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Development of tetravalent, bispecific CCR5 antibodies with antiviral activity against CCR5 monoclonal antibody-resistant HIV-1 strains.
Antimicrob Agents Chemother ; 55(5): 2369-78, 2011 May.
Article en En | MEDLINE | ID: mdl-21300827
In this study, we describe novel tetravalent, bispecific antibody derivatives that bind two different epitopes on the HIV coreceptor CCR5. The basic protein formats that we applied were derived from Morrison-type bispecific antibodies: whole IgGs to which we connected single-chain antibodies (scFvs) via (Gly4Ser)n sequences at either the C or N terminus of the light chain or heavy chain. By design optimization, including disulfide stabilization of scFvs or introduction of 30-amino-acid linkers, stable molecules could be obtained in amounts that were within the same range as or no less than 4-fold lower than those observed with monoclonal antibodies in transient expression assays. In contrast to monospecific CCR5 antibodies, bispecific antibody derivatives block two alternative docking sites of CCR5-tropic HIV strains on the CCR5 coreceptor. Consequently, these molecules showed 18- to 57-fold increased antiviral activities compared to the parent antibodies. Most importantly, one prototypic tetravalent CCR5 antibody had antiviral activity against virus strains resistant to the single parental antibodies. In summary, physical linkage of two CCR5 antibodies targeting different epitopes on the HIV coreceptor CCR5 resulted in tetravalent, bispecific antibodies with enhanced antiviral potency against wild-type and CCR5 antibody-resistant HIV-1 strains.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: VIH-1 / Anticuerpos Biespecíficos / Receptores CCR5 Límite: Humans Idioma: En Revista: Antimicrob Agents Chemother Año: 2011 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: VIH-1 / Anticuerpos Biespecíficos / Receptores CCR5 Límite: Humans Idioma: En Revista: Antimicrob Agents Chemother Año: 2011 Tipo del documento: Article País de afiliación: Alemania Pais de publicación: Estados Unidos