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- W2169367715 endingPage "2528" @default.
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- W2169367715 abstract "Human immunodeficiency virus type 1 (HIV-1) neutralizing antibodies are thought be distinguished from nonneutralizing antibodies by their ability to recognize functional gp120/gp41 envelope glycoprotein (Env) trimers. The antibody responses induced by natural HIV-1 infection or by vaccine candidates tested to date consist largely of nonneutralizing antibodies. One might have expected a more vigorous neutralizing response, particularly against virus particles that bear functional trimers. The recent surprising observation that nonneutralizing antibodies can specifically capture HIV-1 may provide a clue relating to this paradox. Specifically, it was suggested that forms of Env, to which nonneutralizing antibodies can bind, exist on virus surfaces. Here, we present evidence that HIV-1 particles bear nonfunctional gp120/gp41 monomers and gp120-depleted gp41 stumps. Using a native electrophoresis band shift assay, we show that antibody-trimer binding predicts neutralization and that the nonfunctional forms of Env may account for virus capture by nonneutralizing antibodies. We hypothesize that these nonfunctional forms of Env on particle surfaces serve to divert the antibody response, helping the virus to evade neutralization." @default.
- W2169367715 created "2016-06-24" @default.
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- W2169367715 date "2006-03-01" @default.
- W2169367715 modified "2023-10-18" @default.
- W2169367715 title "Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1" @default.
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- W2169367715 doi "https://doi.org/10.1128/jvi.80.5.2515-2528.2006" @default.
- W2169367715 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1395414" @default.
- W2169367715 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/16474158" @default.
- W2169367715 hasPublicationYear "2006" @default.
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