Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein

S. S.L. Chen, C. N. Lee, W. R. Lee, K. McIntosh, T. H. Lee

研究成果: 雜誌貢獻評論/辯論同行評審

110 引文 斯高帕斯(Scopus)

摘要

The N-terminal region of the envelope (env) transmembrane protein of human immunodeficiency virus type 1 (HIV-1) has a leucine zipper-like motif. This highly conserved zipper motif, which consists of a heptad repeat of leucine or isoleucine residues, has been suggested to play a role in HIV-1 env glycoprotein oligomerization. This hypothesis was tested by replacing the highly conserved leucine or isoleucine residues in the zipper motif with a strong α-helix breaker, proline. We report here that such substitutions did not abolish the ability of env protein to form oligomers, indicating that this highly conserved zipper motif does not have a crucial role in env protein oligomerization. However, the mutant viruses all showed impaired infectivity, suggesting that this conserved zipper motif can have an important role in the virus life cycle.

原文英語
頁(從 - 到)3615-3619
頁數5
期刊Journal of Virology
67
發行號6
DOIs
出版狀態已發佈 - 1993

ASJC Scopus subject areas

  • 微生物學
  • 免疫學
  • 昆蟲科學
  • 病毒學

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