Abstract
A new anti-HIV protein, scytovirin, was isolated from aqueous extracts of the cultured cyanobacterium Scytonema varium. The protein displayed potent anticytopathic activity against laboratory strains and primary isolates of HIV-1 with EC50 values ranging from 0.3 to 22 nM. Scytovirin binds to viral coat proteins gp120, gp160, and gp41 but not to cellular receptor CD4 or other tested proteins. This unique protein consists of a single 95-amino acid chain with significant internal sequence duplication and 10 cysteines forming five intrachain disulfide bonds.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Animals
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Anti-HIV Agents / chemistry*
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Anti-HIV Agents / isolation & purification
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Anti-HIV Agents / pharmacology
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Bacterial Proteins / chemistry*
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Bacterial Proteins / isolation & purification
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Bacterial Proteins / pharmacology
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Carrier Proteins / chemistry*
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Carrier Proteins / isolation & purification
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Carrier Proteins / metabolism
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Carrier Proteins / pharmacology
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Cell Line
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Child
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Chitin / metabolism
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Chlorophyta / chemistry
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Cyanobacteria / chemistry*
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Cyanobacteria / growth & development*
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Disulfides / chemistry
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HIV Envelope Protein gp120 / chemistry
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HIV Envelope Protein gp41 / chemistry
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HIV-1 / drug effects*
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HIV-1 / isolation & purification
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HeLa Cells
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Humans
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Lectins
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Membrane Proteins
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Molecular Sequence Data
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Protein Binding
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Rabbits
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Sequence Homology, Amino Acid
Substances
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Anti-HIV Agents
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Bacterial Proteins
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Carrier Proteins
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Disulfides
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HIV Envelope Protein gp120
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HIV Envelope Protein gp41
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Lectins
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Membrane Proteins
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scytovirin protein, S varium
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Chitin