Abstract
A cofactor for HIV-1 (human immunodeficiency virus-type 1) fusion and entry was identified with the use of a novel functional complementary DNA (cDNA) cloning strategy. This protein, designated "fusin," is a putative G protein-coupled receptor with seven transmembrane segments. Recombinant fusin enabled CD4-expressing nonhuman cell types to support HIV-1 Env-mediated cell fusion and HIV-1 infection. Antibodies to fusin blocked cell fusion and infection with normal CD4-positive human target cells. Fusin messenger RNA levels correlated with HIV-1 permissiveness in diverse human cell types. Fusin acted preferentially for T cell line-tropic isolates, in comparison to its activity with macrophagetropic HIV-1 isolates.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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3T3 Cells
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Amino Acid Sequence
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Animals
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CD4 Antigens / physiology*
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CD4-Positive T-Lymphocytes / virology
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Cell Line
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Cell Membrane / virology
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Chemokines / physiology
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Cloning, Molecular*
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DNA, Complementary / genetics
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Disease Models, Animal
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GTP-Binding Proteins / metabolism
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Giant Cells
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HIV Envelope Protein gp120 / physiology
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HIV-1 / pathogenicity*
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HIV-1 / physiology
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HeLa Cells
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Humans
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Leukocytes, Mononuclear / virology
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Macrophages / virology
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Membrane Fusion*
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Membrane Proteins / genetics
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Membrane Proteins / physiology*
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Mice
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Molecular Sequence Data
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RNA, Messenger / metabolism
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Receptors, CXCR4
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Recombinant Proteins
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Transfection
Substances
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CD4 Antigens
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Chemokines
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DNA, Complementary
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HIV Envelope Protein gp120
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Membrane Proteins
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RNA, Messenger
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Receptors, CXCR4
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Recombinant Proteins
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GTP-Binding Proteins