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J Gen Virol 77 (1996), 743-751; DOI 10.1099/0022-1317-77-4-743
© 1996 Society for General Microbiology

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Gag-Gag interactions in the C-terminal domain of human immunodeficiency virus type 1 p24 capsid antigen are essential for Gag particle assembly

Wei-Hong Zhang1, David J. Hockley2, Milan V. Nermut2, Yuko Morikawa3 and Ian M. Jones1,*

The1 Institute of Virology, Mansfield Road, Oxford OX1 3SR, UK
2 National Institute for Biological Standards and Control, South Mimms, Potters Bar EN6 3QG, UK
and3 Kitasato Institute, 5-9-1 Shirogane, Minato-ku, Tokyo 108, Japan

Seven internal deletions within the p24 domain of the human immunodeficiency virus type 1 Gag precursor have been assessed for their effect on Gag particle formation following their expression using recombinant baculoviruses. In addition, each deleted molecule was assessed for its ability to bind soluble p24 antigen in vitro. The mutants fell into three different phenotypic groups: (i) three mutants that had no effect on either p24 binding or Gag particle assembly, (ii) three mutants that abolished both features and (iii) one mutant that bound p24 in vitro but failed to assemble particles. Mutations that abolished both in vitro p24 binding and particle assembly mapped to the C terminus of p24 confirming this region as critical for virion assembly. We suggest the division of virion assembly into at least two distinct phases and suggest a model in which the critical sequences mapped to date are combined with available structural information.

* Author for correspondence. Fax +44 1865 59962. e-mail ijones@molbiol.ox.ac.uk

Received 18 September 1995; accepted 8 December 1995.


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