A potent broadly neutralizing human RSV antibody targets conserved site IV of the fusion glycoprotein

Respiratory syncytial virus (RSV) infection is the leading cause of hospitalization and infant mortality under six months of age worldwide; therefore, the prevention of RSV infection in all infants represents a significant unmet medical need. Here we report the isolation of a potent and broadly neut...

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Autores principales: Tang, Aimin, Chen, Zhifeng, Cox, Kara S., Su, Hua-Poo, Callahan, Cheryl, Fridman, Arthur, Zhang, Lan, Patel, Sangita B., Cejas, Pedro J., Swoyer, Ryan, Touch, Sinoeun, Citron, Michael P., Govindarajan, Dhanasekaran, Luo, Bin, Eddins, Michael, Reid, John C., Soisson, Stephen M., Galli, Jennifer, Wang, Dai, Wen, Zhiyun, Heidecker, Gwendolyn J., Casimiro, Danilo R., DiStefano, Daniel J., Vora, Kalpit A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2019
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6742648/
https://www.ncbi.nlm.nih.gov/pubmed/31515478
http://dx.doi.org/10.1038/s41467-019-12137-1
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author Tang, Aimin
Chen, Zhifeng
Cox, Kara S.
Su, Hua-Poo
Callahan, Cheryl
Fridman, Arthur
Zhang, Lan
Patel, Sangita B.
Cejas, Pedro J.
Swoyer, Ryan
Touch, Sinoeun
Citron, Michael P.
Govindarajan, Dhanasekaran
Luo, Bin
Eddins, Michael
Reid, John C.
Soisson, Stephen M.
Galli, Jennifer
Wang, Dai
Wen, Zhiyun
Heidecker, Gwendolyn J.
Casimiro, Danilo R.
DiStefano, Daniel J.
Vora, Kalpit A.
author_facet Tang, Aimin
Chen, Zhifeng
Cox, Kara S.
Su, Hua-Poo
Callahan, Cheryl
Fridman, Arthur
Zhang, Lan
Patel, Sangita B.
Cejas, Pedro J.
Swoyer, Ryan
Touch, Sinoeun
Citron, Michael P.
Govindarajan, Dhanasekaran
Luo, Bin
Eddins, Michael
Reid, John C.
Soisson, Stephen M.
Galli, Jennifer
Wang, Dai
Wen, Zhiyun
Heidecker, Gwendolyn J.
Casimiro, Danilo R.
DiStefano, Daniel J.
Vora, Kalpit A.
author_sort Tang, Aimin
collection PubMed
description Respiratory syncytial virus (RSV) infection is the leading cause of hospitalization and infant mortality under six months of age worldwide; therefore, the prevention of RSV infection in all infants represents a significant unmet medical need. Here we report the isolation of a potent and broadly neutralizing RSV monoclonal antibody derived from a human memory B-cell. This antibody, RB1, is equipotent on RSV A and B subtypes, potently neutralizes a diverse panel of clinical isolates in vitro and demonstrates in vivo protection. It binds to a highly conserved epitope in antigenic site IV of the RSV fusion glycoprotein. RB1 is the parental antibody to MK-1654 which is currently in clinical development for the prevention of RSV infection in infants.
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spelling pubmed-67426482019-09-16 A potent broadly neutralizing human RSV antibody targets conserved site IV of the fusion glycoprotein Tang, Aimin Chen, Zhifeng Cox, Kara S. Su, Hua-Poo Callahan, Cheryl Fridman, Arthur Zhang, Lan Patel, Sangita B. Cejas, Pedro J. Swoyer, Ryan Touch, Sinoeun Citron, Michael P. Govindarajan, Dhanasekaran Luo, Bin Eddins, Michael Reid, John C. Soisson, Stephen M. Galli, Jennifer Wang, Dai Wen, Zhiyun Heidecker, Gwendolyn J. Casimiro, Danilo R. DiStefano, Daniel J. Vora, Kalpit A. Nat Commun Article Respiratory syncytial virus (RSV) infection is the leading cause of hospitalization and infant mortality under six months of age worldwide; therefore, the prevention of RSV infection in all infants represents a significant unmet medical need. Here we report the isolation of a potent and broadly neutralizing RSV monoclonal antibody derived from a human memory B-cell. This antibody, RB1, is equipotent on RSV A and B subtypes, potently neutralizes a diverse panel of clinical isolates in vitro and demonstrates in vivo protection. It binds to a highly conserved epitope in antigenic site IV of the RSV fusion glycoprotein. RB1 is the parental antibody to MK-1654 which is currently in clinical development for the prevention of RSV infection in infants. Nature Publishing Group UK 2019-09-12 /pmc/articles/PMC6742648/ /pubmed/31515478 http://dx.doi.org/10.1038/s41467-019-12137-1 Text en © The Author(s) 2019 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Tang, Aimin
Chen, Zhifeng
Cox, Kara S.
Su, Hua-Poo
Callahan, Cheryl
Fridman, Arthur
Zhang, Lan
Patel, Sangita B.
Cejas, Pedro J.
Swoyer, Ryan
Touch, Sinoeun
Citron, Michael P.
Govindarajan, Dhanasekaran
Luo, Bin
Eddins, Michael
Reid, John C.
Soisson, Stephen M.
Galli, Jennifer
Wang, Dai
Wen, Zhiyun
Heidecker, Gwendolyn J.
Casimiro, Danilo R.
DiStefano, Daniel J.
Vora, Kalpit A.
A potent broadly neutralizing human RSV antibody targets conserved site IV of the fusion glycoprotein
title A potent broadly neutralizing human RSV antibody targets conserved site IV of the fusion glycoprotein
title_full A potent broadly neutralizing human RSV antibody targets conserved site IV of the fusion glycoprotein
title_fullStr A potent broadly neutralizing human RSV antibody targets conserved site IV of the fusion glycoprotein
title_full_unstemmed A potent broadly neutralizing human RSV antibody targets conserved site IV of the fusion glycoprotein
title_short A potent broadly neutralizing human RSV antibody targets conserved site IV of the fusion glycoprotein
title_sort potent broadly neutralizing human rsv antibody targets conserved site iv of the fusion glycoprotein
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6742648/
https://www.ncbi.nlm.nih.gov/pubmed/31515478
http://dx.doi.org/10.1038/s41467-019-12137-1
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