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PMID: 7501025 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Crystal structure of SIV matrix antigen and implications for virus assembly.

Nature ·Vol. 378 ·No. 6558 ·1995-12-14 ·Pages 743-7

Rao Z, Belyaev AS, Fry E, Roy P, Jones IM, Stuart DI

Abstract

Simian immunodeficiency virus (SIV) is closely related to human immunodeficiency virus (HIV), their matrix antigens (MAs) sharing some 50% sequence identity. MA is a component of Pr55Gag, the sole protein required for assembly of the virion shell. MA targets Pr55 to the plasma membrane, and facilitates incorporation of the virus envelope protein and assembly of the Pr55Gag shell. Cleavage of Pr55 by the viral protease produces the mature protein of relative molecular mass 17-18K, which underlies the host-derived membrane and is important in both virus entry and nuclear localization of the virion core. Here we report the crystal structure of SIV MA. The molecule forms a trimer consistent with oligomerization in vitro, the observed virion architecture, and various biological properties of MA.

MeSH Terms
Amino Acid Sequence Antigens, Viral/chemistry,physiology Computer Graphics Crystallography, X-Ray Gene Products, gag/chemistry,physiology Models, Molecular Molecular Sequence Data Protein Conformation Simian Immunodeficiency Virus/chemistry,physiology Viral Matrix Proteins/chemistry,physiology Virus Replication
Chemicals
Antigens, Viral Gene Products, gag Viral Matrix Proteins simian immunodeficiency virus matrix protein p17
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Rao Z
Laboratory of Molecular Biophysics, Oxford, UK.
Belyaev A S
Fry E
Roy P
Jones I M
Stuart D I
Article Info
Journal
Nature
Abbr.
Nature
ISSN
0028-0836
Published
1995-12-14
Pages
743-7
Language
English
Region
England
NLM ID
0410462
Subset
IM
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