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 Vu, H. M.
Right arrow Articles by Spicer, L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vu, H. M.
Right arrow Articles by Spicer, L.

 Previous Article  |  Next Article 

Journal of Virology, January 1999, p. 746-750, Vol. 73, No. 1
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Nuclear Magnetic Resonance Analysis of Solution Conformations in C4-V3 Hybrid Peptides Derived from Human Immunodeficiency Virus (HIV) Type 1 gp120: Relation to Specificity of Peptide-Induced Anti-HIV Neutralizing Antibodies

Hai M. Vu,1,2 David Myers,1,2 Robert de Lorimier,1,2 Thomas J. Matthews,3,4,5 M. Anthony Moody,3,4,5 Craig Heinly,3,4,5 Jose V. Torres,6,7 Barton F. Haynes,3,4,5 and Leonard Spicer1,2,*

Departments of Biochemistry,1 Immunology,3 Medicine,4 Surgery,5 and Radiology,2 Duke University Medical Center, Durham, North Carolina 27710, and The Primate Center6 and Department of Medical Pathology,7 University of California---Davis, Davis, California 95616

Received 28 April 1998/Accepted 24 September 1998

Immunogenic peptides containing epitopes of the gp120 C4 and V3 regions from human immunodeficiency virus strains MN and EV91 have been studied by nuclear magnetic resonance and molecular modeling and used as immunogens in rhesus monkeys. The results, combined with those for other peptides, suggest a correlation between solution conformation and immunologic cross-reactivity.

* Corresponding author. Mailing address: Department of Biochemistry, Box 3711, Duke University Medical Center, Durham, NC 27710. Phone: (919) 684-4327. Fax: (919) 684-8885. E-mail: spicer{at}trublu.biochem.duke.edu.

Journal of Virology, January 1999, p. 746-750, Vol. 73, No. 1
0022-538X/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Stanfield, R. L., Gorny, M. K., Zolla-Pazner, S., Wilson, I. A. (2006). Crystal Structures of Human Immunodeficiency Virus Type 1 (HIV-1) Neutralizing Antibody 2219 in Complex with Three Different V3 Peptides Reveal a New Binding Mode for HIV-1 Cross-Reactivity.. J. Virol. 80: 6093-6105 [Abstract] [Full Text]  
  • Liao, H.-X., Etemad-Moghadam, B., Montefiori, D. C., Sun, Y., Sodroski, J., Scearce, R. M., Doms, R. W., Thomasch, J. R., Robinson, S., Letvin, N. L., Haynes, B. F. (2000). Induction of Antibodies in Guinea Pigs and Rhesus Monkeys against the Human Immunodeficiency Virus Type 1 Envelope: Neutralization of Nonpathogenic and Pathogenic Primary Isolate Simian/Human Immunodeficiency Virus Strains. J. Virol. 74: 254-263 [Abstract] [Full Text]  
  • Wu, G., MacKenzie, R., Durda, P. J., Tsang, P. (2000). The Binding of a Glycoprotein 120 V3 Loop Peptide to HIV-1 Neutralizing Antibodies. STRUCTURAL IMPLICATIONS. J. Biol. Chem. 275: 36645-36652 [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»