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J Gen Virol 75 (1994), 2985-2997; DOI 10.1099/0022-1317-75-11-2985
© 1994 Society for General Microbiology

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Comparative Morphology of Gag Protein Structures Produced by Mutants of the gag Gene of Human Immunodeficiency Virus Type 1

D. J. Hockley1, M. V. Nermut1, C. Grief1, J. B. M. Jowett2,{dagger} and I. M. Jones2

1 Electron Microscopy and Photography Section, National Institute for Biological Standards and Control, South Mimms, Potters Bar, Hertfordshire EN6 3QG
and2 Natural Environment Research Council, Institute of Virology and Environmental Microbiology, Mansfield Road, Oxford OX1 3SR, U.K.

Six mutants that differ in the extent of their carboxyterminal sequences and two deletion mutants of the gag gene of HIV-1 have been characterized morphologically following their expression in Spodoptera frugiperda cells using recombinant baculoviruses. Electron microscopy has revealed distinct morphological forms of the Gag protein that can be classified as either (i) particulate, three-dimensional, spherical or tubular shells or (ii) non-particulate, two-dimensional, flat, curved or convoluted sheets. Progressive truncation of the carboxy terminus of Gag was accompanied by changes in the morphology and formation of spherical particles from predominantly C-type assembly and budding at the plasma membrane, through B-type intracytoplasmic assembly, to A-type assembly with budding mainly into cytoplasmic vacuoles. Deletions within the Pr24 CA domain of Gag abolished particle formation but retained association of the protein with the plasma membrane. All of the observed morphologies of the mutant Gag proteins could be accommodated within an icosahedral model for the organization of spherical particles and a basic hexagonal arrangement of assembled Gag protein monomers.

{dagger} Present address: Department of Microbiology, UCLA School of Medicine, Los Angeles, California 90073, U.S.A.

Received 4 February 1994; accepted 6 July 1994.


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