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 Center, R. J.
Right arrow Articles by Moss, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Center, R. J.
Right arrow Articles by Moss, B.

 Previous Article  |  Next Article 

Journal of Virology, August 2002, p. 7863-7867, Vol. 76, No. 15
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.15.7863-7867.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Oligomeric Structure of the Human Immunodeficiency Virus Type 1 Envelope Protein on the Virion Surface

Rob J. Center,1 Richard D. Leapman,2 Jacob Lebowitz,2 Larry O. Arthur,3 Patricia L. Earl,1 and Bernard Moss1*

Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases,,1 Division of Bioengineering and Physical Science, Office of Research Services, National Institutes of Health, Bethesda, Maryland 20892,2 AIDS Vaccine Program, Science Applications International Corporation—Frederick, National Cancer Institute at Frederick, Frederick, Maryland 217023

Received 26 February 2002/ Accepted 29 April 2002

The envelope protein (Env) of human immunodeficiency virus type 1 forms homo-oligomers in the endoplasmic reticulum. The oligomeric structure of Env is maintained after cleavage in a Golgi compartment and transport to the surfaces of infected cells, where incorporation into budding virions takes place. Here, we use biophysical techniques to assess the oligomeric valency of virion-associated Env prior to fusion activation. Virion-associated Env oligomers were stabilized by chemical cross-linking prior to detergent extraction and were purified by immunoaffinity chromatography. Gel filtration revealed a single predominant oligomeric species, and sedimentation equilibrium analysis-derived mass values indicated a trimeric structure. Determination of the masses of individual Env molecules by scanning transmission electron microscopy demonstrated that virion-associated Env was trimeric, and a triangular morphology was observed in 20 to 30% of the molecules. These results, which firmly establish the oligomeric structure of human immunodeficiency virus virion-associated Env, parallel those of our previous analysis of the simian immunodeficiency virus Env.


* Corresponding author. Mailing address: Laboratory of Viral Diseases, National Institutes of Health, Building 4, Room 229, 9000 Rockville Pike, Bethesda, MD 20892. Phone: (301) 496-9869. Fax: (301) 480-1147. E-mail: bmoss{at}nih.gov.


Journal of Virology, August 2002, p. 7863-7867, Vol. 76, No. 15
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.15.7863-7867.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Chien, M.-P., Jiang, S., Chang, D.-K. (2008). The function of coreceptor as a basis for the kinetic dissection of HIV type 1 envelope protein-mediated cell fusion. FASEB J. 22: 1179-1192 [Abstract] [Full Text]  
  • Ching, L. K., Vlachogiannis, G., Bosch, K. A., Stamatatos, L. (2008). The First Hypervariable Region of the gp120 Env Glycoprotein Defines the Neutralizing Susceptibility of Heterologous Human Immunodeficiency Virus Type 1 Isolates to Neutralizing Antibodies Elicited by the SF162gp140 Immunogen. J. Virol. 82: 949-956 [Abstract] [Full Text]  
  • Wexler-Cohen, Y., Shai, Y. (2007). Demonstrating the C-terminal boundary of the HIV 1 fusion conformation in a dynamic ongoing fusion process and implication for fusion inhibition. FASEB J. 21: 3677-3684 [Abstract] [Full Text]  
  • Shibata, J., Yoshimura, K., Honda, A., Koito, A., Murakami, T., Matsushita, S. (2007). Impact of V2 Mutations on Escape from a Potent Neutralizing Anti-V3 Monoclonal Antibody during In Vitro Selection of a Primary Human Immunodeficiency Virus Type 1 Isolate. J. Virol. 81: 3757-3768 [Abstract] [Full Text]  
  • Bloch, I., Quintana, F. J., Gerber, D., Cohen, T., Cohen, I. R., Shai, Y. (2007). T-Cell inactivation and immunosuppressive activity induced by HIV gp41 via novel interacting motif. FASEB J. 21: 393-401 [Abstract] [Full Text]  
  • Derby, N. R., Kraft, Z., Kan, E., Crooks, E. T., Barnett, S. W., Srivastava, I. K., Binley, J. M., Stamatatos, L. (2006). Antibody Responses Elicited in Macaques Immunized with Human Immunodeficiency Virus Type 1 (HIV-1) SF162-Derived gp140 Envelope Immunogens: Comparison with Those Elicited during Homologous Simian/Human Immunodeficiency Virus SHIVSF162P4 and Heterologous HIV-1 Infection.. J. Virol. 80: 8745-8762 [Abstract] [Full Text]  
  • Sackett, K., Wexler-Cohen, Y., Shai, Y. (2006). Characterization of the HIV N-terminal Fusion Peptide-containing Region in Context of Key gp41 Fusion Conformations. J. Biol. Chem. 281: 21755-21762 [Abstract] [Full Text]  
  • Yuan, W., Bazick, J., Sodroski, J. (2006). Characterization of the Multiple Conformational States of Free Monomeric and Trimeric Human Immunodeficiency Virus Envelope Glycoproteins after Fixation by Cross-Linker. J. Virol. 80: 6725-6737 [Abstract] [Full Text]  
  • Moore, P. L., Crooks, E. T., Porter, L., Zhu, P., Cayanan, C. S., Grise, H., Corcoran, P., Zwick, M. B., Franti, M., Morris, L., Roux, K. H., Burton, D. R., Binley, J. M. (2006). Nature of Nonfunctional Envelope Proteins on the Surface of Human Immunodeficiency Virus Type 1. J. Virol. 80: 2515-2528 [Abstract] [Full Text]  
  • Pancera, M., Lebowitz, J., Schon, A., Zhu, P., Freire, E., Kwong, P. D., Roux, K. H., Sodroski, J., Wyatt, R. (2005). Soluble Mimetics of Human Immunodeficiency Virus Type 1 Viral Spikes Produced by Replacement of the Native Trimerization Domain with a Heterologous Trimerization Motif: Characterization and Ligand Binding Analysis. J. Virol. 79: 9954-9969 [Abstract] [Full Text]  
  • Beddows, S., Schulke, N., Kirschner, M., Barnes, K., Franti, M., Michael, E., Ketas, T., Sanders, R. W., Maddon, P. J., Olson, W. C., Moore, J. P. (2005). Evaluating the Immunogenicity of a Disulfide-Stabilized, Cleaved, Trimeric Form of the Envelope Glycoprotein Complex of Human Immunodeficiency Virus Type 1. J. Virol. 79: 8812-8827 [Abstract] [Full Text]  
  • Wilson, K. A., Bar, S., Maerz, A. L., Alizon, M., Poumbourios, P. (2005). The Conserved Glycine-Rich Segment Linking the N-Terminal Fusion Peptide to the Coiled Coil of Human T-Cell Leukemia Virus Type 1 Transmembrane Glycoprotein gp21 Is a Determinant of Membrane Fusion Function. J. Virol. 79: 4533-4539 [Abstract] [Full Text]  
  • Lenz, O., Dittmar, M. T., Wagner, A., Ferko, B., Vorauer-Uhl, K., Stiegler, G., Weissenhorn, W. (2005). Trimeric Membrane-anchored gp41 Inhibits HIV Membrane Fusion. J. Biol. Chem. 280: 4095-4101 [Abstract] [Full Text]  
  • Yuste, E., Reeves, J. D., Doms, R. W., Desrosiers, R. C. (2004). Modulation of Env Content in Virions of Simian Immunodeficiency Virus: Correlation with Cell Surface Expression and Virion Infectivity. J. Virol. 78: 6775-6785 [Abstract] [Full Text]  
  • Shnaper, S., Sackett, K., Gallo, S. A., Blumenthal, R., Shai, Y. (2004). The C- and the N-terminal Regions of Glycoprotein 41 Ectodomain Fuse Membranes Enriched and Not Enriched with Cholesterol, Respectively. J. Biol. Chem. 279: 18526-18534 [Abstract] [Full Text]  
  • Center, R. J., Lebowitz, J., Leapman, R. D., Moss, B. (2004). Promoting Trimerization of Soluble Human Immunodeficiency Virus Type 1 (HIV-1) Env through the Use of HIV-1/Simian Immunodeficiency Virus Chimeras. J. Virol. 78: 2265-2276 [Abstract] [Full Text]  
  • Zhu, P., Chertova, E., Bess, J. Jr., Lifson, J. D., Arthur, L. O., Liu, J., Taylor, K. A., Roux, K. H. (2003). Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions. Proc. Natl. Acad. Sci. USA 100: 15812-15817 [Abstract] [Full Text]  
  • Poumbourios, P., Maerz, A. L., Drummer, H. E. (2003). Functional Evolution of the HIV-1 Envelope Glycoprotein 120 Association Site of Glycoprotein 41. J. Biol. Chem. 278: 42149-42160 [Abstract] [Full Text]  
  • Srivastava, I. K., Stamatatos, L., Kan, E., Vajdy, M., Lian, Y., Hilt, S., Martin, L., Vita, C., Zhu, P., Roux, K. H., Vojtech, L., C. Montefiori, D., Donnelly, J., Ulmer, J. B., Barnett, S. W. (2003). Purification, Characterization, and Immunogenicity of a Soluble Trimeric Envelope Protein Containing a Partial Deletion of the V2 Loop Derived from SF162, an R5-Tropic Human Immunodeficiency Virus Type 1 Isolate. J. Virol. 77: 11244-11259 [Abstract] [Full Text]  
  • Reeves, J. D., Gallo, S. A., Ahmad, N., Miamidian, J. L., Harvey, P. E., Sharron, M., Pohlmann, S., Sfakianos, J. N., Derdeyn, C. A., Blumenthal, R., Hunter, E., Doms, R. W. (2002). Sensitivity of HIV-1 to entry inhibitors correlates with envelope/coreceptor affinity, receptor density, and fusion kinetics. Proc. Natl. Acad. Sci. USA 99: 16249-16254 [Abstract] [Full Text]