ES2546333T3 - Anticuerpos monoclonales humanos para ligandos 1 (PD-L1) de muerte programada - Google Patents

Anticuerpos monoclonales humanos para ligandos 1 (PD-L1) de muerte programada Download PDF

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Publication number
ES2546333T3
ES2546333T3 ES06786260.7T ES06786260T ES2546333T3 ES 2546333 T3 ES2546333 T3 ES 2546333T3 ES 06786260 T ES06786260 T ES 06786260T ES 2546333 T3 ES2546333 T3 ES 2546333T3
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seq
chain variable
variable region
cdr3
cdr2
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Alan J. Korman
Mark J. Selby
Changyu Wang
Mohan Srinivasan
David B. Passmore
Haichun Huang
Haibin Chen
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ER Squibb and Sons LLC
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ER Squibb and Sons LLC
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    • C07K16/2827—Immunoglobulins [IG], e.g. monoclonal or polyclonal antibodies against material from animals or humans against receptors, cell surface antigens or cell surface determinants against the immunoglobulin superfamily against B7 molecules, e.g. CD80, CD86
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Abstract

Un anticuerpo monoclonal humano aislado o una porción de enlace a antígeno del mismo que se enlazan específicamente a PD-L1, que comprende: (a) una región variable de cadena pesada CDR1 que comprende aminoácidos que tienen la secuencia definida en la SEC ID nº 22; (b) una región variable de cadena pesada CDR2 que comprende aminoácidos que tienen la secuencia definida en la SEC ID nº 32; (c) una región variable de cadena pesada CDR3 que comprende aminoácidos que tienen la secuencia definida en la SEC ID nº 42; (d) una región variable de cadena ligera CDR1 que comprende aminoácidos que tienen la secuencia definida en la SEC ID nº 52; (e) una región variable de cadena ligera CDR2 que comprende aminoácidos que tienen la secuencia definida en la SEC ID nº 62 y (f) una región variable de cadena ligera CDR3 que comprende aminoácidos que tienen la secuencia definida en la SEC ID nº 72.

Description

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(a) una región variable de cadena pesada CDR1 que comprende la SEC ID Nº:24;
(b) una región variable de cadena pesada CDR2 que comprende la SEC ID Nº:34;
(c) una región variable de cadena pesada CDR3 que comprende la SEC ID Nº:44; 5 (d) una región variable de cadena ligera CDR1 que comprende la SEC ID Nº: 54;
(e) una región variable de cadena ligera CDR2 que comprende la SEC ID Nº:64; y
(f) una región variable de cadena ligera CDR3 que comprende la SEC ID Nº:74.
(a) una región variable de cadena pesada CDR1 que comprende la SEC ID Nº:25;
(b) una región variable de cadena pesada CDR2 que comprende la SEC ID Nº:35;
(c) una región variable de cadena pesada CDR3 que comprende la SEC ID Nº:45;
(d) una región variable de cadena ligera CDR1 que comprende la SEC ID Nº:55;
(e) una región variable de cadena ligera CDR2 que comprende la SEC ID Nº:65; y 15 (f) una región variable de cadena ligera CDR3 que comprende la SEC ID Nº:75.
(a) una región variable de cadena pesada CDR1 que comprende la SEC ID Nº:26;
(b) una región variable de cadena pesada CDR2 que comprende la SEC ID Nº:36;
(c) una región variable de cadena pesada CDR3 que comprende la SEC ID Nº:46;
(d) una región variable de cadena ligera CDR1 que comprende la SEC ID Nº:56;
(e) una región variable de cadena ligera CDR2 que comprende la SEC ID Nº:66; y
(f) una región variable de cadena ligera CDR3 que comprende la SEC ID Nº:76.
(a) una región variable de cadena pesada CDR1 que comprende la SEC ID Nº:27; 25
(b) una región variable de cadena pesada CDR2 que comprende la SEC ID Nº:37;
(c) una región variable de cadena pesada CDR3 que comprende la SEC ID Nº:47;
(d) una región variable de cadena ligera CDR1 que comprende la SEC ID Nº:57;
(e) una región variable de cadena ligera CDR2 que comprende la SEC ID Nº:67; y
(f) una región variable de cadena ligera CDR3 que comprende la SEC ID Nº:77.
(a) una región variable de cadena pesada CDR1 que comprende la SEC ID Nº:28;
(b) una región variable de cadena pesada CDR2 que comprende la SEC ID Nº:38; 35 (c) una región variable de cadena pesada CDR3 que comprende la SEC ID Nº:48;
(d) una región variable de cadena ligera CDR1 que comprende la SEC ID Nº:58;
(e) una región variable de cadena ligera CDR2 que comprende la SEC ID Nº:68; y
(f) una región variable de cadena ligera CDR3 que comprende la SEC ID Nº:78.
(a) una región variable de cadena pesada CDR1 que comprende la SEC ID Nº:29;
(b) una región variable de cadena pesada CDR2 que comprende la SEC ID Nº:39;
(c) una región variable de cadena pesada CDR3 que comprende la SEC ID Nº:49;
(d) una región variable de cadena ligera CDR1 que comprende la SEC ID Nº:59; 45 (e) una región variable de cadena ligera CDR2 que comprende la SEC ID Nº:69; y
(f) una región variable de cadena ligera CDR3 que comprende la SEC ID Nº:79.
(a) una región variable de cadena pesada CDR1 que comprende la SEC ID Nº:30;
(b) una región variable de cadena pesada CDR2 que comprende la SEC ID Nº:40;
(c) una región variable de cadena pesada CDR3 que comprende la SEC ID Nº:50;
(d) una región variable de cadena ligera CDR1 que comprende la SEC ID Nº:60;
(e) una región variable de cadena ligera CDR2 que comprende la SEC ID Nº:70; y
(f) una región variable de cadena ligera CDR3 que comprende la SEC ID Nº:80. 55 Anticuerpos que tienen secuencias de línea germinal particular
En ciertas realizaciones, un anticuerpo de la invención comprende una región variable de cadena pesada de un gen de inmunoglobulina de cadena pesada de línea germinal particular y/o una región variable de cadena ligera de un gen de inmunoglobulina de cadena ligera de línea germinal particular. Además, se describe en el presente documento un anticuerpo monoclonal aislado, o una porción de enlace a antígeno del mismo, que anticuerpo se enlaza específicamente a PD-L1 y que comprende una región variable de cadena pesada que es el producto o se deriva de un gen VH 1-18 humano; una región variable de cadena pesada que es el producto o se deriva de un gen VH 1-69 humano; una región variable de cadena pesada que es el producto o se deriva de un gen VH 1-3 humano; 65 una región variable de cadena pesada que es el producto o se deriva de un gen VH 3-9 humano; una región variable de cadena ligera que es el producto o se deriva de un gen VK L6 humano; una región variable de cadena ligera que
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(g)
el anticuerpo estimula las respuestas del anticuerpo; y
(h)
invierte el efecto de células reguladoras T sobre células efectoras de células T y/o células dendríticas.
En otras realizaciones, la secuencia de aminoácidos VH y/o VL puede ser 85 %, 90 %, 95 %, 96 %, 97 %, 98 % o 99
5 % homóloga a las secuencias establecidas arriba. Un anticuerpo que tiene regiones VH y VL que tienen alta (es decir, 80 % o más) homología a las regiones VH y VL de las secuencias establecidas arriba, puede obtenerse por mutagénesis (por ejemplo, mutagénesis mediada por PCR o dirigida a sitio) de moléculas de ácido nucleico que codifican SEC ID Nos:25, 26, 27, 28, 29, y 30, seguido por la prueba del anticuerpo alterado codificado para función retenida (es decir, las funciones establecidas en (c) a (h) arriba) utilizando los ensayos funcionales descritos en el presente documento.
Como se utiliza en el presente documento, el porcentaje de homología entre dos secuencias de aminoácidos es equivalente al porcentaje de identidad entre las dos secuencias. El porcentaje de identidad entre las dos secuencias es una función del número de posiciones idénticas compartidas por las secuencias (es decir, % homología = # de
15 posiciones idénticas/total # de posiciones x 100), tomando en cuenta el número de espacios, y la longitud de cada espacio, que no necesita introducirse para alineación óptima de las dos secuencias. La comparación de secuencias y determinación del porcentaje de identidad entre dos secuencias puede realizarse utilizando un algoritmo matemático, como se describe en los ejemplos no limitantes abajo. El porcentaje de identidad entre dos secuencias de aminoácidos puede determinarse utilizando el algoritmo de E. Meyers y W. Miller (Comput. Appl. Biosci., 4:11-17 (1988)) que se ha incorporado en el programa ALIGN (versión 2.0), utilizando una tabla de residuo de peso PAM120, una penalidad de longitud de espacio de 12 y una penalidad de espacio de 4. Además, el porcentaje de identidad entre dos secuencias de aminoácidos puede determinarse utilizando el algoritmo Needleman y Wunsch (J. Mol. Biol. 48:444-453 (1970)) que se ha incorporado en el programa GAP en el paquete de software GCG (disponible en www.gcg.com), utilizando ya sea una matriz Blossum 62 o una
25 matriz PAM250, y un peso de espacio de 16, 14, 12, 10, 8, 6, o 4 y un peso de longitud de 1, 2, 3, 4, 5, o 6.
En ciertos casos, las secuencias de proteína de la invención pueden utilizarse además como una “secuencia de consulta” para realizar una consulta contra bases de datos públicas para, por ejemplo, identificar secuencias relacionadas. Tales búsquedas pueden realizarse utilizando el programa XBLAST (versión 2.0) de Altschul, et al. (1990) J. Mol. Biol. 215:403-10. Las búsquedas de proteína BLAST pueden realizarse con el programa XBLAST, puntuación = 50, longitud de palabra = 3 para obtener secuencias de aminoácidos homólogas a las moléculas de anticuerpo de la invención. Para obtener alineaciones espaciadas para propósitos de comparación, Gapped BLAST espaciado puede utilizarse como se describe en Altschul et al, (1997) Nucleic Acids Res. 25(17):3389-3402. Cuando se utilizan los programas BLAST y Gapped BLAST, los parámetros de falla de los programas respectivos (por
35 ejemplo, XBLAST y NBLAST) pueden utilizarse. Ver www.ncbi.nlm.nih.gov.
Anticuerpos Modificados y Formados
Un anticuerpo de la invención puede prepararse además utilizando un anticuerpo que tiene una o más de las secuencias VH y/o VL descritas en el presente documento como material inicial para formar un anticuerpo modificado, tal anticuerpo modificado puede tener propiedades alteradas del anticuerpo inicial. Un anticuerpo puede formarse al modificar uno o más residuos dentro de una o ambas regiones variables {es decir, VH y/o VL), por ejemplo dentro de una o más regiones CDR y/o dentro de una o más regiones de estructura. Adicional o alternativamente, un anticuerpo puede formarse al modificar residuos dentro de la(s) región(es) constante(s), por
45 ejemplo para alterar la(s) función(es) efector(as) del anticuerpo.
Un tipo de formación de región variable que puede realizarse es injerto CDR. Los anticuerpos interactúan con antígenos objetivo predominantemente a través de residuos de aminoácido que se ubican en las seis regiones de determinación de complemento de cadena pesada y ligera (CDR). Por esta razón, las secuencias de aminoácidos dentro de CDR son más diversas entre anticuerpos individuales que secuencias fuera de CDR. Debido a que las secuencias CDR son responsables de la mayoría de las interacciones de anticuerpo-antígeno, es posible expresar anticuerpos recombinantes que imitan las propiedades de anticuerpos que ocurren de manera natural específicos al construir vectores de expresión que incluyen secuencias CDR del anticuerpo que ocurre de manera natural específico injertado en secuencias de estructura de un anticuerpo diferente con diferentes propiedades (ver, por 55 ejemplo, Riechmann, L. et al. (1998) Nature 332:323-327; Jones, P. et al. (1986) Nature 321:522-525; Queen, C. et al. (1989) Proc. Natl. Acad. Ver. U.S.A. 86:10029-10033; Patente de E.U. No. 5,225,539 para Winter, y Patentes de
E.U. Nos. 5,530,101; 5,585,089; 5,693,762 y 6,180,370 para Queen et al.)
De acuerdo con lo anterior, otra realización de la invención pertenece a un anticuerpo monoclonal aislado, o porción de enlace a antígeno del mismo, que comprende una región variable de cadena pesada que comprende secuencias CDR1, CDR2, y CDR3 que comprenden una secuencia de aminoácidos seleccionada del grupo que consiste de la SEC ID Nº 22 y la SEC ID Nº 32 y la SEC ID Nº 42respectivamente, y una región variable de cadena ligera que comprende secuencias CDR1, CDR2, y CDR3 que comprenden una secuencia de aminoácidos seleccionada del grupo que consiste de la SEC ID Nº 52, la SEC ID Nº 62, y la SEC ID Nº 72SEC, respectivamente. De esta manera,
65 tales anticuerpos contienen las secuencias CDR VH y VL del anticuerpo monoclonal 12A4 pero que puede contener diferentes secuencias de estructura de estos anticuerpos.
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VH 1-69 de línea germinal de origen se muestra en la Figura 16. La alineación de la región VH para 7H1 contra la secuencia VH 1-69 de línea germinal de origen se muestra en la Figura 17. La alineación de la región VH para 11E6 contra la secuencia VH 1-69 de línea germinal de origen se muestra en la Figura 18. La alineación de la región VH para 12B7 contra la secuencia VH 1-69 de línea germinal de origen se muestra en la Figura 19. La alineación de la
5 región VH para 13G4 contra la secuencia VH 3-9 de línea germinal de origen se muestra en la Figura 20.
Por ejemplo, para 12A4, el residuo de aminoácido #24 (dentro de FRl) de VH es una treonina mientras este residuo en la secuencia de línea germinal VH 1-69 correspondiente es una alanina..
Para devolver las secuencias de región de estructura a su configuración de línea germinal, por ejemplo, el resto nº24 de VH de 12A4 puede ser “mutado de nuevo” de treonina a alanina. También está previsto que estos anticuerpos “mutados de nuevo” están comprendidos en la invención.
Como otro ejemplo, para 12A4, el resto de aminoácido nº27 (dentro de FRl) de VH es un ácido aspártico mientras
15 este resto en la secuencia de línea germinal VH 1-69 correspondiente es una glicina alanina. Para regresar las secuencias de región de estructura a su configuración de línea germinal, por ejemplo, el resto nº 27 de VH de 12A4 puede ser “mutado de nuevo” de ácido aspártico a glicina. También está previsto que estos anticuerpos “mutados de nuevo” están comprendidos en la invención. Otro tipo de modificación de estructura incluye mutar uno o más restos dentro de la región de estructura, para remover los epítopos de células T para reducir así la inmunogenicidad potencial del anticuerpo. Este planteamiento también se refiere a como “de inmunización” y se describe en más detalle en la Publicación de Patente de E.U. No. 20030153043 por Carr et al.
Además o alternativo a las modificaciones hechas dentro de la estructura o región CDR, anticuerpos de la invención
25 pueden formarse para incluir modificaciones dentro de la región Fc, normalmente para alterar una o más propiedades funcionales del anticuerpo, como vida media en suero, fijación complemento), enlace a receptor Fc, y/o citotoxicidad celular dependiente a antígeno. Además, un anticuerpo de la invención puede modificarse químicamente (por ejemplo, uno o más restos químicos pueden unirse al anticuerpo) o modificarse para alterar su glicosilación, de nuevo para alterar una o más propiedades funcionales del anticuerpo. Cada una de estas realizaciones se describe en más detalle abajo. La numeración de los restos en la región Fc es aquella del índice EU de Kabat.
En una realización, la región de articulación de CHl se modifica de manera que el número de restos de cisteína en la región de articulación se altera, por ejemplo, aumenta o disminuye. Este planteamiento se describe además en la
35 Patente de Estados Unidos Nº 5.677.425 por Bodmer et al. El número de restos de cisteína en la región de articulación de CHl se altera, por ejemplo, para facilitar el ensamble de las cadenas pesadas y ligeras o para incrementar o disminuir la estabilidad del anticuerpo.
En otra realización, la región de articulación Fc de un anticuerpo se muta para disminuir la vida media biológica del anticuerpo. Más específicamente, una o más mutaciones de aminoácido se introducen en la región de interfase de dominio CH2-CH3 del fragmento de articulación Fc de manera que el anticuerpo tiene enlace de proteína A estafilocócica (SpA) deteriorado relativo a dominio de articulación Fc nativo de enlace de SpA. Este planteamiento se describe en más detalle en la Patente de Estados Unidos Nº 6.165.745 por Ward et al.
45 En otra realización, el anticuerpo se modifica para incrementar su vida media biológica. Varios planteamientos son posibles. Por ejemplo, una o más de las siguientes mutaciones pueden introducirse: T252L, T254S, T256F, como se describe en la Patente de Estados Unidos Nº 6.277.375 para Ward. Alternativamente, para incrementar la vida media biológica, el anticuerpo puede alterarse dentro de la región CHl o CL para contener un epítopo de enlace al receptor silvestre tomado de dos ciclos de un dominio CH2 de una región Fc de una IgG, como se describe en las Patentes de Estados Unidos números 5.869.046 y 6.121.022 por Presta et al.
En todavía otras realizaciones, la región Fc se altera al reemplazar al menos un resto de aminoácido con un resto de aminoácido diferente para alterar la(s) función(es) efector(as) del anticuerpo. Por ejemplo, uno o más aminoácidos seleccionados de restos de aminoácido 234, 235, 236, 237, 297, 318, 320 y 322 pueden reemplazarse con un resto
55 de aminoácido diferente de manera que el anticuerpo tiene afinidad alterada para un ligando efectuador pero mantiene la capacidad de enlace a antígeno del anticuerpo de origen. El ligando efectuador al cual se altera la afinidad puede ser, por ejemplo, un receptor Fc o el componente C1 del complemento. Este planteamiento se describe en más detalle en las Patentes de Estados Unidos números . 5.624.821 y 5.648.260, ambas para Winter et al.
En otro ejemplo, uno o más aminoácidos seleccionados de restos de aminoácido 329, 331 y 322 pueden reemplazarse con un resto de aminoácido diferente de manera que el anticuerpo tiene enlace C1q alterado y/o citotoxicidad dependiente de complemento (CDC) eliminada o reducida. Este planteamiento se describe en más detalle en las Patentes de Estados Unidos números 6.194.551 de Idusogie et al.
65 En otro ejemplo, uno o más restos de aminoácido dentro de las posiciones de aminoácido 231 y 239 se alteran para alterar así la capacidad del anticuerpo para fijar el complemento. Este planteamiento se describe además en
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VH a.a 12A4 27 VH CDR1 a.a 7H1
3
VH a.a 10A5 28 VH CDR1 a.a 11E6
4
VH a.a 5F8 29 VH CDR1 a.a 12B7
5
VH a.a 10H10 30 VH CDR1 a.a 13G4
6
VH a.a 1B12
7
VH a.a 7H1 31 VH CDR2 a.a 3G10
8
VH a.a 11E6 32 VH CDR2 a.a 12A4
9
VH a.a 12B7 33 VH CDR2 a.a 10A5
10
VH a.a 13G4 34 VH CDR2 a.a 5F8
35
VH CDR2 a.a. 10H10
11
VK a.a. 3G10 36 VH CDR2 a.a. 1B12
12
VK a.a. 12A4 37 VH CDR2 a.a. 7H1
13
VK a.a. 10A5 38 VH CDR2 a.a. 11E6
14
VK a.a. 5F8 39 VH CDR2 a.a. 12B7
15
VK a.a. 10H10 40 VH CDR2 a.a. 13G4
16
VK a.a. 1B12
17
VK a.a. 7H1 41 VH CDR3 a.a. 3G10
18
VK a.a. 11E6 42 VH CDR3 a.a. 12A4
19
VK a.a. 12B7 43 VH CDR3 a.a. 10A5
20
VK a.a. 13G4 44 VH CDR3 a.a. 5F8
45
VH CDR3 a.a. 10H10
21
VH CDR1 a.a. 3G10 46 VH CDR3 a.a. 1B12
22
VH CDR1 a.a. 12A4 47 VH CDR3 a.a. 7H1
23
VH CDR1 a.a. 10A5 48 VH CDR3 a.a. 11E6
24
VH CDR1 a.a. 5F8 49 VH CDR3 a.a. 12B7
25
VH CDR1 a.a. 10H10 50 VH CDR3 a.a. 13G4
51
VH CDR1 a.a. 3G10 79 VK CDR3 a.a. 12B7
52
VH CDR1 a.a. 12A4 80 VK CDR3 a.a. 13G4
53
VH CDR1 a.a. 10A5
54
VH CDR1 a.a. 5F8 81 VH n.t. 3G10
55
VH CDR1 a.a. 10H10 82 VH n.t. 12A4
56
VH CDR1 a.a. 1B12 83 VH n.t. 10A5
57
VH CDR1 a.a. 7H1 84 VH n.t. 5F8
58
VH CDR1 a.a. 11E6 85 VH n.t. 10H10
59
VH CDR1 a.a. 12B7 86 VH n.t. 1B12
60
VH CDR1 a.a. 13G4 87 VH n.t. 7H1
88
VH n.t. 11E6
61
VK CDR2 a.a. 3G10 89 VH n.t. 12B7
62
VK CDR2 a.a. 12A4 90 VH n.t. 13G4
63
VK CDR2 a.a. 10A5
64
VK CDR2 a.a. 5F8 91 VK n.t. 3G10
65
VK CDR2 a.a. 10H10 92 VK n.t. 12A4
66
VK CDR2 a.a. 1B12 93 VK n.t. 10A5
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VK CDR2 a.a. 7H1 94 VK n.t. 5F8
68
VK CDR2 a.a. 11E6 95 VK n.t. 10H10
69
VK CDR2 a.a. 12B7 96 VK n.t. 1B12
70
VK CDR2 a.a. 13G4 97 VK n.t. 7H1
98
VK n.t. 11E6
71
VK CDR3 a.a. 3G10 99 VK n.t. 12B7
72
VK CDR3 a.a. 12A4 100 VK n.t. 13G4
73
VK CDR3 a.a. 10A5
74
VK CDR3 a.a. 5F8 101 VH 1-18 línea germinal a.a.
75
VK CDR3 a.a. 10H10 102 VH 1-69 línea germinal a.a.
76
VK CDR3 a.a. 1B12 103 VH 1-3 línea germinal a.a.
77
VK CDR3 a.a. 7H1 104 VH 3-9línea germinal a.a.
78
VK CDR3 a.a. 11E6
79
VK CDR3 a.a. 12B7
80
VK CDR3 a.a. 13G4
105
VK L6 línea germinal a.a.
106
VK L15 línea germinal a.a.
107
VK A27 línea germinal a.a.
108
VK L18 línea germinal a.a.
109
VK a.a. 11E6a
44

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