Glycan Microheterogeneity at the PGT135 Antibody Recognition Site on HIV-1 gp120 Reveals a Molecular Mechanism for Neutralization Resistance.
J Virol
; 89(13): 6952-9, 2015 Jul.
Article
em En
| MEDLINE
| ID: mdl-25878100
ABSTRACT
Broadly neutralizing antibodies have been isolated that bind the glycan shield of the HIV-1 envelope spike. One such antibody, PGT135, contacts the intrinsic mannose patch of gp120 at the Asn332, Asn392, and Asn386 glycosylation sites. Here, site-specific glycosylation analysis of recombinant gp120 revealed glycan microheterogeneity sufficient to explain the existence of a minor population of virions resistant to PGT135 neutralization. Target microheterogeneity and antibody glycan specificity are therefore important parameters in HIV-1 vaccine design.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Polissacarídeos
/
Anticorpos Anti-HIV
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Proteína gp120 do Envelope de HIV
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HIV-1
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Anticorpos Neutralizantes
Idioma:
En
Revista:
J Virol
Ano de publicação:
2015
Tipo de documento:
Article
País de afiliação:
Reino Unido