Antibodies that are specific for a single amino acid interchange in a protein epitope use structurally distinct variable regions.
J Exp Med
; 174(3): 613-24, 1991 Sep 01.
Article
en En
| MEDLINE
| ID: mdl-1908510
ABSTRACT
We have analyzed how the immune system generates antibodies that are specific for analogues of an epitope on the influenza virus hemagglutinin (HA) that differ solely by the presence of Asp or Gly at amino acid 225. Most antibodies induced in response to HA(Asp225) use one of a few closely related variable (V) region structures that are encoded by characteristic VH/Vk gene segment combinations. Remarkably, none of these VH/Vk combinations was induced in response to HA(Gly225). Instead of modifying the HA(Asp225)-specific V regions by junctional variation or somatic mutation to recognize the altered epitope, new VH/Vk combinations were used. The expression of unique VH/Vk combinations appears to confer exquisite specificity to the selection of HA-specific B cells from the pre-immune repertoire.
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1
Bases de datos:
MEDLINE
Asunto principal:
Virus de la Influenza A
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Hemaglutininas Virales
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Anticuerpos Antivirales
/
Especificidad de Anticuerpos
Límite:
Animals
Idioma:
En
Revista:
J Exp Med
Año:
1991
Tipo del documento:
Article