Abstract

Monomeric HIV-1 gp120 exterior envelope glycoproteins have failed to efficiently elicit neutralizing antibodies. We have therefore attempted to reconstitute the trimeric native g120 structure as solid phase proteoliposomes (PLs) containing HIV envelope glycoproteins (EnvPLs). This study characterizes the native trimeric structure of the glycoproteins in a lipid bilayer environment.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Intramural Research (Z01)
Project #
1Z01AI005025-03
Application #
6987286
Study Section
(SVS)
Project Start
Project End
Budget Start
Budget End
Support Year
3
Fiscal Year
2004
Total Cost
Indirect Cost

  Institution

Name
Niaid Extramural Activities
Department
Type
DUNS #
City
State
Country
United States
Zip Code

  Publications

Huang, Chih-Chin; Lam, Son N; Acharya, Priyamvada et al. (2007) Structures of the CCR5 N terminus and of a tyrosine-sulfated antibody with HIV-1 gp120 and CD4. Science 317:1930-4
Navratilova, Iva; Pancera, Marie; Wyatt, Richard T et al. (2006) A biosensor-based approach toward purification and crystallization of G protein-coupled receptors. Anal Biochem 353:278-83
Grundner, Christoph; Li, Yuxing; Louder, Mark et al. (2005) Analysis of the neutralizing antibody response elicited in rabbits by repeated inoculation with trimeric HIV-1 envelope glycoproteins. Virology 331:33-46
Grundner, Christoph; Pancera, Marie; Kang, Joung-Mo et al. (2004) Factors limiting the immunogenicity of HIV-1 gp120 envelope glycoproteins. Virology 330:233-48
Grundner, Christoph; Mirzabekov, Tajib; Sodroski, Joseph et al. (2002) Solid-phase proteoliposomes containing human immunodeficiency virus envelope glycoproteins. J Virol 76:3511-21