Abstract
We previously described a significant sequence homology between HIV-1 gp120 and the functional sites responsible for the specific binding of snake curare-mimetic neurotoxins and rabies virus glycoprotein to the nicotinic acetylcholine receptor. Here we report findings about the existence of a mechanism of functional molecular mimicry which could enable the binding of HIV-1 gp120 to nicotinic acetylcholine receptors in muscle cells and neurons.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetylcholine / pharmacology
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Amino Acid Sequence
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Antigens, Viral*
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Binding, Competitive
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Bungarotoxins / metabolism
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Glycoproteins / chemistry
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HIV Envelope Protein gp120 / chemistry
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HIV Envelope Protein gp120 / metabolism*
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HIV Envelope Protein gp120 / pharmacology
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HIV-1 / metabolism*
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Humans
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Molecular Sequence Data
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Muscles / metabolism
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Neurotoxins / chemistry
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Nicotine / pharmacology
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Receptors, Nicotinic / metabolism*
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Sequence Homology, Amino Acid
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Tumor Cells, Cultured
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Viral Envelope Proteins / chemistry
Substances
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Antigens, Viral
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Bungarotoxins
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Glycoproteins
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HIV Envelope Protein gp120
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Neurotoxins
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Receptors, Nicotinic
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Viral Envelope Proteins
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glycoprotein G, Rabies virus
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Nicotine
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Acetylcholine