Human neutrophil alpha-defensin 4 inhibits HIV-1 infection in vitro.

Abstract

Human neutrophil alpha-defensin 4 (HNP4) is more effective than HNP1-3 in protecting human peripheral blood mononuclear cells from infection by both X4 and R5 HIV-1 strains. HNP4 binds to both CD4 and gp120 approximately two orders of magnitude weaker than does HNP1, and is less effectively sequestered by glycosylated serum proteins than HNP1. These results suggest that the HIV-1 inhibition by HNP4 stems at least partially from a unique and lectin-independent property of HNP4 with CD4 and/or gp120. Our finding identifies an anti-HIV-1 property of HNP4 and may have implications in the development of new antiviral agents for AIDS therapy.

• Authors: Zhibin Wu, Fiorenza Cocchi, David Gentles, Bryan Ericksen, Jacek Lubkowski, Anthony Devico, Robert I Lehrer, Wuyuan Lu
• Journal: FEBS letters (FEBS Lett) Vol. 579 Issue 1 Pg. 162-6 (Jan 03 2005) ISSN: 0014-5793 [Print] England
• PMID: 15620707 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Anti-HIV Agents
• CD4 Antigens
• HIV Envelope Protein gp120
• Ligands
• alpha-Defensins
• human neutrophil peptide 1
• human neutrophil peptide 4

Topics

• Anti-HIV Agents (pharmacology, therapeutic use)
• CD4 Antigens (metabolism)
• HIV Envelope Protein gp120 (metabolism)
• HIV Infections (drug therapy)
• HIV-1 (drug effects)
• Humans
• Leukocytes, Mononuclear (virology)
• Ligands
• alpha-Defensins (pharmacology, therapeutic use)