Abstract
Current recombinant human immunodeficiency virus (HIV) gp120 protein vaccine candidates are unable to elicit antibodies capable of neutralizing infectivity of primary isolates from patients. Here, "fusion-competent" HIV vaccine immunogens were generated that capture the transient envelope-CD4-coreceptor structures that arise during HIV binding and fusion. In a transgenic mouse immunization model, these formaldehyde-fixed whole-cell vaccines elicited antibodies capable of neutralizing infectivity of 23 of 24 primary HIV isolates from diverse geographic locations and genetic clades A to E. Development of these fusion-dependent immunogens may lead to a broadly effective HIV vaccine.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
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Comment
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Retracted Publication
MeSH terms
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AIDS Vaccines / immunology*
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Animals
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CD4 Antigens / metabolism
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Cell Fusion
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Coculture Techniques
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Epitopes / immunology
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Gene Products, env / chemistry
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Gene Products, env / immunology*
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Gene Products, env / metabolism
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Giant Cells
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HIV Antibodies / biosynthesis
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HIV Antibodies / immunology*
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HIV Antigens / chemistry
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HIV Antigens / immunology*
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HIV Envelope Protein gp120 / chemistry
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HIV Envelope Protein gp120 / immunology
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HIV Envelope Protein gp120 / metabolism
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HIV Envelope Protein gp41 / chemistry
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HIV Envelope Protein gp41 / immunology
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HIV Envelope Protein gp41 / metabolism
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HIV Infections / virology
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HIV-1 / immunology*
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HIV-1 / isolation & purification
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HIV-1 / physiology
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Humans
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Mice
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Mice, Transgenic
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Neutralization Tests
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Protein Conformation
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Receptors, CCR5 / metabolism
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Tumor Cells, Cultured
Substances
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AIDS Vaccines
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CD4 Antigens
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Epitopes
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Gene Products, env
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HIV Antibodies
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HIV Antigens
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HIV Envelope Protein gp120
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HIV Envelope Protein gp41
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Receptors, CCR5