Friday, 27 February 2015 10:15

Nueva diana para el tratamiento de una inmunodeficiencia “rara”

El grupo de Santos Mañes en el Centro Nacional de Biotecnología del CSIC, en colaboración con investigadores de Harvard Medical School de los Estados Unidos, han descubierto que la proteína filamina A es esencial para contrarrestar las mutaciones que originan el Síndrome de WHIM, una inmunodeficiencia congénita rara caracterizada por una neutropenia severa, una linfopenia de células B, hipogammaglobulinemia, infecciones bacterianas y virales recurrentes, y retención de neutrófilos en la médula ósea (mielocatexis).

WHIMWHIM es un acrónimo de los principales síntomas de la enfermedad: verrugas (Warts, en inglés), que se originan por infecciones crónicas con el virus del papiloma humano, hipogammaglobulinemia, infecciones y mielocatexis. Su prevalencia o incidencia en la población general es desconocida, aunque es extremadamente baja, en torno a 0.2/millón de nacimientos. Sólo se han descrito unos 60 casos en la literatura médica, la mayoría en países del sur de Europa (Francia e Italia) y en Estados Unidos. Hasta el momento no se han reportado casos de este Síndrome en España.

El Síndrome de WHIM se origina como consecuencia de mutaciones en el gen que codifica para el receptor de quimioquinas CXCR4. CXCR4 es una proteína de la superficie de las células sanguíneas, que se activa de forma transitoria tras unirse a otra proteína llamada CXCL12; la activación de CXCR4 hace que este se introduzca dentro de las células (un proceso llamado endocitosis) provocando así el apagamiento de la señal. Las mutaciones asociadas al Síndrome de WHIM imposibilitan que CXCR4 se internalice en la célula, haciendo que el receptor esté funcionando continuamente. Según explica Mañes, sus investigaciones muestran que “la filamina A es esencial para que el CXCR4 permanezca funcionando continuamente en los pacientes con Síndrome de WHIM.

Filamina A es una proteína encargada de anclar los receptores de membrana al esqueleto celular. El grupo de Mañes ya sabía que filamina A era capaz de unirse una porción terminal de CXCR4, justamente aquella porción donde se acumulan las mutaciones asociadas al Síndrome de WHIM. Usando estrategias bioinformáticas han encontrado que filamina A también se une a otra región de CXCR4, llamada bucle intracelular 3, y esta unión hace que el receptor se mantenga funcionando por más tiempo en la superficie de las células. Cuando los investigadores impidieron la unión de filamina A al bucle intracelular 3 de receptores con Síndrome de WHIM, estos receptores se internalizaban y recuperaban su función normal. Los resultados obtenidos señalan que fármacos que consigan bloquear la interacción entre filamina A y el CXCR4 mutado pueden constituir nuevas aproximaciones terapéuticas para una enfermedad para la que no existe tratamiento en la actualidad.

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