Abstract
Approximately half of the molecular mass of gp120, the receptor-binding envelope protein of human immunodeficiency virus (HIV), consists of N-linked glycans. Nearly half of these glycans are of the high mannose type. These high mannose glycans furnish a rich forest of mannose residues on the virus surface making HIV a prime target for interaction with mannose-specific lectins of the immune system. This review focuses on the known interactions between gp120 and immune system lectins some of which HIV appears to exploit. The effect of variation in glycosylation of gp120, especially with respect to clades of HIV, on binding of immune system lectins is highlighted.
Publication types
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Research Support, N.I.H., Extramural
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Review
MeSH terms
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Animals
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Bacterial Proteins / chemistry
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Carrier Proteins / chemistry
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Cell Adhesion Molecules / chemistry
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Glycosylation
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HIV / metabolism*
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HIV Envelope Protein gp120 / chemistry
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HIV Infections / immunology
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Humans
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Immune System / virology*
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Lectins / chemistry*
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Lectins, C-Type / chemistry
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Polysaccharides / chemistry*
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Protein Structure, Tertiary
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Receptors, Cell Surface / chemistry
Substances
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Bacterial Proteins
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Carrier Proteins
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Cell Adhesion Molecules
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DC-specific ICAM-3 grabbing nonintegrin
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HIV Envelope Protein gp120
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Lectins
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Lectins, C-Type
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Polysaccharides
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Receptors, Cell Surface
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cyanovirin N