HIV-1 p17 matrix protein interacts with heparan sulfate side chain of CD44v3, syndecan-2, and syndecan-4 proteoglycans expressed on human activated CD4+ T cells affecting tumor necrosis factor alpha and interleukin 2 production.
J Biol Chem
; 286(22): 19541-8, 2011 Jun 03.
Article
en En
| MEDLINE
| ID: mdl-21482826
ABSTRACT
HIV-1 p17 contains C- and N-terminal sequences with positively charged residues and a consensus cluster for heparin binding. We have previously demonstrated by affinity chromatography that HIV-1 p17 binds strongly to heparin-agarose at physiological pH and to human activated CD4(+) T cells. In this study we demonstrated that the viral protein binds to heparan sulfate side chains of syndecan-2, syndecan-4, and CD44v3 purified from HeLa cells and that these heparan sulfate proteoglycans (HSPGs) co-localize with HIV-1 p17 on activated human CD4(+) T cells by confocal fluorescence analysis. Moreover, we observed a stimulatory or inhibitory activity when CD4(+) T cells were activated with mitogens together with nanomolar or micromolar concentrations of the matrix protein.
Texto completo:
1
Bases de datos:
MEDLINE
Asunto principal:
Antígenos VIH
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Linfocitos T CD4-Positivos
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VIH-1
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Interleucina-2
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Factor de Necrosis Tumoral alfa
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Receptores de Hialuranos
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Sindecano-2
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Sindecano-4
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Productos del Gen gag del Virus de la Inmunodeficiencia Humana
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Heparitina Sulfato
Límite:
Female
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Humans
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Male
Idioma:
En
Revista:
J Biol Chem
Año:
2011
Tipo del documento:
Article
País de afiliación:
Italia