Structural and functional properties of the membranotropic HIV-1 glycoprotein gp41 loop region are modulated by its intrinsic hydrophobic core

Jiayin Qiu, Avraham Ashkenazi, Shuwen Liu, Yechiel Shai

Research output: Contribution to journalArticlepeer-review

Abstract

Background:HIV-1 infectivity is decreased by specific mutations that alter the hydrophobicity level in the HIV-1 gp41 loop core. Results:Antibody recognition, disulfide-bond formation, and lipid mixing of loop domain peptides are strongly affected by these mutations. Conclusion:The hydrophobic core maintains proper function and structure of the loop region. Significance:A better understanding of the membrane fusion mechanism of HIV and similar viruses is provided.

Original languageAmerican English
Pages (from-to)29143-29150
Number of pages8
JournalJournal of Biological Chemistry
Volume288
Issue number40
DOIs
StatePublished - 4 Oct 2013

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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