Structure and Interaction with Membrane Model Systems of a Peptide Derived from the Major Epitope Region of HIV Protein gp41: Implications on Viral Fusion Mechanism

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• 作者：Lellys M. Contreras ; Francisco J. Aranda ; Francisco Gavilanes ; José ; M. Gonzá ; lez-Ros ; and José ; Villalaí ; n
• 刊名：Biochemistry
• 出版年：2001
• 出版时间：March 13, 2001
• 年：2001
• 卷：40
• 期：10
• 页码：3196 - 3207
• 全文大小：158K
• 年卷期：v.40,no.10(March 13, 2001)
• ISSN：1520-4995

文摘

The HIV-1 gp41 envelope protein mediates entry of the virus into the target cell by promotingmembrane fusion. With a view toward possible new insights into viral fusion mechanisms, we haveinvestigated by infrared, fluorescence, and nuclear magnetic resonance spectroscopies and calorimetry afragment of 19 amino acids corresponding to the immunodominant region of the gp41 ectodomain, ahighly conserved sequence and major epitope. Information on the structure of the peptide both in solutionand in the presence of model membranes, its incorporation and location in the phospholipid bilayer, andthe modulation of the phase behavior of the membrane has been gathered. Here we demonstrate that thepeptide binds and interacts with negatively charged phospholipids, changes its conformation in the presenceof a membraneous medium, and induces leakage of vesicle contents as well as a new phospholipid phase.These characteristics might be important for the formation of the fusion-active gp41 core structure,promoting the close apposition of the two viral and target-cell membranes and therefore provoking fusion.