The possible involvement of CXCR4 in the inhibition of HIV-1 infection mediated by DP178/gp41.

Abstract

The N- (N36/DP107) and C-terminal peptides (C34/DP178) from two alpha-helical domains of human immunodeficiency virus type 1 (HIV-1) gp41 inhibited HIV infection. A single-round infection using pseudotyped virus clarified that a greater amount of gp41-derived peptides was necessary for the inhibition of R5 virus (ADA) infection than for that of X4 virus (LAI) infection. Furthermore, R5X4 virus (89.6) infection via CCR5 needs more peptides for inhibition than its infection via CXCR4 does. A high sensitivity of X4 virus was partially ascribed to the inhibition of the 12G5 binding to CXCR4 by DP178LAI.

• Authors: Y Xu, X Zhang, M Matsuoka, T Hattori
• Journal: FEBS letters (FEBS Lett) Vol. 487 Issue 2 Pg. 185-8 (Dec 29 2000) ISSN: 0014-5793 [Print] England
• PMID: 11150506 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Anti-HIV Agents
• CD4 Antigens
• HIV Envelope Protein gp41
• Peptide Fragments
• Receptors, CCR5
• Receptors, CXCR4
• Enfuvirtide
• Luciferases

Topics

• Amino Acid Sequence
• Anti-HIV Agents (pharmacology)
• Astrocytes
• CD4 Antigens (physiology)
• Cell Line
• Enfuvirtide
• Genes, Reporter
• HIV Envelope Protein gp41 (chemistry, immunology, pharmacology)
• HIV Infections (immunology)
• HIV-1 (drug effects, physiology)
• Humans
• Kidney
• Luciferases (genetics)
• Molecular Sequence Data
• Peptide Fragments (chemistry, pharmacology)
• Receptors, CCR5 (physiology)
• Receptors, CXCR4 (physiology)
• Transfection