Abstract
SIMIAN immunodeficiency virus (SIV) is closely related to human immunodeficiency virus (HIV)1, their matrix antigens (MAs) sharing some 50% sequence identity. MA is a component of PrSSGag, the sole protein required for assembly of the virion shell2. MA targets Pr55 to the plasma membrane3, and facilitates incorporation of the virus envelope protein4 and assembly of the PrSSGag shell5. Cleavage of PrSS 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 entry6 and nuclear localization of the virion core7. Here we report the crystal structure of SIV MA. The molecule forms a trimer consistent with oligomerization in vitro8, the observed virion architecture9, and various biological properties of MA.
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Rao, Z., Belyaev, A., Fry, E. et al. Crystal structure of SIV matrix antigen and implications for virus assembly. Nature 378, 743–747 (1995). https://doi.org/10.1038/378743a0
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DOI: https://doi.org/10.1038/378743a0
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