Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamer

Ayna Alfadhli, Doug Huseby, Eliot Kapit, Dalbinder Colman, Eric Barklis

Research output: Contribution to journalArticle

36 Scopus citations

Abstract

The membrane-binding matrix (MA) domain of the human immunodeficiency virus type 1 (HIV-1) structural precursor Gag (PrGag) protein oligomerizes in solution as a trimer and crystallizes in three dimensions as a trimer unit. A number of models have been proposed to explain how MA trimers might align with respect to PrGag capsid (CA) N-terminal domains (NTDs), which assemble hexagonal lattices. We have examined the binding of naturally myristoylated HIV-1 matrix (MyrMA) and matrix plus capsid (MyrMACA) proteins on membranes in vitro. Unexpectedly, MyrMA and MyrMACA proteins both assembled hexagonal cage lattices on phosphatidylserine-cholesterol membranes. Membrane-bound MyrMA proteins did not organize into trimer units but, rather, organized into hexamer rings. Our results yield a model in which MA domains stack directly above NTD hexamers in immature particles, and they have implications for IUV assembly and interactions between MA and the viral membrane glycoproteins.

Original languageEnglish (US)
Pages (from-to)1472-1478
Number of pages7
JournalJournal of virology
Volume81
Issue number3
DOIs
StatePublished - Feb 2007

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Insect Science
  • Virology

Fingerprint Dive into the research topics of 'Human immunodeficiency virus type 1 matrix protein assembles on membranes as a hexamer'. Together they form a unique fingerprint.

  • Cite this