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Journal of Virology, February 2007, p. 1472-1478, Vol. 81, No. 3
0022-538X/07/$08.00+0 doi:10.1128/JVI.02122-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Eliot Kapit,
Dalbinder Colman, and
Eric Barklis*
Vollum Institute and Department of Molecular Microbiology and Immunology, Oregon Health & Sciences University, Portland, Oregon
Received 27 September 2006/ Accepted 5 November 2006
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.
Published ahead of print on 15 November 2006.
Present address: Division of Biological Sciences, University of California at Davis, Davis, CA.
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