This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Garnier, L.
Right arrow Articles by Wills, J. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Garnier, L.
Right arrow Articles by Wills, J. W.

 Previous Article  |  Next Article 

J Virol, June 1998, p. 4667-4677, Vol. 72, No. 6
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Particle Size Determinants in the Human Immunodeficiency Virus Type 1 Gag Protein

Laurence Garnier,1 Lee Ratner,2 Benjamin Rovinski,3 Shi-Xian Cao,3 and John W. Wills1,*

Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey, Pennsylvania 170331; Departments of Medicine, Pathology, and Molecular Microbiology, Washington University, St. Louis, Missouri 631102; and Department of Molecular Virology, Pasteur Merieux Connaught Canada, North York, Ontario M2R 3T4, Canada3

Received 19 November 1997/Accepted 10 February 1998

The retroviral Gag protein plays the central role in the assembly process and can form membrane-enclosed, virus-like particles in the absence of any other viral products. These particles are similar to authentic virions in density and size. Three small domains of the human immunodeficiency virus type 1 (HIV-1) Gag protein have been previously identified as being important for budding. Regions that lie outside these domains can be deleted without any effect on particle release or density. However, the regions of Gag that control the size of HIV-1 particles are less well understood. In the case of Rous sarcoma virus (RSV), the size determinant maps to the CA (capsid) and adjacent spacer sequences within Gag, but systematic mapping of the HIV Gag protein has not been reported. To locate the size determinants of HIV-1, we analyzed a large collection of Gag mutants. To our surprise, all mutants with defects in the MA (matrix), CA, and the N-terminal part of NC (nucleocapsid) sequences produced dense particles of normal size, suggesting that oncoviruses (RSV) and lentiviruses (HIV-1) have different size-controlling elements. The most important region found to be critical for determining HIV-1 particle size is the p6 sequence. Particles lacking all or small parts of p6 were uniform in size distribution but very large as measured by rate zonal gradients. Further evidence for this novel function of p6 was obtained by placing this sequence at the C terminus of RSV CA mutants that produce heterogeneously sized particles. We found that the RSV-p6 chimeras produced normally sized particles. Thus, we present evidence that the entire p6 sequence plays a role in determining the size of a retroviral particle.

* Corresponding author. Mailing address: Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, 500 University Dr., P.O. Box 850, Hershey, PA 17033. Phone: (717) 531-3528. Fax: (717) 531-6522. E-mail: jwills{at}psu.edu.

J Virol, June 1998, p. 4667-4677, Vol. 72, No. 6
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Fossen, T., Wray, V., Bruns, K., Rachmat, J., Henklein, P., Tessmer, U., Maczurek, A., Klinger, P., Schubert, U. (2005). Solution Structure of the Human Immunodeficiency Virus Type 1 p6 Protein. J. Biol. Chem. 280: 42515-42527 [Abstract] [Full Text]  
  • Ako-Adjei, D., Johnson, M. C., Vogt, V. M. (2005). The Retroviral Capsid Domain Dictates Virion Size, Morphology, and Coassembly of Gag into Virus-Like Particles. J. Virol. 79: 13463-13472 [Abstract] [Full Text]  
  • Hemonnot, B., Cartier, C., Gay, B., Rebuffat, S., Bardy, M., Devaux, C., Boyer, V., Briant, L. (2004). The Host Cell MAP Kinase ERK-2 Regulates Viral Assembly and Release by Phosphorylating the p6gag Protein of HIV-1. J. Biol. Chem. 279: 32426-32434 [Abstract] [Full Text]  
  • Bleiber, G., Peters, S., Martinez, R., Cmarko, D., Meylan, P., Telenti, A. (2004). The central region of human immunodeficiency virus type 1 p6 protein (Gag residues S14-I31) is dispensable for the virus in vitro. J. Gen. Virol. 85: 921-927 [Abstract] [Full Text]  
  • Wang, S.-W., Noonan, K., Aldovini, A. (2004). Nucleocapsid-RNA Interactions Are Essential to Structural Stability but Not to Assembly of Retroviruses. J. Virol. 78: 716-723 [Abstract] [Full Text]  
  • Cen, S., Niu, M., Saadatmand, J., Guo, F., Huang, Y., Nabel, G. J., Kleiman, L. (2004). Incorporation of Pol into Human Immunodeficiency Virus Type 1 Gag Virus-Like Particles Occurs Independently of the Upstream Gag Domain in Gag-Pol. J. Virol. 78: 1042-1049 [Abstract] [Full Text]  
  • Javanbakht, H., Halwani, R., Cen, S., Saadatmand, J., Musier-Forsyth, K., Gottlinger, H., Kleiman, L. (2003). The Interaction between HIV-1 Gag and Human Lysyl-tRNA Synthetase during Viral Assembly. J. Biol. Chem. 278: 27644-27651 [Abstract] [Full Text]  
  • Halwani, R., Khorchid, A., Cen, S., Kleiman, L. (2003). Rapid Localization of Gag/GagPol Complexes to Detergent-Resistant Membrane during the Assembly of Human Immunodeficiency Virus Type 1. J. Virol. 77: 3973-3984 [Abstract] [Full Text]  
  • Wang, S.-W., Aldovini, A. (2002). RNA Incorporation Is Critical for Retroviral Particle Integrity after Cell Membrane Assembly of Gag Complexes. J. Virol. 76: 11853-11865 [Abstract] [Full Text]  
  • Freed, E. O. (2002). Viral Late Domains. J. Virol. 76: 4679-4687 [Full Text]  
  • Khorchid, A., Halwani, R., Wainberg, M. A., Kleiman, L. (2002). Role of RNA in Facilitating Gag/Gag-Pol Interaction. J. Virol. 76: 4131-4137 [Abstract] [Full Text]  
  • Demirov, D. G., Orenstein, J. M., Freed, E. O. (2002). The Late Domain of Human Immunodeficiency Virus Type 1 p6 Promotes Virus Release in a Cell Type-Dependent Manner. J. Virol. 76: 105-117 [Abstract] [Full Text]  
  • Chen, C., Li, F., Montelaro, R. C. (2001). Functional Roles of Equine Infectious Anemia Virus Gag p9 in Viral Budding and Infection. J. Virol. 75: 9762-9770 [Abstract] [Full Text]  
  • Lindwasser, O. W., Resh, M. D. (2001). Multimerization of Human Immunodeficiency Virus Type 1 Gag Promotes Its Localization to Barges, Raft-Like Membrane Microdomains. J. Virol. 75: 7913-7924 [Abstract] [Full Text]  
  • Bowzard, J. B., Wills, J. W., Craven, R. C. (2001). Second-Site Suppressors of Rous Sarcoma Virus CA Mutations: Evidence for Interdomain Interactions. J. Virol. 75: 6850-6856 [Abstract] [Full Text]  
  • Rayne, F., Bouamr, F., Lalanne, J., Mamoun, R. Z. (2001). The NH2-Terminal Domain of the Human T-Cell Leukemia Virus Type 1 Capsid Protein Is Involved in Particle Formation. J. Virol. 75: 5277-5287 [Abstract] [Full Text]  
  • Wilk, T., Gross, I., Gowen, B. E., Rutten, T., de Haas, F., Welker, R., Kräusslich, H.-G., Boulanger, P., Fuller, S. D. (2001). Organization of Immature Human Immunodeficiency Virus Type 1. J. Virol. 75: 759-771 [Abstract] [Full Text]  
  • Yovandich, J. L., Chertova, E. N., Kane, B. P., Gagliardi, T. D., Bess, J. W. Jr., Sowder, R. C. II, Henderson, L. E., Gorelick, R. J. (2001). Alteration of Zinc-Binding Residues of Simian Immunodeficiency Virus p8NC Results in Subtle Differences in Gag Processing and Virion Maturation Associated with Degradative Loss of Mutant NC. J. Virol. 75: 115-124 [Abstract] [Full Text]  
  • Patnaik, A., Chau, V., Wills, J. W. (2000). Ubiquitin is part of the retrovirus budding machinery. Proc. Natl. Acad. Sci. USA 97: 13069-13074 [Abstract] [Full Text]  
  • Rumlova-Klikova, M., Hunter, E., Nermut, M. V., Pichova, I., Ruml, T. (2000). Analysis of Mason-Pfizer Monkey Virus Gag Domains Required for Capsid Assembly in Bacteria: Role of the N-Terminal Proline Residue of CA in Directing Particle Shape. J. Virol. 74: 8452-8459 [Abstract] [Full Text]  
  • Accola, M. A., Strack, B., Göttlinger, H. G. (2000). Efficient Particle Production by Minimal Gag Constructs Which Retain the Carboxy-Terminal Domain of Human Immunodeficiency Virus Type 1 Capsid-p2 and a Late Assembly Domain. J. Virol. 74: 5395-5402 [Abstract] [Full Text]  
  • Vogt, V. M., Simon, M. N. (1999). Mass Determination of Rous Sarcoma Virus Virions by Scanning Transmission Electron Microscopy. J. Virol. 73: 7050-7055 [Abstract] [Full Text]  
  • Dettenhofer, M., Yu, X.-F. (1999). Proline Residues in Human Immunodeficiency Virus Type 1 p6Gag Exert a Cell Type-Dependent Effect on Viral Replication and Virion Incorporation of Pol Proteins. J. Virol. 73: 4696-4704 [Abstract] [Full Text]  
  • Bennett, R. P., Wills, J. W. (1999). Conditions for Copackaging Rous Sarcoma Virus and Murine Leukemia Virus Gag Proteins during Retroviral Budding. J. Virol. 73: 2045-2051 [Abstract] [Full Text]  
  • Garnier, L., Parent, L. J., Rovinski, B., Cao, S.-X., Wills, J. W. (1999). Identification of Retroviral Late Domains as Determinants of Particle Size. J. Virol. 73: 2309-2320 [Abstract] [Full Text]  
  • Ott, D. E., Chertova, E. N., Busch, L. K., Coren, L. V., Gagliardi, T. D., Johnson, D. G. (1999). Mutational Analysis of the Hydrophobic Tail of the Human Immunodeficiency Virus Type 1 p6Gag Protein Produces a Mutant That Fails To Package Its Envelope Protein. J. Virol. 73: 19-28 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»