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

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

Nature communications (2019-09-14)
Aimin Tang, Zhifeng Chen, Kara S Cox, Hua-Poo Su, Cheryl Callahan, Arthur Fridman, Lan Zhang, Sangita B Patel, Pedro J Cejas, Ryan Swoyer, Sinoeun Touch, Michael P Citron, Dhanasekaran Govindarajan, Bin Luo, Michael Eddins, John C Reid, Stephen M Soisson, Jennifer Galli, Dai Wang, Zhiyun Wen, Gwendolyn J Heidecker, Danilo R Casimiro, Daniel J DiStefano, Kalpit A Vora
ABSTRACT

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.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
Anti-Human Metapneumovirus Antibody, clone 132, clone 132, Chemicon®, from mouse