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 journalComment/debate

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 languageEnglish
Pages (from-to)1799-1803
Number of pages5
JournalJournal of Virology
Volume66
Issue number3
DOIs
Publication statusPublished - 1992

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

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