Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41

W. R. Lee; X. F. Yu; W. J. Syu; M. Essex; T. H. Lee

doi:10.1128/jvi.66.3.1799-1803.1992

Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41

W. R. Lee, X. F. Yu, W. J. Syu, M. Essex, T. H. Lee

Research output: Contribution to journal › Comment/debate › peer-review

40 Citations (Scopus)

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.

Original language	English
Pages (from-to)	1799-1803
Number of pages	5
Journal	Journal of Virology
Volume	66
Issue number	3
DOIs	https://doi.org/10.1128/jvi.66.3.1799-1803.1992
Publication status	Published - 1992
Externally published	Yes

ASJC Scopus subject areas

Microbiology
Immunology
Insect Science
Virology

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.1128/jvi.66.3.1799-1803.1992

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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.",

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AU - Yu, X. F.

AU - Syu, W. J.

AU - Essex, M.

AU - Lee, T. H.

PY - 1992

Y1 - 1992

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AB - 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.

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U2 - 10.1128/jvi.66.3.1799-1803.1992

DO - 10.1128/jvi.66.3.1799-1803.1992

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C2 - 1738209

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Mutational analysis of conserved N-linked glycosylation sites of human immunodeficiency virus type 1 gp41

Abstract

ASJC Scopus subject areas

UN SDGs

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