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

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. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.