ES2284161T3 - Generacion de anticuerpos xenogenicos. - Google Patents
Generacion de anticuerpos xenogenicos. Download PDFInfo
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- ES2284161T3 ES2284161T3 ES95115451T ES95115451T ES2284161T3 ES 2284161 T3 ES2284161 T3 ES 2284161T3 ES 95115451 T ES95115451 T ES 95115451T ES 95115451 T ES95115451 T ES 95115451T ES 2284161 T3 ES2284161 T3 ES 2284161T3
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Abstract
LA PRESENTE INVENCION PROPORCIONA HUESPEDES MAMIFEROS NO HUMANOS CARACTERIZADOS POR LUGARES LG ENDOGENOS INACTIVADOS Y LUGARES LG HUMANOS FUNCIONALES PARA RESPONDER A UN INMUNOGENO PRODUCIENDO ANTICUERPOS HUMANOS O ANALOGOS DE LOS MISMOS. LOS HUESPEDES SE PRODUCEN MEDIANTE TRANSFORMACIONES REPETIDAS DE CELULAS TALLO EMBRIONICAS MEDIANTE RECOMBINACION HOMOLOGA, PREFERENTEMENTE EN COMBINACION CON SU REPRODUCCION. SE EMPLEAN DIFERENTES ESTRATEGIAS PARA LA RECOMBINACION DE LOS LUGARES HUMANOS ALEATORIAMENTE O EN LUGARES ANALOGOS DEL HUESPED.
Description
Generación de anticuerpos xenogénicos.
El campo de este invento es la producción de
proteínas de unión específicas xenogénicas en un hospedante
mamífero viable.
Los anticuerpos monoclonales encuentran uso
tanto en diagnóstico como en terapia. Debido a su habilidad para
unirse a un epítopo específico, pueden ser usados de modo único
para identificar moléculas que llevan ese epítopo o pueden ser
dirigidos, por sí mismos o junto a otro resto, a un sitio
específico para diagnosis o terapia.
Los anticuerpos monoclonales comprenden las
cadenas pesadas y ligeras que juntas definen una región de unión
para el epítopo. Cada una de estas cadenas está comprendida por una
región variable y una región constante. La secuencia aminoacídica de
la región constante es específica para un isotipo particular del
anticuerpo, así como el hospedante que produce el anticuerpo.
Debido a la relación entre la secuencia de la
región constante y la especie a partir de la que el anticuerpo es
producido, la introducción de un anticuerpo xenogénico en el
sistema vascular del hospedante puede producir una respuesta inmune.
En los casos en que el anticuerpo xenogénico puede ser introducido
de modo repetitivo, como en el caso de las enfermedades crónicas,
se hace impráctico administrar el anticuerpo puesto que seria
rápidamente destruido y puede tiene un efecto adverso. Ha habido,
por tanto, muchos esfuerzos para proporcionar una fuente de
anticuerpos singénicos o alogénicos. Una técnica ha implicado el
uso de la tecnología de ADN recombinante en el que los genes para
las cadenas pesadas y ligera a partir del hospedante fueron
identificadas y las regiones que codifican la región constante
aisladas. Estas regiones fueron después unidas a la región variable
que codifica la porción de otros genes de inmunoglobulinas a partir
de otras especies dirigidas a un epítopo específico.
Aunque el anticuerpo quimérico parcialmente
xenogénico resultante es sustancialmente más útil que usar un
anticuerpo completamente xenogénico, éste tiene aún un número de
desventajas. La identificación, aislamiento y unión de las regiones
variable y constante requiere un trabajo sustancial. Además, la
unión de una región constante de una especie a una región variable
a partir de otra especie puede cambiar la especificidad y afinidad
de las regiones variables, a modo de perder las propiedades deseadas
de la región variable. También, hay estructuras y secuencias
hipervariables específicas para una especie en la región variable.
Estas estructuras y secuencias hipervariables pueden dar como
resultado respuestas antigénicas indeseables.
Sería por tanto más deseable producir
anticuerpos alogénicos para la administración a una hospedante
inmunizando el hospedante con un inmunógeno de interés. Para los
primates, particularmente humanos, esta aproximación no es práctica.
Los anticuerpos humanos que han sido producidos se han basado en la
presencia adventicia de una bazo disponible, a partir de un
hospedante que ha sido previamente inmunizado por el epítopo de
interés. Mientras que los linfocitos de sangre periférica humana
pueden ser empleados para la producción de anticuerpos
monoclonales, éstos no han sido particularmente exitosos en fusiones
y han conducido normalmente sólo a IgM. Por otro lado, es
particularmente difícil generar una respuesta de anticuerpos humanos
frente a una proteína humana, una diana diseñada en muchas
aplicaciones terapéuticas y de diagnóstico. Hay, por lo tanto, un
interés sustancial en encontrar rutas alternativas a la producción
de anticuerpos alogénicos para humanos.
Thomas y Capecchi, Cell,
51, 503-512, 1987. Koller y
Smithies, Proc. Natl. Acad. Sci. USA, 86,
8932-8935, 1989, describen la inactivación
del locus de B2 micro-blobulina mediante
recombinación homóloga en células madre embrionarias. Berman
y otros, EMBO J. 7, 727-738, 1986,
describe el locus VH de Ig humanos. Burke y otros,
Science, 236, 806-912, 1987, describe
vectores de cromosomas artificiales de levadura. Véase también,
Garza y otros, Science, 246, 641-646,
1989, y Brownstein y otros, Science, 244,
1348-1351, 1989. Sakano, y otros,
describen un segmento de diversidad de los genes de la cadena
pesada de inmunoglobulina. Sakano y otros, Nature;
290, 562-565, 1981. Tucker y otros,
Proc. Natl. Acad. Sci. USA, 78, 7684-7688,
1981, describen la secuencia génica de la cadena pesada de
IgA de ratón. Blankenstein y Kruwinkel Eur. J.
Immunol., 17, 1351-1357, 1987, describen
la región de la cadena pesada variable de ratón. Véase también,
Joyner y otros, Nature, 338, 153-155,
1989, Traver y otros, Proc. Natl. Acad. Sci.
USA 86, 5898-5902, 1989, y Panchas
y otros, Proc. Natl. Acad. Sci. USA, 87,
5109-5113, 1990.
El presente invento se refiere a un vector
dirigido de recombinación homóloga que comprende una secuencia
nucleotidica que tiene homología con las secuencias intrónicas 3' y
5' de, y está próxima a. los genes del segmento de la región de
unión (J) de una cadena pesada o una cadena ligera kappa en un
locus de inmunoglobulina endógena de un ratón y teniendo un gen
marcador entremedias, siendo dicho vector capaz de recombinación
homóloga con dicho locus de inmunoglobulina de ratón endógeno y
remplazando todos los genes de la región de unión (J) con dicho gen
marcador para prevenir el reordenamiento funcional de dicho locus y
la producción de una mensajero el reordenamiento funcional de dicho
locus y la producción de una mensajero funcional que codifica una
inmunoglobulina.
Además, el presente invento se refiere a un
método para inactivar un locus de inmunoglobulina de cadena pesada
o ligera kappa en un mamífero no humano que comprende la etapa de
delecionar suficientes secuencias del locus de Ig para impedir el
reordenamiento del locus Ig o para impedir la producción de un
mensajero funcional que codifica el locus Ig.
El presente invento también se refiere a los
ratones caracterizados en las reivindicaciones.
Las proteínas de unión específicas xenogénicas
son producidas en un hospedante mamífero viable no primate mediante
inmunización del hospedante mamífero con un inmunógeno
apropiado.
El hospedante se caracteriza por: (1) ser
incapaz de producir inmunoglobulina endógena; (2) un locus de
inmunoglobulina exógeno, que comprende al menos una región constante
de inmunoglobulina, o proteína de la misma, secuencias de
inmunoglobulina que proporcionan los componentes de la región
variable de al menos una de las cadenas ligera y pesada, y al menos
un intrón con sitios de corte y empalme para excisión y ensamblaje
de una subunidad de inmunoglobulina funcional. Así, el hospedantes
mamífero comprenderá al menos una región constante xenogénica o una
proteína de la misma capaz de ser cortada y empalmada a una región
J funcional de un locus de inmunoglobulina endógeno o exógeno, puede
tener un locus de inmunoglobulina entero del hospedante sustituido
por una porción o un locus de inmunoglobulina xenogénico entero, o
puede tener un locus de inmunoglobulina xenogénica insertado en un
cromosoma de la célula hopedante y una región de inmunoglobulina
endógena inactivada. Estas diversas alternativas se lograrán, al
menos en parte, empleando recombinación homóloga en los loci de
inmunoglobulina para las cadenas pesadas y ligeras.
Nuevos hospedantes mamíferos transgénicos,
distintos de primates, particularmente distintos de humanos, son
proporcionados, en los que el hospedante es capaz de montar una
respuesta inmune a un inmunógeno, en el que la respuesta produce
anticuerpos que tienen las regiones constantes y/o variables de
primate, particularmente humanas, o tales otras secuencias
peptídicas efectoras de interés. Los hospedantes se caracterizan por
ser capaces de producir anticuerpos xenogénicos o modificados como
resultado de la sustitución y/o inactivación de los loci que
codifican la subunidad de inmunoglobulina endógena. Las
modificaciones conservan al menos una porción de las regiones
constantes que proporciona el ensamblaje del sitio de unión de la
región variable unida al extremo C-terminal con un
péptido funcional. El péptido funcional puede tomar muchas formas o
conformaciones y puede servir como una enzima, factor de
crecimiento, proteína de unión, ligando, citosina, proteína
efectoras, proteínas quelantes, etc. Los anticuerpos pueden ser de
cualquier isotipo, por ejemplo, IgA, D, E, G o M o subtipos dentro
del isotipo.
Un número de estrategias puede ser empleado para
lograr los hospedantes transgénicos deseados. Diversos hospedantes
transgénicos pueden ser empleados, particularmente murinos,
lagomorfos, ovinos, porcinos, equinos, caninos, felinos o similares,
normalmente distintos de primates. Para la mayor parte, los ratones
han sido usados para la producción de linfocitos B para la
inmortalización para la producción de anticuerpos. Puesto que los
ratones son fáciles de manejar, pueden ser producidos en grandes
cantidades, y se conoce que tienen un extenso repertorio inmune, los
ratones serán normalmente los animales de elección. Por lo tanto,
la discusión siguiente se referirá a ratones, pero debería
entenderse que otros animales, particularmente mamíferos, pueden
ser fácilmente sustituidos por los ratones, siguiendo los mismos
procedimientos.
En una estrategia, como etapas individuales, los
complejos génicos de inmunoglobulina de la cadena pesada y ligera
humanas son introducidos en la línea germinal de ratón y en una
etapa separada los genes de ratón correspondientes se vuelven no
funcionales. Los genes de la cadena pesada y ligera humana son
reconstruidos en un microorganismo eucariótico y procariótico y los
fragmentos de ADN resultantes pueden ser introducidos en pronúcleos
de oocitos de ratón fertilizados o células madre embrionarias. La
inactivación de los loci de inmunoglobulina de ratón endógenos son
logrados mediante interrupción dirigida de los loci apropiados
mediante recombinación homóloga en células madre embrionarias de
ratón. En cada caso los animales quimeras son generados de modo que
se derivan en parte a través de las células madre embrionarias
modificadas y son capaces de transmitir las modificaciones genéticas
a través de la línea germinal. El cruce de las cepas de ratón con
loci de inmunoglobulina humana con cepas con los loci de ratón
inactivas darán animales cuya producción de anticuerpos es puramente
humana.
En la siguiente estrategia, los fragmentos de
los loci de inmunoglobulina de la cadena pesada y ligera humanas
son usados para remplazar directamente los loci de ratón
correspondiente mediante recombinación homóloga en células madre
embrionarias de ratón. Esto es seguido por la generación de animales
transgénicos quiméricos en los que las células derivadas de las
células madre embrionarias contribuyen a la línea germinal.
Estas estrategias se basan en la organización
conocida de los loci de cadena de inmunoglobulinas en un número de
animales, ya que la organización, localización relativa de exones
que codifican dominios individuales, y localización de los sitios de
corte y empalme y de los elementos transcripcionales, se entiende
que varían en diversos grados. En humanos, el locus de la cadena
pesada de inmunoglobulina está situada en el cromosoma 14. En la
dirección 5'-3' de la transcripción, el locus
comprende un grupo grande de genes de la región variable (V_{H}),
genes de la región de diversidad (D), seguidos por los genes de la
región de unión (J_{H}) y el grupo del gen constante (CH). El
tamaño del locus se estima que es alrededor de 2500 kilobases (kb).
Durante el desarrollo de células B, segmentos génicos discontinuos
a partir del locus IgH de la línea germinal son yuxtapuestos
mediante un reordenamiento físico del ADN. Para que se produzca un
polipéptido de Ig de la cadena pesada funcional, tres segmentos de
ADN discontinuos, a partir de las regiones V_{H}, D y J_{H} se
deben unir en una forma secuencial específica; V_{H} a DJ_{H},
generando la unidad funcional V_{H}DJ_{H}. Una vez que
V_{H}DJ_{H} ha sido formada, las cadenas pesadas específicas
son producidas siguiendo la transcripción del locus Ig, utilizando
como molde la unidad V_{H}DJ_{H}C_{H} específica que comprende
exones e intrones. Hay dos loci para las cadenas ligeras de Ig, el
locus \kappa en el cromosoma 2 humano y el locus \lambda en el
cromosoma 22 humano. La estructura de los loci IgL es similar a la
del locus IgH, excepto que la región D no está presente. Siguiendo
el reordenamiento IgH, el reordenamiento de locus de la cadena
ligera se logra de modo similar por la unión de V_{L} y J_{L}
de la cadena \kappa o \lambda. Los tamaños de los loci \kappa
o \lambda son cada uno aproximadamente 1000 kb. La expresión del
IgH reordenado y la cadena ligera Ig\kappa o Ig\lambda en una
célula B particular permite la generación de moléculas de
anticuerpos.
Para aislar, donar y transferir el locus
IgH_{hu}, un cromosoma de levadura artificial puede ser empleado.
El locus IgH_{hu}, entero puede estar contenido dentro de uno o
unos pocos clones de cromosomas de levadura artificiales (YAC). Lo
mismo es verdad para los loci de cadenas ligeras de Ig. La
introducción subsiguiente de los clones YAC de cadena pesada o
cadena ligera en la levadura recipiente permite la reconstitución de
los loci de Ig de la línea germinal intactos mediante recombinación
homóloga entre las regiones de homología solapantes. De esta
manera, el aislamiento de los fragmentos de ADN que codifican para
la cadena Ig humana es obtenido.
Para obtener un amplio espectro de anticuerpos
de alta afinidad, no es necesario que uno incluya la región V
entera. Diversas familias génicas de la región V están intercaladas
dentro del agrupamiento de la región V. Así, obteniendo un subgrupo
de los genes de la región V conocida de los loci de Ig de la cadena
pesada y ligera humanas (Berman y otros, EMBO J. (1988) 7:
727-738) más que el complemento entero de las
regiones V, el hospedante transgénico puede ser inmunizado y ser
capaz de montar una respuesta inmune fuerte y proporcionar
anticuerpos de alta afinidad. De esta manera fragmentos de ADN
relativamente pequeños del cromosoma pueden ser empleados, por
ejemplo, un fragmento de 670 kb documentado del locus Ig_{Hu}, es
mostrado en la Figura 1b. Este fragmento de restricción
NotI-NotI serviría para proporcionar una variedad de
regiones V, lo que proporciona la una diversidad aumentada mediante
la recombinación con las diversas regiones D y J y sufren mutación
somática.
Para proporcionar la producción de anticuerpos
humanos en un hospedante xenogénico, es necesario que el hospedante
competente proporcione las enzimas necesarias y otros factores
implicados en la producción de anticuerpos, cuando falten los genes
endógenos competentes para la expresión de las subunidades pesada y
ligera de inmunoglobulinas. Así, esas enzimas y otros factores
asociados con el reordenamiento de la línea germinal, corte y
empalme, mutación somática, y similares, serán funcionales en el
hospedante xenogénico. Lo que faltará es una región natural
fun-
cional que comprende los diversos exones asociados con la producción de subunidades de inmunoglobulina endógena.
cional que comprende los diversos exones asociados con la producción de subunidades de inmunoglobulina endógena.
El ADN humano puede ser introducido en los
pronúcleos de los oocitos fertilizados o células madre embrionarias.
La integración puede ser aleatoria u homóloga dependiendo de la
estrategia particular a ser empleada. Así, usando la transformación,
usando etapas repetitivas o en combinación con cruces, se pueden
obtener animales transgénicos capaces de producir anticuerpos
humanos en ausencia sustancial de subunidades de inmunoglobulina
ligera o pesada del hospedante.
Para inactivar los loci de inmunoglobulina
hospedantes, la recombinación homóloga puede ser empleada, en la
que el ADN es introducido en los loci de la cadena pesada y la
cadena ligera de inmunoglobulina que inhiben la producción de las
subunidades de inmunoglobulina endógena. Puesto que hay dos alelos
de cadena pesada y dos loci de cadena ligera, cada uno con dos
alelos, aunque se puede elegir ignorar el loci \lambda, tendrá
que haber múltiples transformaciones que resultan en la inactivación
de cada uno de los alelos. La transformación pretende referirse a
una técnica para introducir ADN en una célula viable, tal como
conjugación, transformación, transfección, transducción,
electroporación, lipofección, biolística, o similares). La
recombinación homóloga puede ser empleada para inactivar
funcionalmente los loci, introducir el ADN homólogo en células
madre embrionarias, seguido por la introducción de las células
modificadas en blastocistos receptores. Los cruces subsiguientes
permiten la transmisión por la línea germinal del locus inactivado.
Se puede entonces elegir cruzar la progenie heterozigótica y
seleccionar la progenie homozigota a partir de los padres
homozigotos o de nuevo, se puede usar: la célula madre embrionaria
para la recombinación homóloga y la inactivación del locus
comparable.
El número de etapas de transformación puede ser
reducido proporcionando al menos un fragmento del locus de la
subunidad de inmunoglobulina para la recombinación homóloga con la
inmunoglobulina endógena análoga, de modo que el locus humano es
sustituido por al menos una parte del locus de inmunoglobulina
hospedante, con una inactivación resultante del locus de la
subunidad de inmunoglobulina hospedante. De particular interés es
el uso de la transformación por una inactivación única, seguida por
el cruce de la progenie heterozigota para producir una progenie
homozigota. En los casos en que el locus humano es empleado para
sustitución o inserción en el locus hospedante para la inactivación,
el número de transformaciones puede ser limitado a tres
transformaciones y como ya se ha indicado, uno puede elegir ignorar
el locus \lambda menos usado y limitar la transformación a dos
transformaciones. Alternativamente, uno puede elegir proporcionar
la inactivación como una etapa separada para cada locus, empleando
células madre embrionarias de progenies que han tenido previamente
uno o más loci inactivados. En el evento en que sólo se usa la
transformación y el locus humano es integrado en el genoma
hospedante en una manera aleatoria, un total de ocho
transformaciones pueden ser requeridas.
Para la inactivación, cualquier lesión en el
locus diana resultante en la prevención de la expresión de una
subunidad de inmunoglobulina de ese locus puede ser empleada. Así,
la lesión, puede estar en una región que comprende el potenciador,
por ejemplo, 5' aguas arriba o intrón, en las regiones V, J o C, y
con la cadena pesada, existe la oportunidad en la región D, o
combinaciones de las mismas. Así, el factor importante es que el
reordenamiento génico de la línea germinal de Ig es inhibido, o un
mensajero funcional que codifica la subunidad de inmunoglobulina no
puede ser producido, bien debido a un fallo de la transcripción, o
un fallo en el procesamiento del mensajero o algo similar.
Preferiblemente, cuando sólo se está interesado
en la inactivación del locus de la subunidad de inmunoglobulina, la
lesión será introducida en la región J del locus de la subunidad de
inmunoglobulina. Así, se produce una construcción a la que le falta
una región J funcional y puede comprender las secuencias de la
región J adyacente a y aguas arriba y/o aguas abajo de la región J
o comprende todas o parte de la región con una inserción
inactivante en la región J. La inserción puede ser de 50 pb o más,
en la que tal inserción tienen como resultado una interrupción de
la formación de un mARN funcional. De modo deseable, la región J al
completo o una parte sustancial, normalmente al menos de alrededor
del 75% del locus, preferiblemente al menos alrededor del 90% del
locus, es delecionada. Si se desea, la lesión entre las dos
secuencias flanqueantes que definen la región homóloga pueden
extenderse mas allá de la región J, en la región disponible y/o en
la región constante.
De modo deseable, un gen marcador es usado para
remplazar la región J. Diversos marcadores pueden ser empleados,
particularmente aquellos que permiten la selección positiva. De
interés particular es el uso de la resistencia a G418, que resulta
de la expresión del gen para la neomicina fosfotransferasa.
Aguas arriba y/o aguas abajo de la construcción
del gen diana puede estar un gen que permite la identificación de
si un entrecruzamiento doble ha tenido lugar o no. Para este
propósito, el gen de la timidina quinasa del virus del Herpes
simplex puede ser empleado, puesto que las células expresan el gen
de la timidina quinasa pueden ser eliminadas mediante el uso de
análogos nucleósidos tales como aciclovir o ganciclovir, mediante
sus efectos citotóxicos en las células que contiene un gen
HSV-tk funcional. La ausencia de sensibilidad a
estos análogos nucleósidos indica la ausencia del gen de timidina
quinasa-HSV y, por lo tanto, en los casos en que la
recombinación ha tenido lugar, que un entrecruzamiento doble
también ha tenido lugar.
Mientras que la presencia del gen marcado en el
genoma indicará que la integración ha tenido lugar, aún será
necesario determinar si la integración ha tenido lugar. Esto puede
lograrse en un número de vías. Para la mayor parte, se empleará el
análisis de ADN para establecer la localización de la integración.
Empleando sondas para el inserto y después secuenciando las
regiones 5' y 3' flanqueantes del inserto en busca de la presencia
del locus diana, que se extiende más allá de las regiones
flanqueantes de la construcción, o identificando la presencia de
una deleción, cuando tal deleción ha sido introducida, la
integración deseada puede ser establecida.
La reacción en cadena de la polimerasa (PCR)
puede ser usada con ventaja en la detección de la presencia de
recombinación homóloga. Se pueden usar sondas que son
complementarias a una secuencia dentro de la construcción y
complementarias a una secuencia fuera de la construcción y en el
locus diana. De este modos, sólo se pueden obtener cadenas de ADN
que tienen ambos cebadores presentes en las cadenas complementarias
si la recombinación homóloga ha tenido lugar. Demostrando la
presencia de las sondas para el tamaño de secuencia esperado, se
apoya la presencia de la recombinación homóloga.
La construcción puede incluir además un sistema
de replicación que es funcional en la células hospedante de
mamífero. Para la mayor parte, estos sistemas de replicación
implicarán sistemas de replicación viral, tales como el virus 40 de
simio, el virus de Epstein-Barr, el virus del
polioma, el papiloma virus, y similares. Diversos sistemas de
iniciación transcripcional pueden ser empleados, bien a partir de
virus o bien a partir de genes de mamíferos, tales como SV40, genes
de metalotioneína I y II, gen de \beta-actina,
genes tempranos y tardíos de adenovirus, gen de fosfoglicerato
quinasa, gen de la ARN polimerasa II, o similares. Además de
promotores, ser pueden emplear potenciadores silvestres para
potenciar adicionalmente la expresión del gen marcador.
A la hora de construir las construcciones sujeto
para la recombinación homóloga, un sistema de replicación para
procariotas, particularmente E. coli, puede ser incluido,
para la preparación de la construcción, para la clonación tras cada
manipulación, para el análisis, tales como mapas de restricción o
secuenciación, para la expansión y aislamiento de la secuencia
deseada. En los casos en que la construcción es grande, generalmente
que excede alrededor de 50 kpb, normalmente que excede los 100 kpb,
y normalmente no más de alrededor de 1000 kpb, un cromosoma
artificial de levadura (YAC) puede ser usado para el clonaje de la
construcción.
Una vez que la construcción ha sido preparada y
cualquier secuencia no deseable ha sido eliminada, por ejemplo,
secuencias procariotas, la construcción puede ser introducida en la
célula diana. Cualquier técnica conveniente para introducir el ADN
en las células diana puede ser empleada. Las técnicas incluyen la
fusión de esferoplastos, lipofección, electroporación,
transferencia de ADN mediada por fosfato cálcico o microinyección
directa. Tras la transformación o transfección de las células diana,
las células diana pueden ser seleccionadas por medio de marcadores
positivos y/o negativos, como se indica previamente, resistencia a
neomicina y aciclovir o ganciclovir. Esas células que muestran el
fenotipo deseado pueden ser entonces analizadas adicionalmente
mediante análisis de restricción, electroforesis, análisis Southern,
PCR, o similares. Identificando fragmentos que muestran la
presencia de la(s) lesión(es) en el locus diana, se
pueden identificar células en las que la recombinación homóloga ha
tenido lugar para inactivar una copia del locus diana.
El proceso arriba descrito pueden ser realizado
primero con un locus de cadena pesada en una célula madre
embrionaria y después maduración de las células para proporcionar un
hospedante fértil maduro. Entonces, mediante el cruce de los
hospedantes heterocigotos, un hospedantes homocigoto puede ser
obtenido o células madre embrionarias pueden ser aisladas y
transformadas para inactivar el segundo locus IgH, y el proceso ser
repetido hasta que todos los loci deseados hayan sido inactivados.
Alternativamente, el locus de la cadena ligera puede ser el primero.
En cualquier etapas, los loci humanos pueden ser introducidos.
Como ya se ha indicado, el locus diana puede ser
sustituido con el locus humano análogo. De esta manera, el locus
humano se colocará sustancialmente en la misma región que el locus
hospedante análogo, de modo que cualquier regulación asociada con la
posición del locus será sustancialmente la misma para el locus de
inmunoglobulina humana. Por ejemplo, aislando el locus génico
V_{H} entero (incluyendo las secuencias V, D, y J), o una porción
del mismo, y flanqueando el locus humano con las secuencias a
partir del locus de ratón, preferiblemente las secuencias separadas
por al menos alrededor de 5 kpb, en el locus hospendante,
preferiblemente a alrededor de 10 kpb en el locus hospedante, se
puede insertar el fragmento humano en esta región en un
evento(s) de recombinación, sustituyendo el locus de
inmunoglobulina humana por la región variable del locus de
inmunoglobulina hospedante. De esta manera, se puede interrumpir la
capacidad del hospedante para producir una subunidad de
inmunoglobulina endógena, mientras que se permite al promotor del
locus de la inmunoglobulina humana ser activado por el potenciador
hospedante y ser regulado por el sistema regulador del
hospedante.
Una vez que los loci humanos han sido
introducidos en el genoma hospedante, bien mediante recombinación
homóloga o bien mediante integración aleatoria, y los animales
hospedantes han sido producidos con los loci de inmunoglobulina
endógenos inactivados mediante el cruce apropiado de los diversos
animales transgénicos o mutados, uno puede producir un hospedante al
que le falta la capacidad nativa para producir subunidades de
inmunoglobulinas endógenas, pero que tenga la capacidad para
producir inmunoglobulinas humanas con al menos una porción
significativa del repertorio humano.
La inactivación funcional de las dos copias de
cada uno de los tres loci de Ig hospedantes, en los que el
hospedante contiene el IgH humano y los loci de Ig \kappa y/o
\lambda permitirá la producción de moléculas de anticuerpos
puramente humanos sin la producción de anticuerpos hospedantes o
quimeras hospedantes/humanos. Tal cepa hospedante, mediante la
inmunización con antígenos específicos, respondería mediante la
producción de células B de ratón productoras de anticuerpos
específicos humanos, células B que podrían ser fusionadas con
células de mieloma de ratón o ser inmortalizadas de cualquier otra
manera para la producción estable continua de anticuerpos
monoclonales humanos.
La metodología y estrategias sujeto no necesitan
limitarse a la producción de inmunoglobulinas completas, pero
proporcionan la oportunidad de proporcionar regiones unidas a una
porción de la región constante, por ejemplo, C_{H1}, C_{H2},
C_{H3}, o C_{H4}, o combinaciones de las mismas.
Alternativamente, uno o más de los exones de las regiones C_{H} y
C_{\kappa} o C_{\lambda}), pueden ser remplazadas o unidas a una
secuencia que codifican una proteína diferente, tal como una enzima,
por ejemplo, el activador de plasminógeno, la superóxido dismutasa,
etc.; la cadena A de la toxina, por ejemplo, ricino, abrino, toxina
diftérica, etc.; factores de crecimiento, agentes citotóxicos, por
ejemplo, TNF, o similares. Véase, por ejemplo, los documentos de
Patentes WO 89/07142; WO 89/09344; y WO 88/03559. Insertando la
proteína de interés en un exón de la región constante y
proporcionando el corte y empalme de la región variable al exón de
la región constante modificada, la proteína de unión resultante
puede tener una región C-terminal diferente de la
inmunoglobulina. Proporcionando una secuencia stop con el gen
insertado, el producto de la proteína tendrá la proteína insertada
como la región C-terminal. Si se desea, la región
constante puede ser enteramente sustituida mediante la otra
proteína, proporcionando una construcción con los sitios de corte y
empalme apropiados para unir la región variable a la otra
proteína.
Las células B productoras de anticuerpos o de
análogos de anticuerpos a partir del hospedante transgénico pueden
ser usadas para su fusión a una célula mieloide de ratón para
producir hibridomas o inmortalizarlas mediante otros procesos
convencionales, por ejemplo, la transfección con oncogenes. Estas
células inmortalizadas pueden entonces ser hechas crecer en un
cultivo continuo o introducidas en el peritoneo de un hospedante
compatible para la producción de ascitos.
El invento sujeto proporciona la producción de
antisueros policlonales humanos o anticuerpos monoclonales humanos
o análogos de anticuerpos. En los casos en que el hospedante
mamífero ha sido inmunizado con un inmunógeno, los anticuerpos
humanos resultantes pueden ser aislados a partir de otras proteínas
usando una columna de afinidad, que tiene un resto de unión a Fc,
tal como proteína A, o similar.
Para producir animales a partir de células madre
embrionarias, tras la transformación, las células pueden ser puestas
en placas sobre una capa alimentadora en un medio apropiado, por
ejemplo, DMEM potenciado con suero bovino fetal. Las células que
contienen la construcción pueden ser detectadas empleando un medio
selectivo y tras un tiempo suficiente para que las colonias
crezcan, las colonias pueden ser recogidas y analizadas en lo que
respecta a la aparición de integración o recombinación homóloga.
Como se describió previamente, se puede usar PCR, con cebadores
dentro o fuera de la secuencia de la construcción, pero en el locus
diana.
Estas colonias que muestran recombinación
homóloga pueden entonces ser usadas para la manipulación embrionaria
y la inyección en blastocistos. Los blastocistos pueden ser
obtenidos a partir de hembras mediante lavado del útero 3- días tras
la ovulación. Las células madre embrionarias pueden entonces ser
tripsinizadas y las células modificadas añadidas a una gota que
contiene el blastocisto. Al menos una y hasta treinta células madre
embrionarias pueden ser inyectadas en el blastocele del blastocisto.
Tras la inyección, al menos uno y no mas de alrededor de quince de
los blastocistos son devueltos a cada una de las trompas uterinas
de hembras pseudos-preñadas. Se deja entonces que
las hembras lleguen a término y la progenie resultante es cribada en
busca de células mutantes que tengan la construcción.
Los mamíferos pueden ser cualquier no humano,
particularmente mamíferos no primates, tales como animales de
laboratorio, particularmente animales de laboratorio pequeños,
tales como ratones, ratas, cobayas, etc., animales domésticos,
mascotas, etc.
Los siguientes ejemplos son ofrecidos a modo de
ilustración y no a modo de limitación.
Un fragmento EcoRI de 6,4 Kb, que contiene los
genes J de la cadena pesada de ratón y las secuencias flanquantes,
está clonado a partir de la librería genómica embrionaria de ratones
Balb/c usando las sondas descritas en Sakano y otros, Nature 290:
562-565, 1981. Este fragmento (mDJ) es insertado en
el plásmido pUC19 digerido con EcoRI (pmDJ). Un fragmento de 2,9 Kb,
que contiene los 4 genes J, es delecionado mediante digestión con
XhoI-Scal (pmD\deltaJNeo, véase la gráfica 1). Un
fragmento XhoI-BamHI de 1150 pb, que contiene un gen
de resistencia a neomicina dirigido por el promotor del gen de la
timidina quinasa del virus del Herpes simplex
(HSV-tk) y un potenciador del polioma es aislado a
partir de pMCINeo (Thomas y Capecchi, Cell, 51,
503-512, 1987). Un adaptador sintético es añadido
sobre este fragmento para convertir el extremo Bam HI en un extremo
Scal y el fragmento resultante es unido al XhoI-ScaI
pmD\deltaJ para formar el vector de inactivacicón
(pmD\deltaJ.Neo) en el que la orientación 5' a 3' de la neomicina
y los promotores de la cadena pesada es idéntica. Este plásmido es
linearizado mediante digestión don NdeI antes de la transfección en
células ES. Las secuencias que dirigen el evento de la
recombinación homóloga son fragmentos de 3 kb y de 0,5 kb, situadas
5' y 3' del gen de neomicina, respectivamente.
\vskip1.000000\baselineskip
\vskip1.000000\baselineskip
Gráfica
1
Vector de inactivación de los
genes J de la cadena pesada de
ratón
\newpage
La línea celular ES E14TG2a (Hooper y otros,
Nature., 326: 292-295, 1987) es cultivada en capas
alimentadoras-fibroblastos embrionarios primarios
tratados con mitomicina esencialmente como está descrito (Doetschman
y otros, J. Embriol. Exp. Morphol. 87:27-45, 1985).
Los fibroblastos embrionarios son preparados a partir de embriones
de hembras C57BL/6 que han sido cruzadas 14 a 17 días antes con un
macho homocigoto para un transgén de neomicina (Gossler y otros,
PNAS 83: 9065-9069, 1986). Estas células son
capaces de crecer en medio que contiene G418. Las condiciones de
electroporación son descritas por Bogas, y otros., Ex. Hematol. (NY)
149:988-994, 1986. Las células ES son tripsinizadas,
resuspendidas en medio de cultivo a una concentración de 4 x
10^{7}/ml y electroporadas en presencia del ADN diana a una
concentración de 12 nm en el primer experimento y 5 nM de ADN en el
segundo. Un voltaje de 300 V con una capacitancia de
150-250 \muF es encontrado óptimo con una célula
de electroporación de 5 mm de longitud y 100 mm^{2} de sección
transversal. 5 x 10^{6} células electroporadas son puestas en
placas sobre fibroblastos tratados con mitomicina en placas de 100
mm en presencia de medio Eagle modificado de Dulbecco (DMEM)
suplementado con suero bovino fetal al 15% y 0,1 mM de
2-mercaptoetanol. El medio es remplazado 24 horas
tras electroporación con un medio que contiene 200 \mug/ml de
G418.
Las colonias ES resultantes
10-14 días tras electroporación son recogidas con
pipetas capilares alargadas para análisis usando PCR. La mitad de
cada colonia recogida es colocada en una placa de 24 pocillos ya
sembrada con células alimentadoras tratadas con mitomicina. Las
otras mitades, combinadas en grupos de 3-4, son
transferidas a tubos Eppendorf que contiene aproximadamente 0,5 ml
de PBS y analizadas en busca de recombinación homóloga mediante
PCR. Las condiciones para las reacciones de PCR están esencialmente
descritas (Kim y Smithies, Nucleic Acids Res. 16:
8887-8893, 1988). Tras precipitarlas, las células
ES son resuspendidas en 5 \mul de PBS y son lisadas mediante la
adición de 55 \mul de H_{2}O a cada tubo. Las DNasas son
inactivadas por calentamiento de cada tubo a 95°C durante 10 min.
Tras el tratamiento con proteinasa K a 55°C durante 30 min, 30
\mul de cada lisado son transferidos a un tubo que contiene 20
\mul de una mezcla de reacción que incluye tampón de PCR: 1,5
\mug de cada cebador, 3U de Taq polimerasa, 10% de DMSO, y dNTPs,
cada uno a 0,2 mM. La expansión de la PCR emplea 55 ciclos usando
un termociclador con 65 segundos de fusión a 92°C y una temperatura
de hibridación (annealing) y tiempo de extensión a 65°C. Los dos
oligonucleótidos cebadores son TGGCGGACCGCTATCCCCCAGGAC y
TAGCCTGGGTCCCTCCTTAC, que corresponden respectivamente a una región
de 650 bases 3' del codon de inicio del gen de neomicina y
secuencias situadas en el gen de la cadena pesada de ratón, 1100
bases 3' del sitio de inserción. 30 \mul de la mezcla de reacción
son sometidos a electroforesis en geles de agarosa y transferidos a
membranas de nilón (Zeta Bind). Los filtros son hibridados con un
fragmento marcado con ^{32}P del fragmento XbaI de 991 pb de la
región J-C.
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Un fragmento EcoRI de 6,1 Kb, que contiene los
genes de la región J de la cadena pesada de inmunoglobulina de ratón
y secuencias flanqueantes, clonado a partir de una librería
genómica embrionaria de ratón Balb/c e insertado en el pUC18 (pJH),
fue digerido con Xhol y Nael para eliminar alrededor de 2,3 kpb del
fragmento que contenía cuatro genes J (véase la Gráfica 2A El
fragmento Xhol-BamHI) de alrededor de 1,1 kpb, romo
en el sitio BamHI, que contiene un gen de resistencia a la neomicina
dirigido por el promotor de gen de la timidina quinasa
(HSV-tk) del virus de Herpes simplex y potenciador
del polioma fue aislado del pMCINeo (Thomas y Capecchi, Cell, 51,
503-512, 1987). Este fragmento fue insertado en el
pJH eliminado del Xhol-Nael para formar el vector
de inactivación (pmHJ, véase la Gráfica 2B), en la que la
orientación transcripcional de la neomicina y los genes de la cadena
pesada son la misma. Este plásmido fue linearizado mediante la
digestión Ndel antes de la transfección a las células ES. Las
secuencias que conducen el evento de recombinación homóloga son
fragmentos de alrededor de 2,8 kpb y alrededor de 1,1 kpb,
localizados en los genes 5' y 3', respectivamente.
La línea celular ES E14TG2a (Koller y Smithies,
1989, PNAS, USA, 86, 8932-8935) fue cultivada en
capas alimentadoras de fibroblastos embrionarios primarios tratados
con mitomicina C como está descrito (Koller y Smithies, 1989, PNAS,
USA, 86, 8932-8935). Las células ES fueron
tripsinizadas, resuspendidas en tampón HBS (pH 7,05; 137 mM de
NaCl, 5 mM de KC1, 2 mM de CaCl_{2}, 0,7 mM de Na_{2}HPO_{4},
21 mM de HEPES pH 7,1) en una concentración de 2,10^{7}/ml y
electroporadas en presencia de 50 \mug/ml del vector de
inactivación linearizado. La electroporación fue llevada a cabo con
el pulsador de gen BioRad usando 240 voltios y una capacidad de 500
\muF. Las células electroporadas 5 x 10^{6} fueron colocadas en
placas de 100 mm de fibroblastos tratados con mitomicina C en
presencia del medio Eagle modificado de Dulbecco (DMEM)
suplementado con 15% de suero de bovino fetal y
2-mercaptoetanol 0,1 mM. El medio fue reemplazado
24 h después de la electroporación con el medio que contiene 200
\mug/ml de G418. Las colonias de células ES resistentes al G418
resultantes 12-14 días después de la
electroporación fueron recogidas con pipetas capilares alargadas
para el análisis usando la reacción en cadena de la polimerasa
(PCR). La mitad de cada colonia recogida fue transferida a un
pocillo de una placa de microvaloración de 24 pocillos, ya sembrada
con células alimentadoras tratadas con mitomicina C. Las otras
mitades, combinadas en grupos de cuatro, fueron transferidas a
tubos Eppendorf que contienen 0,3 ml de PBS y los lisados celulares
fueron preparados para el análisis mediante PCR como se describe en
Joyner y otros (Nature, 338:153-155, 1989).
La reacción de PCR incluía 5-20 \mul de lisados
celulares, 1 \muM de cada cebador, 1,5 u de polimerasa Taq y 20
\mul de lisados celulares, 1 \muM de cada cebador, 1,5 u de
polimerasa Taq y 200 \muM de dNTPS. La amplificación por PCR
empleó 45 ciclos usando un termociclador
(Perkin-Elmer Cetus), con 1 min. De fusión a 94°C, 2
min. de hibridación a 55°C, y 3 min de extensión a 72°C. Los dos
oligonucleotidos desencadenantes son ACGGTATCGCCQCTCCCGAT y
AGTCACTGTAAAGACTTCGGGTA, que corresponden respectivamente a
alrededor de 120 bases del sitio BamHI 5' del gen de neomicina, y a
las secuencias situadas en el gen de la cadena pesada de ratón,
alrededor de 160 bases 3' del sitio de inserción. Una recombinación
homóloga exitosa da lugar a un fragmento de alrededor de 1,4 kpb.
20 \mul de la mezcla de la reacción son sometidos a
electroforesis en gel de agarosa al 1%, teñido con bromuro de etidio
y transferido a las membranas de nilón (Gene Screen). Los filtros
fueron hibridados con un fragmento EcoRI-Pstl
marcado con P^{32} de alrededor de 1,4 kpb situado en la cadena
pesada de ratón, 3' del sitio de inserción. Para análisis
adicionales, el ADN genómico fue preparado a partir de las células
ES, digerido con enzimas de restricción como se recomendó por los
fabricantes y los fragmentos fueron separados en geles de agarosa al
1%. El ADN fue transferido a las membranas de nilón (Gene Screen) e
hibridado con el fragmento marcado con P^{32} como se
describe
anteriormente.
anteriormente.
En el primer experimento, el análisis por PCR de
las colonias combinadas detectó una señal de PCR positiva del tamaño
esperado (alrededor de 1,4 kpb) de entre 34 muestras combinadas que
representan 136 colonias resistentes al G418. Las cuatro colonias
individuales que habían contribuido a las mezcla combinada positiva
fueron analizadas individualmente por PCR y un clon positivo,
ES33D5, fue identificado. Un análisis similar de 540 colonias
resistentes al G418 obtenidas en el segundo experimento dio 4
clones positivos adicionales (ES41-1,
ES61-1, ES65-1,
ES110-1).
Para verificar la interrupción dirigida de una
copia de los genes J (el gen es autosómico y por tanto está presente
en dos copias), los clones positivos por PCR fueron expandidos y el
ADN genómico fue preparado, digerido con HindIII o con Sacl y
analizado por análisis Southern como se describe usando la sonda
EcoRI-Pstl.
El reemplazamiento de los genes J por inserción
del gen de neomicina mediante un evento de recombinación homóloga
da como resultado un fragmento HindIII, detectable con la sonda
EcoRI-Pstl, que es alrededor de 1,9 kpb mayor que el
fragmento equivalente en el locus nativo, debido a la pérdida de
dos sitios HindIII situados en la región del gen J eliminado (véase
la Gráfica 2C). Los análisis Southern de cada uno de los 5 clones
positivos por digestión HindIII dieron un patrón que indicó que una
de las dos copias de los genes J de la cadena pesada había sido
interrumpida. Tres fragmentos marcados fueron detectados: un
fragmento (alrededor de 760 pb), idéntico en tamaño que el presente
en las células no tratadas a la misma intensidad, un fragmento
(alrededor de 2,3 kpb) idéntico en tamaño que el presente en las
células no tratadas, pero de intensidad disminuida en el clon
positivo por PCR, y un fragmento adicional de alrededor de 4,2 kpb,
el tamaño predicho para un evento de recombinación homóloga,
presente sólo en los clones positivos por PCR.
Similarmente, el reemplazo de los genes J por el
gen de neomicina por un evento de recombinación homóloga resulta en
una pérdida de uno de los sitios Sad y la aparición de un fragmento,
detectable con la sonda EcoRI-Pstl, que es alrededor
de 570 pb menor que el fragmento equivalente en el locus nativo
(véase la Gráfica 2C). Los análisis Southern de los clones por
digestión Sacl dieron el patrón esperado de un alelo nativo y un
alelo diana: un fragmento de alrededor de 4,0 kpb, idéntico en
tamaño que el detectado en las células sin tratar, pero de
intensidad disminuida en los 5 clones positivos, y un fragmento
adicional de alrededor de 3,4 kpb; el tamaño predicho para un
evento de recombinación homóloga diana, presente solamente en los
clones identificados. La rehibridacion de las membranas de Southern
con una sonda para el gen de neomicina muestra que sólo los
fragmento de 4,2 kpb y 3,4 kpb, resultantes de la digestión HindIII
y Sacl, respectivamente, hibridaron con la sonda como se predice por
el evento
diana.
diana.
Los ratones fueron adquiridos de Jackson.
Laboratorios (Bar Harbor, ME). Los blastocistos
C57BL/6 de tres días y medio de edad fueron obtenidos de hembras
superovuladas de 4-5 semanas de edad como se
describe por Koller y otros 1989 (supra). Las células
ES fueron tripsinizadas, lavadas una vez con un medio DMEM fresco y
diluidas en un medio M2 de alrededor de 1x10^{6} células/ml.
Alrededor de 5 \mul de células fueron añadidas a una gota de 150
\mul del medio M2, bajo aceite de parafina, que contenía los
blastocistos. De diez a quince células fueron inyectadas en el
blastocele de cada blastocisto. De seis a nueve blastocistos que
contenían células ES fueron devueltos a cada trompa uterina de las
hembras C57BL/6 x DBA F1 pseudo preñadas apareadas 2,5 días antes
con machos vasectomizados. Los retoños derivados de los
blastocistos inyectados nacieron generalmente 16-18
días mas tarde. La contribución de las células ES a los
descendientes fue juzgada visualmente mediante examen del color de
la piel de los retoños. Los blastocistos fueron obtenidos de los
ratones C57BL/6, que son de color negro oscuro. La línea celular ES
E14TG2a, línea parental de la cual fueron derivadas las líneas
celulares diana, fue aislada de los ratones 129/01a. Esta cepa de
ratón es de color crema, el efecto combinado de tres genes de color,
el alelo dominante Aw en el locus agouti, el alelo recesivo de ojos
rosado diluido en el locus p y el alelo C^{ch} recesivo en el
locus C. La progenie, en las que las células ES participaron en la
formación del animal, tenían pieles que contenían pelo marrón y
crema. La línea celular ES ES41-1 que transportaba
la cadena pesada de inmunoglobulina de ratón inactivado, fue
inyectada en los blastocistos del ratón C57BL/6 como se describe
anteriormente. Seis de los 18 retoños supervivientes tenían un alto
grado de quimerismo en el color de la piel (70-90%).
Los análisis de PCR del ADN aislado de los retoños recién nacidos
quiméricos de una hembra implantada con blastocitos inyectados con
las células ES inactivadas, indicaron que el locus de la cadena
pesada de inmunoglobulina mutado está presente en una variedad de
órganos tales como el. bazo, timo, riñón, hígado, cerebro y
piel.
piel.
Un fragmento HindIII-BamHI de
5,6 kb, que contiene los genes de la región J de la cadena kappa de
inmunoglobulina de ratón y secuencias flanqueantes, fue clonado a
partir de una librería genómica embrionaria de ratón Balb/c e
insertado en el vector pBluescriptSK para dar el plásmido (pKJ). El
pKJ fue digerido con HindIII y Pstl para eliminar un fragmento de
alrededor de 1,7 kpb que contenía 5 genes J (véase la Gráfica
3).
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Gráfica
3
Vector de inactivación de la
cadena
kappa
Un fragmento I de HindIII romo de 570 pb, que
abarca la región 5' del sitio HindIII adyacente a la región kappa J,
fue clonado a partir del ADN genómico de ratón mediante reacción en
cadena de la polimerasa (PCR). Este fragmento fue insertado en el
vector de clonación plc digerido de HindIII-Smal
(Marsh y otros, 1984, Gene, 32:481-485) y fue
cortado por digestión con Kpnl-Xhol. Un fragmento
Xhol-BamHI de alrededor de 1,1 kb, romo en el sitio
BamHI, que contenía el gen resistente a la neomicina dirigido por el
promotor de gen de la timidina quinasa de virus de Herpes simplex
(HSV-tk) y el potenciador del polioma fueron
aislados a partir del pMC 1Neo (Thomas y Capecchi, 1987,
supra). El fragmento de neomicina fue insertado en el pKJ
suprimido del HindIII-Pstl, que fue hecho romo en
el sitio Pstl, 5'de las secuencias kappa. El plásmido resultante
fue digerido con Kpnl y Xhol y el fragmento kappa
Kpnl-Xhol de 570 pb fue insertado en el vector
cortado por Kpnl-Xhol, 5' del gen de neomicina, para
generar el vector de inactivacion (pmK\deltaJ, véase la Gráfica
3). La orientación transcripcional de los genes de la cadena de
neomicina y kappa es la misma en pmK\deltaJ. El plásmido fue
linearizado por ApaLI antes de la transfección en las células ES.
La secuencia linearizada tiene alrededor de 3,8 kb y 570 pb de
homología con las secuencias celulares, situadas 3' y 5' del gen de
neomicina, respectivamente.
La electroporación del vector de inactivación
kappa en las células ES y el cribado en busca de los eventos de
recombinación homóloga fueron llevados a cabo como se describe para
la inactivación de la cadena pesada de inmunoglobulina. Las colonias
ES resistentes a G418 fueron analizadas en busca de recombinación
homóloga dirigida mediante PCR usando dos oligonucleótidos
activadores CGGTTGCTGTTGTATCCATAACTC y CATCAGAGCAGCC
GATTGTCTG, que corresponden respectivamente a las secuencias situadas en el gen de la cadena kappa de ratón, alrededor de 67 pb 5'del sitio de inserción, y alrededor de 370 pb 3' del sitio Xhol del gen de neomicina. Un oligonucleótido de 80 bases marcado con p^{32}, que comienza alrededor de 10 bp 5' del sitio de inserción, fue usado como una sonda para detectar el producto PCR diana. La recombinación homóloga exitosa da un aumento de fragmento de alrededor de 1030 pb. El análisis por PCR de 650 colonias resistentes a G418 detectó 3 colonias positivas (ES56-1, ES69-4, ES147-1). Los análisis Southern de estas colonias confirmaron la integración del vector de inactivación en un alelo de los loci de inmunoglobulina kappa conduciendo a la supresión de la-región J.
GATTGTCTG, que corresponden respectivamente a las secuencias situadas en el gen de la cadena kappa de ratón, alrededor de 67 pb 5'del sitio de inserción, y alrededor de 370 pb 3' del sitio Xhol del gen de neomicina. Un oligonucleótido de 80 bases marcado con p^{32}, que comienza alrededor de 10 bp 5' del sitio de inserción, fue usado como una sonda para detectar el producto PCR diana. La recombinación homóloga exitosa da un aumento de fragmento de alrededor de 1030 pb. El análisis por PCR de 650 colonias resistentes a G418 detectó 3 colonias positivas (ES56-1, ES69-4, ES147-1). Los análisis Southern de estas colonias confirmaron la integración del vector de inactivación en un alelo de los loci de inmunoglobulina kappa conduciendo a la supresión de la-región J.
Un fragmento Spel, que abarca la región
VH6-D-J-C\mu-C\delta
de la cadena pesada humana (Berman y otros, EMBO J. (1988)
7: 727-738; véase la gráfica 4) es aislado de una
librería humana y clonado en un vector de cromosoma artificial de
levadura (YAC) (Burke, y otros, Science,
236:806-812) usando las sondas de ADN descritas por
Berman y otros (EMBO J. (1988) 7: 727-738).
Un clon es obtenido, el cual se estima que es alrededor de 100 Kb.
El clon YAC aislado es caracterizado por electroforesis en gel de
campo pulsado (Burke, y otros, supra; Brownstein y
otros, Science, 244:1348-1351), usando sondas
radiomarcadas para la cadena pesada humana (Berman, y otros,
supra).
Un ADN de peso molecular elevado es preparado en
bolas de agarosa a partir de células de levadura que contienen el
YAC de interés (es decir, un YAC que contiene el fragmento Spel
mencionado del locus IgH). El ADN es fraccionado por tamaño en un
aparato de gel CHEF y la banda YAC es eliminada del gel de agarosa
de bajo punto de fusión. El fragmento de gel es equilibrado con
poliaminas y luego fundido y tratado con agarasa para digerir la
agarosa. El ADN revestido de poliamina es luego inyectado en el
pronúcleo macho de los embriones de ratón fertilizados que son
introducidos quirúrgicamente en el útero de una hembra pseudo
preñada como se describe anteriormente. La naturaleza transgénica
de los recién nacidos es analizada por una tranferencia en ranura
de ADN aislado de las colas y la producción de la cadena pesada
humana es analizada mediante la obtención de una cantidad pequeña
de suero y ensayado en busca de la presencia de cadenas Ig con
anticuerpos anti humanos de conejo.
Como alternativa a la microinyección, el ADN YAC
es transferido a las células ES murinas por células ES: fusión de
protoplasto de levadura (Traver y otros, 1989 Proc. Natl.
Acad.Sc, USA, 86:5898-5902; Pachnis y otros,
1990, ibid 87:5109-5113). Primero, el gen
resistente a la neomicina del pMCINeo y un marcador de selección de
levadura son insertados en las secuencias del vector YAC no
esenciales en un plásmido. Esta construcción es usada para
transformar una cepa de levadura que contiene el IgH YAC, y el
pMCINeo es integrado en las secuencias del vector del IgH YAC por
recombinación homóloga. El YAC modificado es luego transferido a la
célula ES por fusión de protoplastos (Traver y otros, 1989;
Pachnis y otros, 1990), y las células ES resistentes a G418
resultantes que contienen las secuencias IgH humanas intactas son
usadas para generar ratones quiméricos.
Las secuencias humanas reemplazantes incluyen el
fragmento Spel de 100 kpb del ADN geonómico que rodea la región de
la cadena pesada
VH6-D-J-C\mu.-C\delta
humana aislada de una librería YAC humana como se describe
anteriormente. Las secuencias de la cadena pesada de ratón
flanqueantes, que dirigen el evento de reemplazamiento por
recombinación homóloga, contienen un fragmento BamHI de 10 kpb de la
cadena pesada C\epsilon-C\alpha de ratón y un
fragmento J558 5' que comprende la mitad 5' del fragmento J558 de
la región variable de la cadena pesada de ratón, y los extremos 3' y
5' de las secuencias humanas, respectivamente (Gráfica 4). Estas
secuencias de ratón son aisladas de una librería genómica
embrionaria de ratón usando las sondas descritas en Tucker y
otros, PNAS USA, 78: 7684-7688, 1981 y
Blankenstein y Krawinkel (1987, supra), respectivamente. El
fragmento BamHI a Xhol de 1150 pb, que contiene un gen resistente a
la neomicina dirigido por el promotor (HSV-tk) del
gen de la timidina quinasa de virus del Herpes simplex y un
potenciador de polioma son aislado del pMClNeo (Koller y Smithies,
1989, supra). Un adaptador sintético es añadido a este
fragmento para convertir el extremo Xhol en un extremo BamHI y el
fragmento resultante es unido al BamHI
C\epsilon-C\alpha de ratón en un plásmido.
A partir del clon YAC que contiene el locus de
la cadena pesada humana, las secuencias de ADN de cada extremo del
inserto son recuperadas bien mediante PCR inversa (Silverman y
otros, PNAS, 86:7485-7489, 1989) o bien mediante
rescate del plásmido en E. coli (Burke y otros, 1987;
Garza y otros, Science, 246: 641-646, 1989;
Traver y otros, 1989) (véase la Gráfica 4). La secuencia
humana aislada del extremo 5' V6 del YAC es ligada a la secuencia
J558 de ratón en un plásmido y asimismo, la secuencia humana
derivada del extremo 3' C\delta del YAC es ligada al gen Neo en el
plásmido que contiene el gen Neo y el
C\epsilon-C\alpha de ratón descrito
anteriormente. El segmento J558 de ratón-V6 humano
es ahora subclonado en un vector de clonación mitad YAC que incluye
un marcador de selección de levadura (HIS3) no presente en la IgH
YAC original, un centrómero (CEN) y un telómero único (TEL). El
C\epsilon-C\alpha de ratón-Neo-
C\delta humano es asimismo subclonado en un vector mitad YAC
separado mediante un marcador de selección de levadura diferente
(LEU2) y un TEL único. El vector mitad YAC que contiene el ADN V6
humano es linearizado y usado para transformar una cepa de levadura
que tiene delecionados los sitios LEU2 y HIS3 cromosómicos y que
lleva la IgH YAC.
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La selección para la prototrofía a histidina da
lugar a colonias de levadura que han sufrido una recombinación
homóloga entre las secuencias de ADN V6 y que contienen un YAC
recombinante. El vector mitad YAC que contiene el ADN C\delta
humano es luego linearizado y usado para transformar la cepa de
levadura generada en la etapa anterior. La selección para la
prototrofía a leucina da como resultado en una cepa de levadura que
contiene el YAC con reemplazamiento de IgH completo (véase la
Gráfica 4). Este YAC es aislado e introducido en las células ES por
microinyección como se describe anteriormente para los
embriones.
Según los procedimientos anteriores, un
hospedante no primate quimérico o antigénico, particularmente un
hospedante ratón, puede ser producido, el cual puede ser inmunizado
para producir anticuerpos humanos o análogos específicos para un
inmunógeno. De esta manera, los problemas asociados con los
anticuerpos monoclonales humanos obtenidos son evitados, puesto que
los ratones pueden ser inmunizados con inmunógenos que no podrían
ser usados con un hospedante humano. Además, se puede proporcionar
inyecciones de recuerdo y adyuvantes que no podrían ser permitidos
con un hospedante humano. Las células B resultantes pueden ser
luego usadas para inmortalización para la producción continua del
anticuerpo deseado. Las células inmortalizadas pueden ser usadas
para el aislamiento de los genes que codifican la inmunoglobulina o
análogos y ser sujetos a mutación por mutagénesis in vitro u
otras técnicas mutagénicas para modificar las propiedades de los
anticuerpos. Estos genes mutados pueden ser luego devueltos a las
células inmortalizadas para la recombinación homóloga para
proporcionar una fuente celular de mamífero continua de los
anticuerpos deseados. El sujeto del invento proporciona una fuente
conveniente de anticuerpos humanos, en la que los anticuerpos
humanos son producidos de forma análoga a la producción de
anticuerpos en un hospedante humano. Las células de ratón
proporcionan convenientemente la activación y reajuste del ADN
humano en las células de ratón para la producción de anticuerpos
humanos.
Claims (7)
1. Un vector dirigido de recombinación homóloga
que comprende una secuencia nucleotídica que tiene homología con las
secuencias intrónicas 3' y 5' de, y próximas a los genes de los
segmentos de la región (J) de unión de una cadena pesada o una
cadena ligera kappa en un locus endógeno de inmunoglobulina de un
ratón y que tiene un gen marcador entre medias, siendo dicho vector
capaz de recombinar homólogamente con dicho locus endógeno de
inmunoglobulina de ratón y de reemplazar todos los genes de la
región (J) de unión con dicho gen marcador para evitar el
reordenamiento funcional de dicho locus y la producción de un
mensajero funcional que codifica una inmunoglobulina.
2. El vector dirigido de la reivindicación 1,
en el que el gen marcador es un gen resistente a la neomicina.
3. Un método de inactivación de un locus de
cadena ligera kappa o pesada endógena de inmunoglobulina en un
mamífero no humano que comprende la etapa de delecionar suficientes
secuencias del locus de Ig para evitar el reordenamiento del locus
de Ig o para evitar la producción de un mensajero funcional que
codifica el locus de Ig.
4. El método de la reivindicación 3, en el que
el locus de Ig es el locus de la cadena pesada de Ig.
5. El método de la reivindicación 3, en el que
el locus de Ig es el locus de la cadena ligera kappa de Ig.
6. Un ratón producido por el método de la
reivindicación 3, en el que dicha deleción está en una región C del
locus de la cadena pesada de inmunoglobulina.
7. Un ratón producido por el método de la
reivindicación 3, en el que dicha deleción está en el locus de la
cadena ligera kappa de inmunoglobulina.
Applications Claiming Priority (4)
Application Number | Priority Date | Filing Date | Title |
---|---|---|---|
US46600890A | 1990-01-12 | 1990-01-12 | |
US61051590A | 1990-11-08 | 1990-11-08 | |
US610515 | 1990-11-08 | ||
US466008 | 1990-11-08 |
Publications (1)
Publication Number | Publication Date |
---|---|
ES2284161T3 true ES2284161T3 (es) | 2007-11-01 |
Family
ID=27041502
Family Applications (2)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ES95115451T Expired - Lifetime ES2284161T3 (es) | 1990-01-12 | 1991-01-11 | Generacion de anticuerpos xenogenicos. |
ES91903098T Expired - Lifetime ES2087997T3 (es) | 1990-01-12 | 1991-01-11 | Generacion de anticuerpos xenogenicos. |
Family Applications After (1)
Application Number | Title | Priority Date | Filing Date |
---|---|---|---|
ES91903098T Expired - Lifetime ES2087997T3 (es) | 1990-01-12 | 1991-01-11 | Generacion de anticuerpos xenogenicos. |
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---|---|
US (3) | US5939598A (es) |
EP (4) | EP1690935A3 (es) |
JP (10) | JP3068180B2 (es) |
KR (1) | KR100203511B1 (es) |
AT (2) | ATE139258T1 (es) |
AU (1) | AU633698B2 (es) |
CA (1) | CA2050918A1 (es) |
DE (2) | DE69120146T2 (es) |
DK (2) | DK0463151T3 (es) |
ES (2) | ES2284161T3 (es) |
GR (1) | GR3020240T3 (es) |
HK (2) | HK1007330A1 (es) |
NO (2) | NO913558L (es) |
SG (1) | SG48759A1 (es) |
WO (1) | WO1991010741A1 (es) |
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1991
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- 1991-01-11 AU AU71814/91A patent/AU633698B2/en not_active Expired
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- 1991-01-11 EP EP06006801A patent/EP1690934A3/en not_active Withdrawn
- 1991-01-11 WO PCT/US1991/000245 patent/WO1991010741A1/en active IP Right Grant
- 1991-01-11 AT AT91903098T patent/ATE139258T1/de not_active IP Right Cessation
- 1991-01-11 DK DK91903098.1T patent/DK0463151T3/da active
- 1991-01-11 ES ES95115451T patent/ES2284161T3/es not_active Expired - Lifetime
- 1991-01-11 SG SG9601352A patent/SG48759A1/en unknown
- 1991-01-11 AT AT95115451T patent/ATE356869T1/de not_active IP Right Cessation
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- 1991-01-11 DK DK95115451T patent/DK0710719T3/da active
- 1991-01-11 DE DE69120146T patent/DE69120146T2/de not_active Expired - Lifetime
- 1991-01-11 EP EP91903098A patent/EP0463151B1/en not_active Expired - Lifetime
- 1991-01-11 DE DE69133566T patent/DE69133566T2/de not_active Expired - Lifetime
- 1991-01-11 CA CA002050918A patent/CA2050918A1/en not_active Abandoned
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- 1991-09-11 KR KR1019910701093A patent/KR100203511B1/ko not_active IP Right Cessation
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1992
- 1992-07-30 US US07/922,649 patent/US5939598A/en not_active Expired - Lifetime
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1995
- 1995-06-05 US US08/464,582 patent/US6114598A/en not_active Expired - Lifetime
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1996
- 1996-06-17 GR GR960401184T patent/GR3020240T3/el unknown
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1997
- 1997-06-05 JP JP9147795A patent/JP3068506B2/ja not_active Expired - Lifetime
- 1997-06-05 JP JP9147805A patent/JP3068507B2/ja not_active Expired - Lifetime
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1998
- 1998-06-24 HK HK98106528A patent/HK1007330A1/xx not_active IP Right Cessation
- 1998-09-21 HK HK98110786A patent/HK1009979A1/xx not_active IP Right Cessation
- 1998-12-11 JP JP10352239A patent/JPH11262388A/ja active Pending
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- 1998-12-11 JP JP10352242A patent/JPH11239491A/ja active Pending
- 1998-12-11 JP JP10352243A patent/JPH11243973A/ja not_active Withdrawn
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- 1998-12-11 JP JP10352240A patent/JPH11239490A/ja active Pending
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2001
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