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Journal of Virology, September 1998, p. 7659-7663, Vol. 72, No. 9
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Detection of a Trimeric Human Immunodeficiency Virus Type 1 Gag Intermediate Is Dependent on Sequences in the Matrix Protein, p17

Yuko Morikawa,1,* Wei-Hong Zhang,2 David J. Hockley,3 Milan V. Nermut,3 and Ian M. Jones2,*

The Kitasato Institute, Minato-ku, Tokyo 108, Japan,1 and National Institute for Biological Standards and Control, South Mimms, Hertsfordshire EN6 3QG,3 and NERC Institute of Virology, Oxford OX1 3SR,2 United Kingdom

Received 9 February 1998/Accepted 20 May 1998

Previous studies have shown that single amino acid changes in the amino-terminal matrix (MA) domain, p17, of the human immunodeficiency virus type 1 Gag precursor Pr55, can abrogate virion particle assembly. In the three-dimensional structure of MA such mutations lie in a single helix spanning residues 54 to 68, suggesting a key role for this helix in the assembly process. The fundamental nature of this involvement, however, remains poorly understood. In the present study, the essential features of the MA helix required for virus assembly have been investigated through the analysis of a further 15 site-directed mutants. With previous mutants that failed to assemble, residues mapped as critical for assembly were all located on the hydrophobic face of the helix and had a key role in stabilizing the trimeric interface. This implies a role for the MA trimer in virus assembly. We support this interpretation by showing that purified MA is trimeric in solution and that mutations that prevent virus assembly also prevent trimerization. Trimerization in solution was also a property of a larger MA-capsid (CA) Gag molecule, while under the same conditions CA only was a monomer. These data suggest that Gag trimerization driven by the MA domain is an intermediate stage in normal virion assembly and that it relies, in turn, on an MA conformation dependent on the hydrophobic core of the molecule.

* Corresponding author. Mailing address for Yuko Morikawa: The Kitasato Institute, 5-9-1 Shirokane, Minato-ku, Tokyo 108, Japan. Phone: (81) 3 5791 6129. Fax: (81) 3 5791 6120. E-mail: ymorikawa{at}kitasato.or.jp. Mailing address for Ian M. Jones: NERC Institute of Virology, Mansfield Road, Oxford OX1 3SR, United Kingdom. Phone: (44) 1865 281635. Fax: (44) 1865 281696. E-mail: imj{at}mail.nox.ac.uk.

Journal of Virology, September 1998, p. 7659-7663, Vol. 72, No. 9
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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