Actin-dependent receptor colocalization required for human immunodeficiency virus entry into host cells

S. Iyengar, James Hildreth, D. H. Schwartz

Research output: Contribution to journalArticle

165 Scopus citations

Abstract

Human immunodeficiency virus (HIV) envelope binds CD4 and a chemokine receptor in sequence, releasing hydrophobic vital gp41 residues into the target membrane. HIV entry required actin-dependent concentration of coreceptors, which could be disrupted by cytochalasin D (CytoD) without an effect on cell viability or mitosis. Pretreatment of peripheral blood mononuclear cells, but not virus, inhibited entry and infection. Immunofluorescent confocal microscopy of activated cells revealed CD4 and CXCR4 in nonoverlapping patterns. Addition of gp120 caused polarized cocapping of both molecules with subsequent pseudopod formation, while CytoD pretreatment blocked these membrane changes completely.

Original languageEnglish (US)
Pages (from-to)5251-5255
Number of pages5
JournalJournal of Virology
Volume72
Issue number6
StatePublished - 1998
Externally publishedYes

ASJC Scopus subject areas

  • Immunology

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