A molecular switch required for retrovirus assembly participates in the hexagonal immature lattice

Judith M Phillips, Paul S Murray, Diana Murray, Volker M Vogt

Research output: Contribution to journalArticlepeer-review

28 Citations (Scopus)

Abstract

In the Rous sarcoma virus (RSV) Gag protein, the 25 amino-acid residues of the p10 domain immediately upstream of the CA domain are essential for immature particle formation. We performed systematic mutagenesis on this region and found excellent correlation between the amino-acid side chains required for in vitro assembly and those that participate in the p10-CA dimer interface in a previously described crystal structure. We introduced exogenous cysteine residues that were predicted to form disulphide bonds across the dimer interface. Upon oxidation of immature particles, a disulphide-linked Gag hexamer was formed, implying that p10 participates in and stabilizes the immature Gag hexamer. This is the first example of a critical interaction between two different Gag domains. Molecular modeling of the RSV immature hexamer indicates that the N-terminal domains of CA must expand relative to the murine leukaemia virus mature hexamer to accommodate the p10 contact; this expansion is strikingly similar to recent cryotomography results for immature human immunodeficiency virus particles.
Original languageEnglish
Pages (from-to)1411-20
Number of pages10
JournalThe EMBO journal
Volume27
Issue number9
DOIs
Publication statusPublished - 2008

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