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Title: Vaccine Induction of Antibodies against a Structurally Heterogeneous Site of Immune Pressure within HIV-1 Envelope Protein Variable Regions 1 and 2
Authors: Hua Xin Liao
Mattia Bonsignori
S. Munir Alam
Jason S. McLellan
Georgia D. Tomaras
M. Anthony Moody
Daniel M. Kozink
Kwan Ki Hwang
Xi Chen
Chun Yen Tsao
Pinghuang Liu
Xiaozhi Lu
Robert J. Parks
David C. Montefiori
Guido Ferrari
Justin Pollara
Mangala Rao
Kristina K. Peachman
Sampa Santra
Norman L. Letvin
Nicos Karasavvas
Zhi Yong Yang
Kaifan Dai
Marie Pancera
Jason Gorman
Kevin Wiehe
Nathan I. Nicely
Supachai Rerks-Ngarm
Sorachai Nitayaphan
Jaranit Kaewkungwal
Punnee Pitisuttithum
James Tartaglia
Faruk Sinangil
Jerome H. Kim
Nelson L. Michael
Thomas B. Kepler
Peter D. Kwong
John R. Mascola
Gary J. Nabel
Abraham Pinter
Susan Zolla-Pazner
Barton F. Haynes
Duke University School of Medicine
National Institutes of Health, Bethesda
Walter Reed Army Institute of Research
Harvard Medical School
Armed Forces Research Institute of Medical Sciences, Thailand
Thailand Ministry of Public Health
Mahidol University
Sanofi Pasteur
Global Solutions for Infectious Diseases
Boston University School of Medicine
Rutgers New Jersey Medical School
VA Medical Center
NYU School of Medicine
Keywords: Immunology and Microbiology;Medicine
Issue Date: 24-Jan-2013
Citation: Immunity. Vol.38, No.1 (2013), 176-186
Abstract: The RV144 HIV-1 trial of the canary pox vector (ALVAC-HIV) plus the gp120 AIDSVAX B/E vaccine demonstrated an estimated efficacy of 31%, which correlated directly with antibodies to HIV-1 envelope variable regions 1 and 2 (V1-V2). Genetic analysis of trial viruses revealed increased vaccine efficacy against viruses matching the vaccine strain at V2 residue 169. Here, we isolated four V2 monoclonal antibodies from RV144 vaccinees that recognize residue 169, neutralize laboratory-adapted HIV-1, and mediate killing of field-isolate HIV-1-infected CD4+T cells. Crystal structures of two of the V2 antibodies demonstrated that residue 169 can exist within divergent helical and loop conformations, which contrasted dramatically with the β strand conformation previously observed with a broadly neutralizing antibody PG9. Thus, RV144 vaccine-induced immune pressure appears to target a region that may be both sequence variable and structurally polymorphic. Variation may signal sites of HIV-1 envelope vulnerability, providing vaccine designers with new options. © 2013 Elsevier Inc.
ISSN: 10974180
Appears in Collections:Scopus 2011-2015

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