Skip to content
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Menu
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Menu
Home
About Us
Resources
Profiles Metrics
Authors Directory
Institutions Directory
Top Authors
Top Institutions
Top Sponsors
AI Digest
Contact Us
Publication Details
AFRICAN RESEARCH NEXUS
SHINING A SPOTLIGHT ON AFRICAN RESEARCH
agricultural and biological sciences
Nature of nonfunctional envelope proteins on the surface of human immunodeficiency virus type 1
Journal of Virology, Volume 80, No. 5, Year 2006
Notification
URL copied to clipboard!
Description
Human immunodeficiency virus type 1 (HIV-1) neutralizing antibodies are thought be distinguished from nonneutralizing antibodies by their ability to recognize functional gp120/gp41 envelope glycoprotein (Env) trimers. The antibody responses induced by natural HIV-1 infection or by vaccine candidates tested to date consist largely of nonneutralizing antibodies. One might have expected a more vigorous neutralizing response, particularly against virus particles that bear functional trimers. The recent surprising observation that nonneutralizing antibodies can specifically capture HIV-1 may provide a clue relating to this paradox. Specifically, it was suggested that forms of Env, to which nonneutralizing antibodies can bind, exist on virus surfaces. Here, we present evidence that HIV-1 particles bear nonfunctional gp120/gp41 monomers and gp120-depleted gp41 stumps. Using a native electrophoresis band shift assay, we show that antibody-trimer binding predicts neutralization and that the nonfunctional forms of Env may account for virus capture by nonneutralizing antibodies. We hypothesize that these nonfunctional forms of Env on particle surfaces serve to divert the antibody response, helping the virus to evade neutralization. Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Authors & Co-Authors
Moore, Penny L.
United States, San Diego
Torrey Pines Institute for Molecular Studies
South Africa, Johannesburg
National Institute for Communicable Diseases
Crooks, Emma T.
United States, San Diego
Torrey Pines Institute for Molecular Studies
Porter, Lauren
United States, Tallahassee
Florida State University
Zhu, Ping
United States, Tallahassee
Florida State University
Cayanan, Charmagne S.
United States, San Diego
Scripps Research Institute
United States, San Diego
Kalypsys, Inc.
Grise, Henry
United States, Tallahassee
Florida State University
Corcoran, Paul
United States, San Diego
Torrey Pines Institute for Molecular Studies
Zwick, Michael B.
United States, San Diego
Scripps Research Institute
Franti, Michael
United States, Bedford
Lantheus
Morris, Lynn
South Africa, Johannesburg
National Institute for Communicable Diseases
Roux, Kenneth H.
United States, Tallahassee
Florida State University
Burton, Dennis Raymond
United States, San Diego
Scripps Research Institute
Binley, James M.
United States, San Diego
Torrey Pines Institute for Molecular Studies
United States, San Diego
Scripps Research Institute
Statistics
Citations: 347
Authors: 13
Affiliations: 6
Identifiers
Doi:
10.1128/JVI.80.5.2515-2528.2006
ISSN:
0022538X
Research Areas
Infectious Diseases