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J Virol. 2007 Feb;81(3):1472-8. Epub 2006 Nov 15.

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

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  • 1Vollum Institute and Department of Molecular Microbiology and Immunology, Oregon Health & Sciences University, Mail Code L220, 3181 SW Sam Jackson Park Road, Portland, OR 97201-3098, USA.


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 HIV assembly and interactions between MA and the viral membrane glycoproteins.

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