Publication: Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved
Issued Date
2014-01-01
Resource Type
ISSN
10974180
10747613
10747613
Other identifier(s)
2-s2.0-84918548024
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Mahidol University
Rights Holder(s)
SCOPUS
Bibliographic Citation
Immunity. Vol.41, No.6 (2014), 909-918
Suggested Citation
Kevin Wiehe, David Easterhoff, Kan Luo, Nathan I. Nicely, Todd Bradley, Frederick H. Jaeger, S. Moses Dennison, Ruijun Zhang, Krissey E. Lloyd, Christina Stolarchuk, Robert Parks, Laura L. Sutherland, Richard M. Scearce, Lynn Morris, Jaranit Kaewkungwal, Sorachai Nitayaphan, Punnee Pitisuttithum, Supachai Rerks-Ngarm, Faruk Sinangil, Sanjay Phogat, Nelson L. Michael, Jerome H. Kim, Garnett Kelsoe, David C. Montefiori, Georgia D. Tomaras, Mattia Bonsignori, Sampa Santra, Thomas B. Kepler, S. Munir Alam, M. Anthony Moody, Hua Xin Liao, Barton F. Haynes Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved. Immunity. Vol.41, No.6 (2014), 909-918. doi:10.1016/j.immuni.2014.11.014 Retrieved from: https://repository.li.mahidol.ac.th/handle/20.500.14594/34111
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Title
Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved
Author(s)
Kevin Wiehe
David Easterhoff
Kan Luo
Nathan I. Nicely
Todd Bradley
Frederick H. Jaeger
S. Moses Dennison
Ruijun Zhang
Krissey E. Lloyd
Christina Stolarchuk
Robert Parks
Laura L. Sutherland
Richard M. Scearce
Lynn Morris
Jaranit Kaewkungwal
Sorachai Nitayaphan
Punnee Pitisuttithum
Supachai Rerks-Ngarm
Faruk Sinangil
Sanjay Phogat
Nelson L. Michael
Jerome H. Kim
Garnett Kelsoe
David C. Montefiori
Georgia D. Tomaras
Mattia Bonsignori
Sampa Santra
Thomas B. Kepler
S. Munir Alam
M. Anthony Moody
Hua Xin Liao
Barton F. Haynes
David Easterhoff
Kan Luo
Nathan I. Nicely
Todd Bradley
Frederick H. Jaeger
S. Moses Dennison
Ruijun Zhang
Krissey E. Lloyd
Christina Stolarchuk
Robert Parks
Laura L. Sutherland
Richard M. Scearce
Lynn Morris
Jaranit Kaewkungwal
Sorachai Nitayaphan
Punnee Pitisuttithum
Supachai Rerks-Ngarm
Faruk Sinangil
Sanjay Phogat
Nelson L. Michael
Jerome H. Kim
Garnett Kelsoe
David C. Montefiori
Georgia D. Tomaras
Mattia Bonsignori
Sampa Santra
Thomas B. Kepler
S. Munir Alam
M. Anthony Moody
Hua Xin Liao
Barton F. Haynes
Other Contributor(s)
Duke University School of Medicine
Centre for the AIDS Programme of Research in South Africa
Mahidol University
Armed Forces Research Institute of Medical Sciences, Thailand
Thailand Ministry of Public Health
Sanofi Pasteur Inc.
Global Solutions for Infectious Diseases
Walter Reed Army Institute of Research
Harvard University
Boston University
Centre for the AIDS Programme of Research in South Africa
Mahidol University
Armed Forces Research Institute of Medical Sciences, Thailand
Thailand Ministry of Public Health
Sanofi Pasteur Inc.
Global Solutions for Infectious Diseases
Walter Reed Army Institute of Research
Harvard University
Boston University
Abstract
© 2014 Elsevier Inc. In HIV-1, the ability to mount antibody responses to conserved, neutralizing epitopes is critical for protection. Here we have studied the light chain usage of human and rhesus macaque antibodies targeted to a dominant region of the HIV-1 envelope second variable (V2) region involving lysine (K) 169, the site of immune pressure in the RV144 vaccine efficacy trial. We found that humans and rhesus macaques used orthologous lambda variable gene segments encoding a glutamic acid-aspartic acid (ED) motif for K169 recognition. Structure determination of an unmutated ancestor antibody demonstrated that the V2 binding site was preconfigured for ED motif-mediated recognition prior to maturation. Thus, light chain usage for recognition of the site of immune pressure in the RV144 trial is highly conserved across species. These data indicate that the HIV-1 K169-recognizing ED motif has persisted over the diversification between rhesus macaques and humans, suggesting an evolutionary advantage of this antibody recognition mode.