly Asp Lys Pro Cys Cys
1 5 10 15
Arg Leu Ser Arg Arg Ala Gln Leu Cys Leu Gly Val Ser Ile Leu Val
20 25 30
Leu Ile Leu Val Val Val Leu Ala Val Val Val Pro Arg Trp Arg Gln
35 40 45
Gln Trp Ser Gly Pro Gly Thr Thr Lys Arg Phe Pro Glu Thr Val Leu
50 55 60
Ala Arg Cys Val Lys Tyr Thr Glu Ile His Pro Glu Met Arg His Val
65 70 75 80
Asp Cys Gln Ser Val Trp Asp Ala Phe Lys Gly Ala Phe Ile Ser Lys
85 90 95
His Pro Cys Asn Ile Thr Glu Glu Asp Tyr Gln Pro Leu Met Lys Leu
100 105 110
Gly Thr Gln Thr Val Pro Cys Asn Lys Ile Leu Leu Trp Ser Arg Ile
115 120 125
Lys Asp Leu Ala His Gln Phe Thr Gln Val Gln Arg Asp Met Phe Thr
130 135 140
Leu Glu Asp Thr Leu Leu Gly Tyr Leu Ala Asp Asp Leu Thr Trp Cys
145 150 155 160
Gly Glu Phe Asn Thr Ser Lys Ile Asn Tyr Gln Ser Cys Pro Asp Trp
165 170 175
Arg Lys Asp Cys Ser Asn Asn Pro Val Ser Val Phe Trp Lys Thr Val
180 185 190
Ser Arg Arg Phe Ala Glu Ala Ala Cys Asp Val Val His Val Met Leu
195 200 205
Asn Gly Ser Arg Ser Lys Ile Phe Asp Lys Asn Ser Thr Phe Gly Ser
210 215 220
Val Glu Val His Asn Leu Gln Pro Glu Lys Val Gln Thr Leu Glu Ala
225 230 235 240
Trp Val Ile His Gly Gly Arg Glu Asp Ser Arg Asp Leu Cys Gln Asp
245 250 255
Pro Thr Ile Lys Glu Leu Glu Ser Ile Ile Ser Lys Arg Asn Ile Gln
260 265 270
Phe Ser Cys Lys Asn Ile Tyr Arg Pro Asp Lys Phe Leu Gln Cys Val
275 280 285
Lys Asn Pro Glu Asp Ser Ser Cys Thr Ser Glu Ile
290 295 300
<210> 2
<211> 360
<212> DNA
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polynucleotide"
<400> 2
caggtgcaat tggtggaaag cggcggcggc ctggtgcaac cgggcggcag cctgcgtctg 60
agctgcgcgg cctccggatt taccttttct tcttattata tgaattgggt gcgccaagcc 120
cctgggaagg gtctcgagtg ggtgagcggt atctctggtg atcctagcaa tacctattat 180
gcggatagcg tgaaaggccg ttttaccatt tcacgtgata attcgaaaaa caccctgtat 240
ctgcaaatga acagcctgcg tgcggaagat acggccgtgt attattgcgc gcgtgatctt 300
cctcttgttt atactggttt tgcttattgg ggccaaggca ccctggtgac ggttagctca 360
<210> 3
<211> 327
<212> DNA
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polynucleotide"
<400> 3
gatatcgaac tgacccagcc gccttcagtg agcgttgcac caggtcagac cgcgcgtatc 60
tcgtgtagcg gcgataatct tcgtcattat tatgtttatt ggtaccagca gaaacccggg 120
caggcgccag ttcttgtgat ttatggtgat tctaagcgtc cctcaggcat cccggaacgc 180
tttagcggat ccaacagcgg caacaccgcg accctgacca ttagcggcac tcaggcggaa 240
gacgaagcgg attattattg ccagacttat actggtggtg cttctcttgt gtttggcggc 300
ggcacgaagt taaccgttct tggccag 327
<210> 4
<211> 351
<212> DNA
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polynucleotide"
<400> 4
caggtgcaat tggttcagag cggcgcggaa gtgaaaaaac cgggcgaaag cctgaaaatt 60
agctgcaaag gttccggata ttccttttct aattattgga tttcttgggt gcgccagatg 120
cctgggaagg gtctcgagtg gatgggcatt atcgatccgg cttctagcaa gacccgttat 180
tctccgagct ttcagggcca ggtgaccatt agcgcggata aaagcattag caccgcgtat 240
cttcaatgga gcagcctgaa agcgagcgat acggccatgt attattgcgc gcgttctcgt 300
ggtgctggta tggattattg gggccaaggc accctggtga cggttagctc a 351
<210> 5
<211> 339
<212> DNA
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polynucleotide"
<400> 5
gatatcgtgc tgacccagcc gccttcagtg agtggcgcac caggtcagcg tgtgaccatc 60
tcgtgtacgg gcagcagcag caacattggt gctggttatg atgtgcattg gtaccagcag 120
ttgcccggga cggcgccgaa acttctgatt tatgctgata ataatcgtcc ctcaggcgtg 180
ccggatcgtt ttagcggatc caaaagcggc accagcgcga gccttgcgat tacgggcctg 240
caaagcgaag acgaagcgga ttattattgc ggttcttatg atgagtcttc taattctatg 300
gtgtttggcg gcggcacgaa gttaaccgtt cttggccag 339
<210> 6
<211> 609
<212> PRT
<213> Homo sapiens
<400> 6
Met Lys Trp Val Thr Phe Ile Ser Leu Leu Phe Leu Phe Ser Ser Ala
1 5 10 15
Tyr Ser Arg Gly Val Phe Arg Arg Asp Ala His Lys Ser Glu Val Ala
20 25 30
His Arg Phe Lys Asp Leu Gly Glu Glu Asn Phe Lys Ala Leu Val Leu
35 40 45
Ile Ala Phe Ala Gln Tyr Leu Gln Gln Cys Pro Phe Glu Asp His Val
50 55 60
Lys Leu Val Asn Glu Val Thr Glu Phe Ala Lys Thr Cys Val Ala Asp
65 70 75 80
Glu Ser Ala Glu Asn Cys Asp Lys Ser Leu His Thr Leu Phe Gly Asp
85 90 95
Lys Leu Cys Thr Val Ala Thr Leu Arg Glu Thr Tyr Gly Glu Met Ala
100 105 110
Asp Cys Cys Ala Lys Gln Glu Pro Glu Arg Asn Glu Cys Phe Leu Gln
115 120 125
His Lys Asp Asp Asn Pro Asn Leu Pro Arg Leu Val Arg Pro Glu Val
130 135 140
Asp Val Met Cys Thr Ala Phe His Asp Asn Glu Glu Thr Phe Leu Lys
145 150 155 160
Lys Tyr Leu Tyr Glu Ile Ala Arg Arg His Pro Tyr Phe Tyr Ala Pro
165 170 175
Glu Leu Leu Phe Phe Ala Lys Arg Tyr Lys Ala Ala Phe Thr Glu Cys
180 185 190
Cys Gln Ala Ala Asp Lys Ala Ala Cys Leu Leu Pro Lys Leu Asp Glu
195 200 205
Leu Arg Asp Glu Gly Lys Ala Ser Ser Ala Lys Gln Arg Leu Lys Cys
210 215 220
Ala Ser Leu Gln Lys Phe Gly Glu Arg Ala Phe Lys Ala Trp Ala Val
225 230 235 240
Ala Arg Leu Ser Gln Arg Phe Pro Lys Ala Glu Phe Ala Glu Val Ser
245 250 255
Lys Leu Val Thr Asp Leu Thr Lys Val His Thr Glu Cys Cys His Gly
260 265 270
Asp Leu Leu Glu Cys Ala Asp Asp Arg Ala Asp Leu Ala Lys Tyr Ile
275 280 285
Cys Glu Asn Gln Asp Ser Ile Ser Ser Lys Leu Lys Glu Cys Cys Glu
290 295 300
Lys Pro Leu Leu Glu Lys Ser His Cys Ile Ala Glu Val Glu Asn Asp
305 310 315 320
Glu Met Pro Ala Asp Leu Pro Ser Leu Ala Ala Asp Phe Val Glu Ser
325 330 335
Lys Asp Val Cys Lys Asn Tyr Ala Glu Ala Lys Asp Val Phe Leu Gly
340 345 350
Met Phe Leu Tyr Glu Tyr Ala Arg Arg His Pro Asp Tyr Ser Val Val
355 360 365
Leu Leu Leu Arg Leu Ala Lys Thr Tyr Glu Thr Thr Leu Glu Lys Cys
370 375 380
Cys Ala Ala Ala Asp Pro His Glu Cys Tyr Ala Lys Val Phe Asp Glu
385 390 395 400
Phe Lys Pro Leu Val Glu Glu Pro Gln Asn Leu Ile Lys Gln Asn Cys
405 410 415
Glu Leu Phe Glu Gln Leu Gly Glu Tyr Lys Phe Gln Asn Ala Leu Leu
420 425 430
Val Arg Tyr Thr Lys Lys Val Pro Gln Val Ser Thr Pro Thr Leu Val
435 440 445
Glu Val Ser Arg Asn Leu Gly Lys Val Gly Ser Lys Cys Cys Lys His
450 455 460
Pro Glu Ala Lys Arg Met Pro Cys Ala Glu Asp Tyr Leu Ser Val Val
465 470 475 480
Leu Asn Gln Leu Cys Val Leu His Glu Lys Thr Pro Val Ser Asp Arg
485 490 495
Val Thr Lys Cys Cys Thr Glu Ser Leu Val Asn Arg Arg Pro Cys Phe
500 505 510
Ser Ala Leu Glu Val Asp Glu Thr Tyr Val Pro Lys Glu Phe Asn Ala
515 520 525
Glu Thr Phe Thr Phe His Ala Asp Ile Cys Thr Leu Ser Glu Lys Glu
530 535 540
Arg Gln Ile Lys Lys Gln Thr Ala Leu Val Glu Leu Val Lys His Lys
545 550 555 560
Pro Lys Ala Thr Lys Glu Gln Leu Lys Ala Val Met Asp Asp Phe Ala
565 570 575
Ala Phe Val Glu Lys Cys Cys Lys Ala Asp Asp Lys Glu Thr Cys Phe
580 585 590
Ala Glu Glu Gly Lys Lys Leu Val Ala Ala Ser Gln Ala Ala Leu Gly
595 600 605
Leu
<210> 7
<211> 120
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polypeptide"
<400> 7
Gln Val Gln Leu Val Glu Ser Gly Gly Gly Leu Val Gln Pro Gly Gly
1 5 10 15
Ser Leu Arg Leu Ser Cys Ala Ala Ser Gly Phe Thr Phe Ser Ser Tyr
20 25 30
Tyr Met Asn Trp Val Arg Gln Ala Pro Gly Lys Gly Leu Glu Trp Val
35 40 45
Ser Gly Ile Ser Gly Asp Pro Ser Asn Thr Tyr Tyr Ala Asp Ser Val
50 55 60
Lys Gly Arg Phe Thr Ile Ser Arg Asp Asn Ser Lys Asn Thr Leu Tyr
65 70 75 80
Leu Gln Met Asn Ser Leu Arg Ala Glu Asp Thr Ala Val Tyr Tyr Cys
85 90 95
Ala Arg Asp Leu Pro Leu Val Tyr Thr Gly Phe Ala Tyr Trp Gly Gln
100 105 110
Gly Thr Leu Val Thr Val Ser Ser
115 120
<210> 8
<211> 109
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polypeptide"
<400> 8
Asp Ile Glu Leu Thr Gln Pro Pro Ser Val Ser Val Ala Pro Gly Gln
1 5 10 15
Thr Ala Arg Ile Ser Cys Ser Gly Asp Asn Leu Arg His Tyr Tyr Val
20 25 30
Tyr Trp Tyr Gln Gln Lys Pro Gly Gln Ala Pro Val Leu Val Ile Tyr
35 40 45
Gly Asp Ser Lys Arg Pro Ser Gly Ile Pro Glu Arg Phe Ser Gly Ser
50 55 60
Asn Ser Gly Asn Thr Ala Thr Leu Thr Ile Ser Gly Thr Gln Ala Glu
65 70 75 80
Asp Glu Ala Asp Tyr Tyr Cys Gln Thr Tyr Thr Gly Gly Ala Ser Leu
85 90 95
Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly Gln
100 105
<210> 9
<211> 10
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 9
Gly Phe Thr Phe Ser Ser Tyr Tyr Met Asn
1 5 10
<210> 10
<211> 5
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 10
Ser Tyr Tyr Met Asn
1 5
<210> 11
<211> 17
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 11
Gly Ile Ser Gly Asp Pro Ser Asn Thr Tyr Tyr Ala Asp Ser Val Lys
1 5 10 15
Gly
<210> 12
<211> 11
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 12
Asp Leu Pro Leu Val Tyr Thr Gly Phe Ala Tyr
1 5 10
<210> 13
<211> 11
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 13
Ser Gly Asp Asn Leu Arg His Tyr Tyr Val Tyr
1 5 10
<210> 14
<211> 7
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 14
Gly Asp Ser Lys Arg Pro Ser
1 5
<210> 15
<211> 8
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 15
Gln Thr Tyr Thr Gly Gly Ala Ser
1 5
<210> 16
<211> 117
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polypeptide"
<400> 16
Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Glu
1 5 10 15
Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Ser Phe Ser Asn Tyr
20 25 30
Trp Ile Ser Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met
35 40 45
Gly Ile Ile Asp Pro Ala Ser Ser Lys Thr Arg Tyr Ser Pro Ser Phe
50 55 60
Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Ser Thr Ala Tyr
65 70 75 80
Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Met Tyr Tyr Cys
85 90 95
Ala Arg Ser Arg Gly Ala Gly Met Asp Tyr Trp Gly Gln Gly Thr Leu
100 105 110
Val Thr Val Ser Ser
115
<210> 17
<211> 113
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polypeptide"
<400> 17
Asp Ile Val Leu Thr Gln Pro Pro Ser Val Ser Gly Ala Pro Gly Gln
1 5 10 15
Arg Val Thr Ile Ser Cys Thr Gly Ser Ser Ser Asn Ile Gly Ala Gly
20 25 30
Tyr Asp Val His Trp Tyr Gln Gln Leu Pro Gly Thr Ala Pro Lys Leu
35 40 45
Leu Ile Tyr Ala Asp Asn Asn Arg Pro Ser Gly Val Pro Asp Arg Phe
50 55 60
Ser Gly Ser Lys Ser Gly Thr Ser Ala Ser Leu Ala Ile Thr Gly Leu
65 70 75 80
Gln Ser Glu Asp Glu Ala Asp Tyr Tyr Cys Gly Ser Tyr Asp Glu Ser
85 90 95
Ser Asn Ser Met Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly
100 105 110
Gln
<210> 18
<211> 9
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 18
Tyr Ser Phe Ser Asn Tyr Trp Ile Ser
1 5
<210> 19
<211> 20
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 19
Trp Met Gly Ile Ile Asp Pro Ala Ser Ser Lys Thr Arg Tyr Ser Pro
1 5 10 15
Ser Phe Gln Gly
20
<210> 20
<211> 8
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 20
Ser Arg Gly Ala Gly Met Asp Tyr
1 5
<210> 21
<211> 14
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 21
Thr Gly Ser Ser Ser Asn Ile Gly Ala Gly Tyr Asp Val His
1 5 10
<210> 22
<211> 11
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 22
Leu Leu Ile Tyr Ala Asp Asn Asn Arg Pro Ser
1 5 10
<210> 23
<211> 10
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
peptide"
<400> 23
Gly Ser Tyr Asp Glu Ser Ser Asn Ser Met
1 5 10
<210> 24
<211> 816
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polypeptide"
<400> 24
Gln Val Gln Leu Val Gln Ser Gly Ala Glu Val Lys Lys Pro Gly Glu
1 5 10 15
Ser Leu Lys Ile Ser Cys Lys Gly Ser Gly Tyr Ser Phe Ser Asn Tyr
20 25 30
Trp Ile Ser Trp Val Arg Gln Met Pro Gly Lys Gly Leu Glu Trp Met
35 40 45
Gly Ile Ile Asp Pro Ala Ser Ser Lys Thr Arg Tyr Ser Pro Ser Phe
50 55 60
Gln Gly Gln Val Thr Ile Ser Ala Asp Lys Ser Ile Ser Thr Ala Tyr
65 70 75 80
Leu Gln Trp Ser Ser Leu Lys Ala Ser Asp Thr Ala Met Tyr Tyr Cys
85 90 95
Ala Arg Ser Arg Gly Ala Gly Met Asp Tyr Trp Gly Gln Gly Thr Leu
100 105 110
Val Thr Val Ser Ser Ala Ser Thr Lys Gly Pro Ser Val Phe Pro Leu
115 120 125
Ala Pro Ser Ser Lys Ser Thr Ser Gly Gly Thr Ala Ala Leu Gly Cys
130 135 140
Leu Val Lys Asp Tyr Phe Pro Glu Pro Val Thr Val Ser Trp Asn Ser
145 150 155 160
Gly Ala Leu Thr Ser Gly Val His Thr Phe Pro Ala Val Leu Gln Ser
165 170 175
Ser Gly Leu Tyr Ser Leu Ser Ser Val Val Thr Val Pro Ser Ser Ser
180 185 190
Leu Gly Thr Gln Thr Tyr Ile Cys Asn Val Asn His Lys Pro Ser Asn
195 200 205
Thr Lys Val Asp Lys Arg Val Glu Pro Lys Ser Asp Ile Asp Ala His
210 215 220
Lys Ser Glu Val Ala His Arg Phe Lys Asp Leu Gly Glu Glu Asn Phe
225 230 235 240
Lys Ala Leu Val Leu Ile Ala Phe Ala Gln Tyr Leu Gln Gln Cys Pro
245 250 255
Phe Glu Asp His Val Lys Leu Val Asn Glu Val Thr Glu Phe Ala Lys
260 265 270
Thr Cys Val Ala Asp Glu Ser Ala Glu Asn Cys Asp Lys Ser Leu His
275 280 285
Thr Leu Phe Gly Asp Lys Leu Cys Thr Val Ala Thr Leu Arg Glu Thr
290 295 300
Tyr Gly Glu Met Ala Asp Cys Cys Ala Lys Gln Glu Pro Glu Arg Asn
305 310 315 320
Glu Cys Phe Leu Gln His Lys Asp Asp Asn Pro Asn Leu Pro Arg Leu
325 330 335
Val Arg Pro Glu Val Asp Val Met Cys Thr Ala Phe His Asp Asn Glu
340 345 350
Glu Thr Phe Leu Lys Lys Tyr Leu Tyr Glu Ile Ala Arg Arg His Pro
355 360 365
Tyr Phe Tyr Ala Pro Glu Leu Leu Phe Phe Ala Lys Arg Tyr Lys Ala
370 375 380
Ala Phe Thr Glu Cys Cys Gln Ala Ala Asp Lys Ala Ala Cys Leu Leu
385 390 395 400
Pro Lys Leu Asp Glu Leu Arg Asp Glu Gly Lys Ala Ser Ser Ala Lys
405 410 415
Gln Arg Leu Lys Cys Ala Ser Leu Gln Lys Phe Gly Glu Arg Ala Phe
420 425 430
Lys Ala Trp Ala Val Ala Arg Leu Ser Gln Arg Phe Pro Lys Ala Glu
435 440 445
Phe Ala Glu Val Ser Lys Leu Val Thr Asp Leu Thr Lys Val His Thr
450 455 460
Glu Cys Cys His Gly Asp Leu Leu Glu Cys Ala Asp Asp Arg Ala Asp
465 470 475 480
Leu Ala Lys Tyr Ile Cys Glu Asn Gln Asp Ser Ile Ser Ser Lys Leu
485 490 495
Lys Glu Cys Cys Glu Lys Pro Leu Leu Glu Lys Ser His Cys Ile Ala
500 505 510
Glu Val Glu Asn Asp Glu Met Pro Ala Asp Leu Pro Ser Leu Ala Ala
515 520 525
Asp Phe Val Glu Ser Lys Asp Val Cys Lys Asn Tyr Ala Glu Ala Lys
530 535 540
Asp Val Phe Leu Gly Met Phe Leu Tyr Glu Tyr Ala Arg Arg His Pro
545 550 555 560
Asp Tyr Ser Val Val Leu Leu Leu Arg Leu Ala Lys Thr Tyr Glu Thr
565 570 575
Thr Leu Glu Lys Cys Cys Ala Ala Ala Asp Pro His Glu Cys Tyr Ala
580 585 590
Lys Val Phe Asp Glu Phe Lys Pro Leu Val Glu Glu Pro Gln Asn Leu
595 600 605
Ile Lys Gln Asn Cys Glu Leu Phe Glu Gln Leu Gly Glu Tyr Lys Phe
610 615 620
Gln Asn Ala Leu Leu Val Arg Tyr Thr Lys Lys Val Pro Gln Val Ser
625 630 635 640
Thr Pro Thr Leu Val Glu Val Ser Arg Asn Leu Gly Lys Val Gly Ser
645 650 655
Lys Cys Cys Lys His Pro Glu Ala Lys Arg Met Pro Cys Ala Glu Asp
660 665 670
Tyr Leu Ser Val Val Leu Asn Gln Leu Cys Val Leu His Glu Lys Thr
675 680 685
Pro Val Ser Asp Arg Val Thr Lys Cys Cys Thr Glu Ser Leu Val Asn
690 695 700
Arg Arg Pro Cys Phe Ser Ala Leu Glu Val Asp Glu Thr Tyr Val Pro
705 710 715 720
Lys Glu Phe Asn Ala Glu Thr Phe Thr Phe His Ala Asp Ile Cys Thr
725 730 735
Leu Ser Glu Lys Glu Arg Gln Ile Lys Lys Gln Thr Ala Leu Val Glu
740 745 750
Leu Val Lys His Lys Pro Lys Ala Thr Lys Glu Gln Leu Lys Ala Val
755 760 765
Met Asp Asp Phe Ala Ala Phe Val Glu Lys Cys Cys Lys Ala Asp Asp
770 775 780
Lys Glu Thr Cys Phe Ala Glu Glu Gly Lys Lys Leu Val Ala Ala Ser
785 790 795 800
Gln Ala Ala Leu Gly Leu Val Asn Ser Arg His His His His His His
805 810 815
<210> 25
<211> 217
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polypeptide"
<400> 25
Asp Ile Val Leu Thr Gln Pro Pro Ser Val Ser Gly Ala Pro Gly Gln
1 5 10 15
Arg Val Thr Ile Ser Cys Thr Gly Ser Ser Ser Asn Ile Gly Ala Gly
20 25 30
Tyr Asp Val His Trp Tyr Gln Gln Leu Pro Gly Thr Ala Pro Lys Leu
35 40 45
Leu Ile Tyr Ala Asp Asn Asn Arg Pro Ser Gly Val Pro Asp Arg Phe
50 55 60
Ser Gly Ser Lys Ser Gly Thr Ser Ala Ser Leu Ala Ile Thr Gly Leu
65 70 75 80
Gln Ser Glu Asp Glu Ala Asp Tyr Tyr Cys Gly Ser Tyr Asp Glu Ser
85 90 95
Ser Asn Ser Met Val Phe Gly Gly Gly Thr Lys Leu Thr Val Leu Gly
100 105 110
Gln Pro Lys Ala Ala Pro Ser Val Thr Leu Phe Pro Pro Ser Ser Glu
115 120 125
Glu Leu Gln Ala Asn Lys Ala Thr Leu Val Cys Leu Ile Ser Asp Phe
130 135 140
Tyr Pro Gly Ala Val Thr Val Ala Trp Lys Ala Asp Ser Ser Pro Val
145 150 155 160
Lys Ala Gly Val Glu Thr Thr Thr Pro Ser Lys Gln Ser Asn Asn Lys
165 170 175
Tyr Ala Ala Ser Ser Tyr Leu Ser Leu Thr Pro Glu Gln Trp Lys Ser
180 185 190
His Arg Ser Tyr Ser Cys Gln Val Thr His Glu Gly Ser Thr Val Glu
195 200 205
Lys Thr Val Ala Pro Thr Glu Cys Ser
210 215
<210> 26
<211> 2448
<212> DNA
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polynucleotide"
<400> 26
caggtgcaat tggttcagag cggcgcggaa gtgaaaaaac cgggcgaaag cctgaaaatt 60
agctgcaaag gttccggata ttccttttct aattattgga tttcttgggt gcgccagatg 120
cctgggaagg gtctcgagtg gatgggcatt atcgatccgg cttctagcaa gacccgttat 180
tctccgagct ttcagggcca ggtgaccatt agcgcggata aaagcattag caccgcgtat 240
cttcaatgga gcagcctgaa agcgagcgat acggccatgt attattgcgc gcgttctcgt 300
ggtgctggta tggattattg gggccaaggc accctggtga cggttagctc agcctccacc 360
aagggtccat cggtcttccc cctggcaccc tcctccaaga gcacctctgg gggcacagcg 420
gccctgggct gcctggtcaa ggactacttc cccgaaccgg tgacggtgtc gtggaactca 480
ggcgccctga ccagcggcgt gcacaccttc ccggctgtcc tacagtcctc aggactctac 540
tccctcagca gcgtggtgac cgtgccctcc agcagcttgg gcacccagac ctacatctgc 600
aacgtgaatc acaagcccag caacaccaag gtggacaaga gagttgagcc caaatctgat 660
atcgacgccc acaagagcga ggtggcccac cggtttaagg acctgggcga ggaaaacttc 720
aaggccctgg tgctgatcgc cttcgcccag tacctgcagc agtgcccctt cgaggaccac 780
gtgaagctcg tgaacgaagt gaccgagttc gccaagacct gcgtggccga tgagagcgcc 840
gagaactgcg acaagagcct gcacaccctg ttcggcgaca agctgtgtac cgtggccacc 900
ctgagagaaa cctacggcga gatggccgac tgctgcgcca agcaggaacc cgagaggaac 960
gagtgcttcc tgcagcacaa ggacgacaac cccaacctgc ccagactcgt gcggcccgaa 1020
gtggacgtga tgtgcaccgc cttccacgac aacgaggaaa ccttcctgaa gaagtacctg 1080
tacgagatcg ccagacggca cccctacttc tacgcccccg agctgctgtt cttcgccaag 1140
cggtacaagg ccgccttcac cgagtgttgc caggccgccg ataaggccgc ttgcctgctg 1200
cctaagctgg acgagctgag ggatgagggc aaggccagct ctgccaagca gagactgaag 1260
tgcgccagcc tgcagaagtt cggcgagcgg gcctttaaag cctgggccgt ggctagactg 1320
agccagagat tccccaaggc cgagtttgcc gaggtgtcca agctcgtgac cgacctgacc 1380
aaggtgcaca ccgagtgctg tcacggcgac ctgctggaat gcgccgacga cagagccgat 1440
ctggccaagt acatctgcga gaaccaggac agcatcagca gcaagctgaa agagtgctgc 1500
gagaagcctc tgctggaaaa gagccactgt atcgccgagg tggaaaacga cgagatgccc 1560
gccgatctgc cttctctggc cgccgacttc gtggaaagca aggacgtgtg caagaactac 1620
gccgaggcca aggatgtgtt cctgggcatg tttctgtatg agtacgcccg cagacacccc 1680
gactacagcg tggtgctgct gctgagactg gccaaaacct acgagacaac cctggaaaag 1740
tgctgtgccg ccgctgaccc ccacgagtgt tacgccaagg tgttcgacga gttcaagcca 1800
ctggtggaag aaccccagaa cctgatcaag cagaattgcg agctgttcga gcagctgggc 1860
gagtacaagt tccagaacgc cctgctcgtg cggtacacca agaaagtgcc ccaggtgtcc 1920
acccccaccc tggtggaagt gtcccggaac ctgggcaaag tgggcagcaa gtgctgcaag 1980
caccctgagg ccaagagaat gccctgcgcc gaggactacc tgtctgtggt gctgaaccag 2040
ctgtgcgtgc tgcacgagaa aacccccgtg tccgacagag tgaccaagtg ctgtaccgag 2100
agcctcgtga acagacggcc ctgcttcagc gccctggaag tggatgagac atacgtgccc 2160
aaagagttca acgccgagac attcaccttc cacgccgaca tctgcaccct gtccgagaaa 2220
gagcggcaga tcaagaaaca gaccgctctg gtggaactcg tgaagcacaa gcccaaggcc 2280
accaaagaac agctgaaggc cgtgatggac gacttcgccg cctttgtgga aaaatgctgc 2340
aaggccgatg acaaagagac atgcttcgcc gaagagggca agaaactggt ggccgcctct 2400
caggctgctc tgggactggt taactctaga caccatcacc atcaccat 2448
<210> 27
<211> 651
<212> DNA
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
polynucleotide"
<400> 27
gatatcgtgc tgacccagcc gccttcagtg agtggcgcac caggtcagcg tgtgaccatc 60
tcgtgtacgg gcagcagcag caacattggt gctggttatg atgtgcattg gtaccagcag 120
ttgcccggga cggcgccgaa acttctgatt tatgctgata ataatcgtcc ctcaggcgtg 180
ccggatcgtt ttagcggatc caaaagcggc accagcgcga gccttgcgat tacgggcctg 240
caaagcgaag acgaagcgga ttattattgc ggttcttatg atgagtcttc taattctatg 300
gtgtttggcg gcggcacgaa gttaaccgtc ctaggtcagc ccaaggctgc cccctcggtc 360
actctgttcc cgccctcctc tgaggagctt caagccaaca aggccacact ggtgtgtctc 420
ataagtgact tctacccggg agccgtgaca gtggcctgga aggcagatag cagccccgtc 480
aaggcgggag tggagaccac cacaccctcc aaacaaagca acaacaagta cgcggccagc 540
agctatctga gcctgacgcc tgagcagtgg aagtcccaca gaagctacag ctgccaggtc 600
acgcatgaag ggagcaccgt ggagaagaca gtggccccta cagaatgttc a 651
<210> 28
<211> 6
<212> PRT
<213> Artificial Sequence
<220>
<221> source
<223> /note="Description of Artificial Sequence: Synthetic
6xHis tag"
<400> 28
His His His His His His
1 5
Claims (15)
- 알부민 또는 알부민의 기능적 단편에 융합된 항-이디오타입 항체로서,
상기 항-이디오타입 항체는 항-CD38 항체에 특이적이며,
상기 항-이디오타입 항체는,
아미노산 서열 YSFSNYWIS(서열번호: 18)의 HCDR1,
아미노산 서열 WMGIIDPASSKTRYSPSFQG(서열번호: 19)의 HCDR2,
아미노산 서열 SRGAGMDY(서열번호: 20)의 HCDR3를 포함하는 가변 중쇄, 및
아미노산 서열 TGSSSNIGAGYDVH(서열번호: 21)의 LCDR1,
아미노산 서열 LLIYADNNRPS(서열번호: 22)의 LCDR2,
아미노산 서열 GSYDESSNSM(서열번호: 23)의 LCDR3를 포함하는 가변 경쇄를 포함하는 것을 특징으로 하는, 항-이디오타입 항체. - 제1항에 있어서, 항-이디오타입 항체는 아미노산 서열
을 포함하는 가변 중쇄 도메인, 및
아미노산 서열
을 포함하는 가변 경쇄 도메인을 갖는 항-CD38 항체에 특이적인 항-이디오타입 항체. - 삭제
- 제1항에 있어서, 상기 항-이디오타입 항체는 아미노산 서열
의 가변 중쇄, 및
아미노산 서열
의 가변 경쇄를 포함하는, 항-이디오타입 항체. - 제1항에 있어서, 중쇄는 다음 아미노산 서열을 포함하는 항-이디오타입 항체.
- 제1항에 있어서, 경쇄는 다음 아미노산 서열을 포함하는 항-이디오타입 항체.
- 제1항에 있어서, 혈액 샘플을 평가하는 데 사용하기 위한 항-이디오타입 항체.
- 제1항, 제2항 및 제4항 내지 제7항 중 어느 한 항에 따른 항-이디오타입 항체를 암호화하는 핵산.
- 다발성 골수종 또는 다른 감마글로불린병증에 대한 처치를 받는 중인 환자의 혈액 샘플을 평가하기 위한 정보 제공 방법으로서,
a) 혈액 샘플을 제1항, 제2항 및 제4항 내지 제7항 중 어느 한 항에 따른 항-이디오타입 항체와 인큐베이션하는 단계,
b) 면역고정 전기영동(immunofixation electrophoresis, IFE)을 수행하는 단계, 및
c) IFE의 결과를 보고하는 단계를 포함하는, 방법. - 제9항에 있어서, 환자는 아미노산 서열
을 포함하는 가변 중쇄 도메인, 및
아미노산 서열
을 포함하는 가변 경쇄 도메인을 갖는 항-CD38 항체로 처치를 받는 중인 것을 특징으로 하는, 방법. - 제9항에 있어서, 샘플은 총 M-단백질 수준에 대하여 평가되는 것을 특징으로 하는, 방법.
- 아미노산 서열
을 포함하는 가변 중쇄 도메인, 및
아미노산 서열
을 포함하는 가변 경쇄 도메인을 갖는 항-CD38 항체에 특이적인 항-이디오타입 항체. - 다발성 골수종 또는 다른 감마글로불린병증에 대한 처치를 받는 중인 환자의 혈액 샘플을 평가하기 위한 정보 제공 방법으로서,
a) 혈액 샘플을 항-이디오타입 항체와 인큐베이션하는 단계,
b) 면역고정 전기영동(immunofixation electrophoresis, IFE)을 수행하는 단계, 및
c) IFE의 결과를 보고하는 단계를 포함하는 방법에 있어서,
환자는 아미노산 서열
을 포함하는 가변 중쇄 도메인, 및
아미노산 서열
을 포함하는 가변 경쇄 도메인을 갖는 항-CD38 항체로 처치를 받는 중인 것을 특징으로 하는, 방법. - 제12항에 있어서, 상기 항-이디오타입 항체는,
아미노산 서열 YSFSNYWIS(서열번호: 18)의 HCDR1,
아미노산 서열 WMGIIDPASSKTRYSPSFQG(서열번호: 19)의 HCDR2,
아미노산 서열 SRGAGMDY(서열번호: 20)의 HCDR3를 포함하는 가변 중쇄, 및
아미노산 서열 TGSSSNIGAGYDVH(서열번호: 21)의 LCDR1,
아미노산 서열 LLIYADNNRPS(서열번호: 22)의 LCDR2,
아미노산 서열 GSYDESSNSM(서열번호: 23)의 LCDR3를 포함하는 가변 경쇄를 포함하는 것인, 항체. - 제13항에 있어서, 상기 항-이디오타입 항체는,
아미노산 서열 YSFSNYWIS(서열번호: 18)의 HCDR1,
아미노산 서열 WMGIIDPASSKTRYSPSFQG(서열번호: 19)의 HCDR2,
아미노산 서열 SRGAGMDY(서열번호: 20)의 HCDR3를 포함하는 가변 중쇄, 및
아미노산 서열 TGSSSNIGAGYDVH(서열번호: 21)의 LCDR1,
아미노산 서열 LLIYADNNRPS(서열번호: 22)의 LCDR2,
아미노산 서열 GSYDESSNSM(서열번호: 23)의 LCDR3를 포함하는 가변 경쇄를 포함하는 것인, 방법.
Applications Claiming Priority (3)
| Application Number | Priority Date | Filing Date | Title |
|---|---|---|---|
| EP16158714 | 2016-03-04 | ||
| EP16158714.2 | 2016-03-04 | ||
| PCT/EP2017/055011 WO2017149122A1 (en) | 2016-03-04 | 2017-03-03 | Clinical assessment of m-protein response in multiple myeloma |
Publications (2)
| Publication Number | Publication Date |
|---|---|
| KR20180118151A KR20180118151A (ko) | 2018-10-30 |
| KR102427948B1 true KR102427948B1 (ko) | 2022-08-02 |
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| KR1020187026496A KR102427948B1 (ko) | 2016-03-04 | 2017-03-03 | 다발성 골수종에서 m-단백질 반응의 임상 평가 |
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|---|---|
| US (2) | US11618789B2 (ko) |
| EP (1) | EP3423498A1 (ko) |
| JP (3) | JP7362250B2 (ko) |
| KR (1) | KR102427948B1 (ko) |
| CN (1) | CN108699161B (ko) |
| AU (2) | AU2017226960B2 (ko) |
| CA (1) | CA3016098A1 (ko) |
| IL (2) | IL305540A (ko) |
| SG (1) | SG11201806214RA (ko) |
| WO (1) | WO2017149122A1 (ko) |
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| WO2019209730A1 (en) | 2018-04-24 | 2019-10-31 | Helena Laboratories Corporation | Removal of interfering factors from serum protein electrophoresis profiles |
| AU2019338999A1 (en) | 2018-09-11 | 2021-03-18 | Jiangsu Hengrui Medicine Co., Ltd. | Anti-CD38 antibody, antigen-binding fragment thereof, and pharmaceutical use |
| WO2020187718A1 (en) | 2019-03-15 | 2020-09-24 | Morphosys Ag | Anti-cd38 antibodies and pharmaceutical compositions thereof for the treatment of autoantibody-mediated autoimmune disease |
| WO2023094696A1 (en) * | 2021-11-29 | 2023-06-01 | Morphosys Ag | Methods for reducing anti-cd38 mab drug interference in serological assays |
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| JOP20210044A1 (ar) | 2010-12-30 | 2017-06-16 | Takeda Pharmaceuticals Co | الأجسام المضادة لـ cd38 |
| BR112014024291B1 (pt) | 2012-03-30 | 2022-07-05 | The Board Of Regents Of The University Of Oklahoma | Método para a produção de forma recombinante de um polímero de heparosan com alto peso molecular, uso do referido polímero para aumento de tecido, polinucleotídeo isolado e composição de material biológico compreendendo o referido polímero |
| CA2885792C (en) | 2012-09-25 | 2021-09-28 | Jan Endell | Pharmaceutical combination of an anti-cd38 antibody and melphalan for treating multiple myeloma |
| EA033115B1 (ru) | 2013-04-29 | 2019-08-30 | Тева Фармасьютикалз Острэйлиа Пти Лтд. | АНТИТЕЛА ПРОТИВ CD38 И СЛИТЫЕ БЕЛКИ С ОСЛАБЛЕННЫМ ИНТЕРФЕРОНОМ АЛЬФА-2b |
| CA2927099A1 (en) | 2013-10-31 | 2015-05-07 | Sanofi | Specific anti-cd38 antibodies for treating human cancers |
| US10836998B2 (en) * | 2014-02-14 | 2020-11-17 | Cellectis | Cells for immunotherapy engineered for targeting antigen present both on immune cells and pathological cells |
-
2017
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- 2017-03-03 US US16/080,870 patent/US11618789B2/en active Active
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- 2017-03-03 EP EP17708766.5A patent/EP3423498A1/en active Pending
- 2017-03-03 CA CA3016098A patent/CA3016098A1/en active Pending
- 2017-03-03 IL IL305540A patent/IL305540A/en unknown
- 2017-03-03 JP JP2018545438A patent/JP7362250B2/ja active Active
- 2017-03-03 IL IL260750A patent/IL260750B2/en unknown
- 2017-03-03 SG SG11201806214RA patent/SG11201806214RA/en unknown
- 2017-03-03 KR KR1020187026496A patent/KR102427948B1/ko active IP Right Grant
- 2017-03-03 WO PCT/EP2017/055011 patent/WO2017149122A1/en active Application Filing
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2022
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Patent Citations (2)
| Publication number | Priority date | Publication date | Assignee | Title |
|---|---|---|---|---|
| US20080066741A1 (en) | 2006-09-20 | 2008-03-20 | Lemahieu Edward | Methods and systems of delivering medication via inhalation |
| US20130302318A1 (en) | 2010-09-27 | 2013-11-14 | Lisa Rojkjaer | Anti-CD38 Antibody and Lenalidomide or Bortezomib for the Treatment of Multipe Myeloma and NHL |
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| Publication number | Publication date |
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| JP2019513346A (ja) | 2019-05-30 |
| JP7362250B2 (ja) | 2023-10-17 |
| IL260750A (ko) | 2018-09-20 |
| AU2017226960A1 (en) | 2018-08-09 |
| US20230203189A1 (en) | 2023-06-29 |
| IL260750B1 (en) | 2023-10-01 |
| CN108699161B (zh) | 2022-06-03 |
| IL260750B2 (en) | 2024-02-01 |
| WO2017149122A1 (en) | 2017-09-08 |
| AU2017226960B2 (en) | 2024-03-21 |
| US20190077875A1 (en) | 2019-03-14 |
| CA3016098A1 (en) | 2017-09-08 |
| IL305540A (en) | 2023-10-01 |
| JP2022058881A (ja) | 2022-04-12 |
| AU2024201503A1 (en) | 2024-03-28 |
| US11618789B2 (en) | 2023-04-04 |
| JP7331168B2 (ja) | 2023-08-22 |
| JP2023157927A (ja) | 2023-10-26 |
| SG11201806214RA (en) | 2018-08-30 |
| CN108699161A (zh) | 2018-10-23 |
| EP3423498A1 (en) | 2019-01-09 |
| KR20180118151A (ko) | 2018-10-30 |
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