HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate

Ayna Alfadhli, Robin Lid Barklis, Eric Barklis

Research output: Contribution to journalArticlepeer-review

93 Scopus citations


The human immunodeficiency virus type 1 (HIV-1) matrix (MA) protein represents the N-terminal domain of the HIV-1 precursor Gag (PrGag) protein and carries an N-terminal myristate (Myr) group. HIV-1 MA fosters PrGag membrane binding, as well as assembly of envelope (Env) proteins into virus particles, and recent studies have shown that HIV-1 MA preferentially directs virus assembly at plasma membrane sites enriched in cholesterol and phosphatidylinositol-(4,5)-bisphosphate (PI[4,5]P2). To characterize the membrane binding of MA and PrGag proteins, we have examined how Myr-MA proteins, and proteins composed of Myr-MA and its neighbor Gag capsid (CA) protein associate on membranes containing cholesterol and PI[4,5]P2. Our results indicate that Myr-MA assembles as a hexamer of trimers on such membranes, and imply that MA trimers interconnect CA hexamer rings in immature virus particles. Our observations suggest a model for the organization of PrGag proteins, and for MA-Env protein interactions.

Original languageEnglish (US)
Pages (from-to)466-472
Number of pages7
Issue number2
StatePublished - May 10 2009


  • Assembly
  • Capsid
  • Gag
  • HIV
  • Matrix
  • Phosphatidylinositol-(4,5)-bisphosphate

ASJC Scopus subject areas

  • Virology


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