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

S. Iyengar, J. E K Hildreth, D. H. Schwartz

    Research output: Contribution to journalArticle

    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

    ASJC Scopus subject areas

    • Immunology

    Fingerprint Dive into the research topics of 'Actin-dependent receptor colocalization required for human immunodeficiency virus entry into host cells'. Together they form a unique fingerprint.

  • Cite this