Abstract
The V3 region of HIV-1 envelope protein possesses a single N-linked sugar chain, which is conserved in most HIV-1 strains. We studied its role in the life cycle of HIV-1 strains with different co-receptor usage. Removal of the glycan appeared to cause a marked reduction of CXCR-4- but not CCR-5-dependent virus entry. A basic amino acid substitution at the 11th position of V3 markedly compensated for the removal of the N-glycan. These results indicate that the N-glycan plays an important role for CXCR-4-dependent virus entry and that this role is exerted in a particular context of the peptide backbone.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Amino Acid Substitution
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Cell Line, Transformed
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Giant Cells / virology*
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Glycosylation
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HIV Envelope Protein gp120 / genetics
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HIV Envelope Protein gp120 / metabolism*
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HIV-1 / isolation & purification
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HIV-1 / metabolism*
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HIV-1 / physiology
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Humans
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Molecular Sequence Data
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Mutagenesis, Site-Directed
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Peptide Fragments / genetics
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Peptide Fragments / metabolism*
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Polysaccharides / physiology*
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Receptors, CCR5 / physiology*
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Receptors, CXCR4 / physiology*
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Receptors, HIV / physiology
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Virus Replication
Substances
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HIV Envelope Protein gp120
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HIV envelope protein gp120 (305-321)
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Peptide Fragments
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Polysaccharides
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Receptors, CCR5
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Receptors, CXCR4
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Receptors, HIV