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Journal of Virology, January 2001, p. 759-771, Vol. 75, No. 2
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.2.759-771.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Organization of Immature Human Immunodeficiency Virus Type 1

Thomas Wilk,1,2 Ingolf Gross,3 Brent E. Gowen,1,2 Twan Rutten,1 Felix de Haas,1 Reinhold Welker,3 Hans-Georg Kräusslich,3,4 Pierre Boulanger,5 and Stephen D. Fuller1,2,*

The Structural Biology Programme, European Molecular Biology Laboratory, D69012 Heidelberg,1 Heinrich-Pette-Institut, Stiftung des Privaten Rechts, D-20251 Hamburg,3 and Abteilung Virologie, Universität Heidelberg, 69120 Heidelberg,4 Federal Republic of Germany; Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, Headington, Oxford OX3 7BN, England2; and Laboratoire de Virologie et Pathogenése Virale, CNRS UMR 5537, Faculté de Médecine RTH Laennec, Lyon 693732 Cedex 08, France5

Received 23 May 2000/Accepted 4 October 2000

Immature retrovirus particles contain radially arranged Gag polyproteins in which the N termini lie at the membrane and the C termini extend toward the particle's center. We related image features to the polyprotein domain structure by combining mutagenesis with cryoelectron microscopy and image analysis. The matrix (MA) domain appears as a thin layer tightly associated with the inner face of the viral membrane, separated from the capsid (CA) layer by a low-density region corresponding to its C terminus. Deletion of the entire p6 domain has no effect on the width or spacing of the density layers, suggesting that p6 is not ordered in immature human immunodeficiency virus type 1 (HIV-1). In vitro assembly of a recombinant Gag polyprotein containing only capsid (CA) and nucleocapsid (NC) domains results in the formation of nonenveloped spherical particles which display two layers with density matching that of the CA-NC portion of immature HIV-1 Gag particles. Authentic, immature HIV-1 displays additional surface features and an increased density between the lipid bilayers which reflect the presence of gp41. The other internal features match those of virus-like particles.

* Corresponding author. Mailing address: Division of Structural Biology, The Wellcome Trust Centre for Human Genetics, Roosevelt Dr., Headington, Oxford OX3 7BN, England. Phone: 44-1865-287546. Fax: 44-1865-287547. E-mail: stephen.fuller{at}strubi.ox.ac.uk.

Journal of Virology, January 2001, p. 759-771, Vol. 75, No. 2
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.2.759-771.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.