Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41.
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.
Lee
W R
WR
Department of Cancer Biology, Harvard University School of Public Health, Boston, Massachusetts 02115.
Yu
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XF
Syu
W J
WJ
Essex
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M
Lee
T H
TH
D000818:Animals; D001483:Base Sequence; D002478:Cells, Cultured; D002522:Chlorocebus aethiops; D004252:DNA Mutational Analysis; D006031:Glycosylation; D015700:HIV Envelope Protein gp41 / Q000737:chemistry* / Q000235:genetics; D015497:HIV-1 / Q000235:genetics* / Q000254:growth & development / Q000472:pathogenicity; D006801:Humans; D066298:In Vitro Techniques; D008562:Membrane Glycoproteins / Q000737:chemistry; D008969:Molecular Sequence Data; D009838:Oligodeoxyribonucleotides / Q000737:chemistry; D013329:Structure-Activity Relationship
D015700:HIV Envelope Protein gp41; D008562:Membrane Glycoproteins; D009838:Oligodeoxyribonucleotides