Crystal structure of SIV matrix antigen and implications for virus assembly

Rao, Zihe; Belyaev, Alexander S.; Fry, Elizabeth; Roy, Polly; Jones, Ian M.; Stuart, David I.

doi:10.1038/378743a0

Cited by 183HIV Research and TreatmentEnzyme Structure and FunctionT-cell and Retrovirus Studies

Crystal structure of SIV matrix antigen and implications for virus assembly

Rao, Zihe, Belyaev, Alexander S., Fry, Elizabeth, Roy, Polly, Jones, Ian M., Stuart, David I.·1995·Nature

DOI 10.1038/378743a0

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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.

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Many other retroviruses, including SIV, EIAV, HTLV-2, BLV, and MPMV, exhibit MA trimers despite their highly varied sequences.
“Many other retroviruses, including SIV, EIAV, HTLV-2, BLV, and MPMV, exhibit MA trimers despite their highly varied sequences.”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Rao et al. 1995
Mutations in the trimer interface, at least in MPMV, compromise CA assembly.
“Mutations in the trimer interface, at least in the case of MPMV, have been shown to compromise CA assembly”
From Beyond reverse transcription: molecular mechanisms and emerging paradigms in retroviral replication (2026) · cites this paper as Rao et al. 1995

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Authors: Rao, Z., Belyaev, A. S., Fry, E., Roy, P., Jones, I. M., & Stuart, D. I.
Affiliations: University of Oxford (GB)
University of Alabama at Birmingham (US)
Natural Environment Research Council (GB)
ORCID: Rao, Zihe
Belyaev, Alexander S.
Fry, Elizabeth
Roy, Polly
Jones, Ian M.
Stuart, David I.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1995-12
Volume: 378
Issue: 6558
Pages: 743-747
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/378743a0
OpenAlex: W2068340726
Cited by: 183
References: 27
Citations by year: 2025: 1 · 2024: 3 · 2020: 5 · 2019: 4 · 2018: 4 · 2017: 1 · 2016: 1 · 2015: 8 · 2014: 6 · 2013: 7 · 2012: 5
FWCI: 4.98
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Virology › HIV Research and Treatment
Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Life Sciences › Immunology and Microbiology › Immunology › T-cell and Retrovirus Studies
Keywords: simian immunodeficiency virus, matrix protein, Pr55gag, protein crystal structure, trimers, viral assembly, primate retroviruses
MeSH terms: Amino Acid Sequence, Antigens, Viral, Computer Graphics, Models, Molecular, Molecular Sequence Data, Protein Conformation, Viral Matrix Proteins, Virus Replication, Simian Immunodeficiency Virus, Gene Products, gag, Crystallography, X-Ray

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Crystal structure of SIV matrix antigen and implications for virus assembly

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