Abstract

The HIV-1 envelope contains multiply overlapping (and redundant) mechanisms of humoral immune defense. These are only partially understood. We have used structure-based methods to define them further.

  Funding Agency

Agency
National Institute of Health (NIH)
Institute
National Institute of Allergy and Infectious Diseases (NIAID)
Type
Intramural Research (Z01)
Project #
1Z01AI005023-04
Application #
7174924
Study Section
(SBS)
Project Start
Project End
Budget Start
Budget End
Support Year
4
Fiscal Year
2005
Total Cost
Indirect Cost

  Institution

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

  Publications

Lin, George; Bertolotti-Ciarlet, Andrea; Haggarty, Beth et al. (2007) Replication-competent variants of human immunodeficiency virus type 2 lacking the V3 loop exhibit resistance to chemokine receptor antagonists. J Virol 81:9956-66
Xie, Hui; Ng, Danny; Savinov, Sergey N et al. (2007) Structure-activity relationships in the binding of chemically derivatized CD4 to gp120 from human immunodeficiency virus. J Med Chem 50:4898-908
Kwong, Peter D (2005) Human immunodeficiency virus: refolding the envelope. Nature 433:815-6
Koch, Markus; Pancera, Marie; Kwong, Peter D et al. (2003) Structure-based, targeted deglycosylation of HIV-1 gp120 and effects on neutralization sensitivity and antibody recognition. Virology 313:387-400
Labrijn, Aran F; Poignard, Pascal; Raja, Aarti et al. (2003) Access of antibody molecules to the conserved coreceptor binding site on glycoprotein gp120 is sterically restricted on primary human immunodeficiency virus type 1. J Virol 77:10557-65
Wei, Xiping; Decker, Julie M; Wang, Shuyi et al. (2003) Antibody neutralization and escape by HIV-1. Nature 422:307-12