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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
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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

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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
Journal Article

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

2019
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Overview
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. Respiratory syncytial virus (RSV) is a leading cause of infant hospitalization. Here, the authors isolate a human monoclonal antibody that binds to a highly conserved epitope on the RSV fusion protein, neutralizes RSV A and B subtypes equipotently and is protective in the cotton rat model.