Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved

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...

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Vydáno v:Immunity (Cambridge, Mass.) Ročník 41; číslo 6; s. 909
Hlavní autoři: Wiehe, Kevin, Easterhoff, David, Luo, Kan, Nicely, Nathan I, Bradley, Todd, Jaeger, Frederick H, Dennison, S Moses, Zhang, Ruijun, Lloyd, Krissey E, Stolarchuk, Christina, Parks, Robert, Sutherland, Laura L, Scearce, Richard M, Morris, Lynn, Kaewkungwal, Jaranit, Nitayaphan, Sorachai, Pitisuttithum, Punnee, Rerks-Ngarm, Supachai, Sinangil, Faruk, Phogat, Sanjay, Michael, Nelson L, Kim, Jerome H, Kelsoe, Garnett, Montefiori, David C, Tomaras, Georgia D, Bonsignori, Mattia, Santra, Sampa, Kepler, Thomas B, Alam, S Munir, Moody, M Anthony, Liao, Hua-Xin, Haynes, Barton F
Médium: Journal Article
Jazyk:angličtina
Vydáno: United States 18.12.2014
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ISSN:1097-4180, 1097-4180
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Abstract 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.
AbstractList 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.
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.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.
Author Parks, Robert
Nitayaphan, Sorachai
Haynes, Barton F
Morris, Lynn
Kelsoe, Garnett
Scearce, Richard M
Nicely, Nathan I
Rerks-Ngarm, Supachai
Zhang, Ruijun
Moody, M Anthony
Liao, Hua-Xin
Kaewkungwal, Jaranit
Kepler, Thomas B
Luo, Kan
Pitisuttithum, Punnee
Dennison, S Moses
Sutherland, Laura L
Kim, Jerome H
Phogat, Sanjay
Bonsignori, Mattia
Michael, Nelson L
Easterhoff, David
Lloyd, Krissey E
Jaeger, Frederick H
Santra, Sampa
Alam, S Munir
Tomaras, Georgia D
Wiehe, Kevin
Sinangil, Faruk
Montefiori, David C
Bradley, Todd
Stolarchuk, Christina
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  organization: Duke Human Vaccine Institute, Duke University School of Medicine, Durham, NC 27710, USA. Electronic address: kevin.wiehe@dm.duke.edu
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  organization: Global Solutions for Infectious Diseases, South San Francisco, CA 94080, USA
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  organization: US Military Research Program, Walter Reed Army Institute of Research, Silver Spring, MD 20910, USA
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  organization: Department of Microbiology, Boston University, Boston, MA 02118, USA
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Snippet 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...
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SubjectTerms AIDS Vaccines
Amino Acid Sequence
Animals
Antibodies, Viral - metabolism
Antibody Affinity - genetics
B-Lymphocytes - immunology
Cells, Cultured
Clinical Trials as Topic
Conserved Sequence - genetics
Epitope Mapping
Epitopes, B-Lymphocyte - genetics
Epitopes, B-Lymphocyte - immunology
Epitopes, B-Lymphocyte - metabolism
HIV Envelope Protein gp120 - genetics
HIV Envelope Protein gp120 - immunology
HIV Envelope Protein gp120 - metabolism
HIV Infections - immunology
HIV Infections - prevention & control
HIV-1 - immunology
Humans
Immunoglobulin Light Chains - metabolism
Macaca mulatta
Molecular Sequence Data
Mutation - genetics
Phylogeny
Protein Binding - genetics
Protein Engineering
Title Antibody light-chain-restricted recognition of the site of immune pressure in the RV144 HIV-1 vaccine trial is phylogenetically conserved
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