Abstract
Amino acid substitutions were introduced into four conserved N-linked glycosylation sites of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein, gp41, to alter the canonical N-linked glycosylation sequences. One altered site produced a severe impairment of viral infectivity, which raises the possibility that N-linked sugars at this site may have an important role in the human immunodeficiency virus type 1 life cycle.
Publication types
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Animals
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Base Sequence
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Cells, Cultured
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Chlorocebus aethiops
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DNA Mutational Analysis
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Glycosylation
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HIV Envelope Protein gp41 / chemistry*
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HIV Envelope Protein gp41 / genetics
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HIV-1 / genetics*
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HIV-1 / growth & development
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HIV-1 / pathogenicity
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Humans
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In Vitro Techniques
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Membrane Glycoproteins / chemistry
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Molecular Sequence Data
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Oligodeoxyribonucleotides / chemistry
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Structure-Activity Relationship
Substances
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HIV Envelope Protein gp41
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Membrane Glycoproteins
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Oligodeoxyribonucleotides