HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]

Publication Date:
2018-03-29
Publisher:
The American Society for Microbiology (ASM)
Print ISSN:
0022-538X
Electronic ISSN:
1098-5514
Topics:
Medicine
Published by:
http://www.asm.org/
_version_ 1839207982907260929
autor Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
beschreibung Induction of broadly cross-reactive antiviral humoral responses with the capacity to target globally diverse circulating strains is a key goal for HIV-1 immunogen design. A major gap in the field is the identification of diverse HIV-1 envelope antigens to evaluate vaccine regimens for binding antibody breadth. In this study, we define unique antigen panels to map HIV-1 vaccine-elicited antibody breadth and durability. Diverse HIV-1 envelope glycoproteins were selected based on genetic and geographic diversity to cover the global epidemic, with a focus on sexually acquired transmitted/founder viruses with a tier 2 neutralization phenotype. Unique antigenicity was determined by nonredundancy (Spearman correlation), and antigens were clustered using partitioning around medoids (PAM) to identify antigen diversity. Cross-validation demonstrated that the PAM method was better than selection by reactivity and random selection. Analysis of vaccine-elicited V1V2 binding antibody in longitudinal samples from the RV144 clinical trial revealed the striking heterogeneity among individual vaccinees in maintaining durable responses. These data support the idea that a major goal for vaccine development is to improve antibody levels, breadth, and durability at the population level. Elucidating the level and durability of vaccine-elicited binding antibody breadth needed for protection is critical for the development of a globally efficacious HIV vaccine. IMPORTANCE The path toward an efficacious HIV-1 vaccine will require characterization of vaccine-induced immunity that can recognize and target the highly genetically diverse virus envelope glycoproteins. Antibodies that target the envelope glycoproteins, including diverse sequences within the first and second hypervariable regions (V1V2) of gp120, were identified as correlates of risk for the one partially efficacious HIV-1 vaccine. To build upon this discovery, we experimentally and computationally evaluated humoral responses to define envelope glycoproteins representative of the antigenic diversity of HIV globally. These diverse envelope antigens distinguished binding antibody breadth and durability among vaccine candidates, thus providing insights for advancing the most promising HIV-1 vaccine candidates.
citation_standardnr 6220712
datenlieferant ipn_articles
feed_id 2375
feed_publisher The American Society for Microbiology (ASM)
feed_publisher_url http://www.asm.org/
insertion_date 2018-03-29
journaleissn 1098-5514
journalissn 0022-538X
publikationsjahr_anzeige 2018
publikationsjahr_facette 2018
publikationsjahr_intervall 7984:2015-2019
publikationsjahr_sort 2018
publisher The American Society for Microbiology (ASM)
quelle Journal of Virology
relation http://jvi.asm.org/cgi/content/short/92/8/e01843-17?rss=1
search_space articles
shingle_author_1 Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
shingle_author_2 Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
shingle_author_3 Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
shingle_author_4 Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
shingle_catch_all_1 HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
Induction of broadly cross-reactive antiviral humoral responses with the capacity to target globally diverse circulating strains is a key goal for HIV-1 immunogen design. A major gap in the field is the identification of diverse HIV-1 envelope antigens to evaluate vaccine regimens for binding antibody breadth. In this study, we define unique antigen panels to map HIV-1 vaccine-elicited antibody breadth and durability. Diverse HIV-1 envelope glycoproteins were selected based on genetic and geographic diversity to cover the global epidemic, with a focus on sexually acquired transmitted/founder viruses with a tier 2 neutralization phenotype. Unique antigenicity was determined by nonredundancy (Spearman correlation), and antigens were clustered using partitioning around medoids (PAM) to identify antigen diversity. Cross-validation demonstrated that the PAM method was better than selection by reactivity and random selection. Analysis of vaccine-elicited V1V2 binding antibody in longitudinal samples from the RV144 clinical trial revealed the striking heterogeneity among individual vaccinees in maintaining durable responses. These data support the idea that a major goal for vaccine development is to improve antibody levels, breadth, and durability at the population level. Elucidating the level and durability of vaccine-elicited binding antibody breadth needed for protection is critical for the development of a globally efficacious HIV vaccine. IMPORTANCE The path toward an efficacious HIV-1 vaccine will require characterization of vaccine-induced immunity that can recognize and target the highly genetically diverse virus envelope glycoproteins. Antibodies that target the envelope glycoproteins, including diverse sequences within the first and second hypervariable regions (V1V2) of gp120, were identified as correlates of risk for the one partially efficacious HIV-1 vaccine. To build upon this discovery, we experimentally and computationally evaluated humoral responses to define envelope glycoproteins representative of the antigenic diversity of HIV globally. These diverse envelope antigens distinguished binding antibody breadth and durability among vaccine candidates, thus providing insights for advancing the most promising HIV-1 vaccine candidates.
Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
The American Society for Microbiology (ASM)
0022-538X
0022538X
1098-5514
10985514
shingle_catch_all_2 HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
Induction of broadly cross-reactive antiviral humoral responses with the capacity to target globally diverse circulating strains is a key goal for HIV-1 immunogen design. A major gap in the field is the identification of diverse HIV-1 envelope antigens to evaluate vaccine regimens for binding antibody breadth. In this study, we define unique antigen panels to map HIV-1 vaccine-elicited antibody breadth and durability. Diverse HIV-1 envelope glycoproteins were selected based on genetic and geographic diversity to cover the global epidemic, with a focus on sexually acquired transmitted/founder viruses with a tier 2 neutralization phenotype. Unique antigenicity was determined by nonredundancy (Spearman correlation), and antigens were clustered using partitioning around medoids (PAM) to identify antigen diversity. Cross-validation demonstrated that the PAM method was better than selection by reactivity and random selection. Analysis of vaccine-elicited V1V2 binding antibody in longitudinal samples from the RV144 clinical trial revealed the striking heterogeneity among individual vaccinees in maintaining durable responses. These data support the idea that a major goal for vaccine development is to improve antibody levels, breadth, and durability at the population level. Elucidating the level and durability of vaccine-elicited binding antibody breadth needed for protection is critical for the development of a globally efficacious HIV vaccine. IMPORTANCE The path toward an efficacious HIV-1 vaccine will require characterization of vaccine-induced immunity that can recognize and target the highly genetically diverse virus envelope glycoproteins. Antibodies that target the envelope glycoproteins, including diverse sequences within the first and second hypervariable regions (V1V2) of gp120, were identified as correlates of risk for the one partially efficacious HIV-1 vaccine. To build upon this discovery, we experimentally and computationally evaluated humoral responses to define envelope glycoproteins representative of the antigenic diversity of HIV globally. These diverse envelope antigens distinguished binding antibody breadth and durability among vaccine candidates, thus providing insights for advancing the most promising HIV-1 vaccine candidates.
Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
The American Society for Microbiology (ASM)
0022-538X
0022538X
1098-5514
10985514
shingle_catch_all_3 HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
Induction of broadly cross-reactive antiviral humoral responses with the capacity to target globally diverse circulating strains is a key goal for HIV-1 immunogen design. A major gap in the field is the identification of diverse HIV-1 envelope antigens to evaluate vaccine regimens for binding antibody breadth. In this study, we define unique antigen panels to map HIV-1 vaccine-elicited antibody breadth and durability. Diverse HIV-1 envelope glycoproteins were selected based on genetic and geographic diversity to cover the global epidemic, with a focus on sexually acquired transmitted/founder viruses with a tier 2 neutralization phenotype. Unique antigenicity was determined by nonredundancy (Spearman correlation), and antigens were clustered using partitioning around medoids (PAM) to identify antigen diversity. Cross-validation demonstrated that the PAM method was better than selection by reactivity and random selection. Analysis of vaccine-elicited V1V2 binding antibody in longitudinal samples from the RV144 clinical trial revealed the striking heterogeneity among individual vaccinees in maintaining durable responses. These data support the idea that a major goal for vaccine development is to improve antibody levels, breadth, and durability at the population level. Elucidating the level and durability of vaccine-elicited binding antibody breadth needed for protection is critical for the development of a globally efficacious HIV vaccine. IMPORTANCE The path toward an efficacious HIV-1 vaccine will require characterization of vaccine-induced immunity that can recognize and target the highly genetically diverse virus envelope glycoproteins. Antibodies that target the envelope glycoproteins, including diverse sequences within the first and second hypervariable regions (V1V2) of gp120, were identified as correlates of risk for the one partially efficacious HIV-1 vaccine. To build upon this discovery, we experimentally and computationally evaluated humoral responses to define envelope glycoproteins representative of the antigenic diversity of HIV globally. These diverse envelope antigens distinguished binding antibody breadth and durability among vaccine candidates, thus providing insights for advancing the most promising HIV-1 vaccine candidates.
Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
The American Society for Microbiology (ASM)
0022-538X
0022538X
1098-5514
10985514
shingle_catch_all_4 HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
Induction of broadly cross-reactive antiviral humoral responses with the capacity to target globally diverse circulating strains is a key goal for HIV-1 immunogen design. A major gap in the field is the identification of diverse HIV-1 envelope antigens to evaluate vaccine regimens for binding antibody breadth. In this study, we define unique antigen panels to map HIV-1 vaccine-elicited antibody breadth and durability. Diverse HIV-1 envelope glycoproteins were selected based on genetic and geographic diversity to cover the global epidemic, with a focus on sexually acquired transmitted/founder viruses with a tier 2 neutralization phenotype. Unique antigenicity was determined by nonredundancy (Spearman correlation), and antigens were clustered using partitioning around medoids (PAM) to identify antigen diversity. Cross-validation demonstrated that the PAM method was better than selection by reactivity and random selection. Analysis of vaccine-elicited V1V2 binding antibody in longitudinal samples from the RV144 clinical trial revealed the striking heterogeneity among individual vaccinees in maintaining durable responses. These data support the idea that a major goal for vaccine development is to improve antibody levels, breadth, and durability at the population level. Elucidating the level and durability of vaccine-elicited binding antibody breadth needed for protection is critical for the development of a globally efficacious HIV vaccine. IMPORTANCE The path toward an efficacious HIV-1 vaccine will require characterization of vaccine-induced immunity that can recognize and target the highly genetically diverse virus envelope glycoproteins. Antibodies that target the envelope glycoproteins, including diverse sequences within the first and second hypervariable regions (V1V2) of gp120, were identified as correlates of risk for the one partially efficacious HIV-1 vaccine. To build upon this discovery, we experimentally and computationally evaluated humoral responses to define envelope glycoproteins representative of the antigenic diversity of HIV globally. These diverse envelope antigens distinguished binding antibody breadth and durability among vaccine candidates, thus providing insights for advancing the most promising HIV-1 vaccine candidates.
Yates, N. L., de; Camp, A. C., Korber, B. T., Liao, H.-X., Irene, C., Pinter, A., Peacock, J., Harris, L. J., Sawant, S., Hraber, P., Shen, X., Rerks-Ngarm, S., Pitisuttithum, P., Nitayapan, S., Berman, P. W., Robb, M. L., Pantaleo, G., Zolla-Pazner, S., Haynes, B. F., Alam, S. M., Montefiori, D. C., Tomaras, G. D.
The American Society for Microbiology (ASM)
0022-538X
0022538X
1098-5514
10985514
shingle_title_1 HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
shingle_title_2 HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
shingle_title_3 HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
shingle_title_4 HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
timestamp 2025-07-31T23:43:35.610Z
titel HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
titel_suche HIV-1 Envelope Glycoproteins from Diverse Clades Differentiate Antibody Responses and Durability among Vaccinees [Vaccines and Antiviral Agents]
topic WW-YZ
uid ipn_articles_6220712