Structure of RSV Fusion Glycoprotein Trimer Bound to a Prefusion-Specific Neutralizing Antibody

Author:

McLellan Jason S.1,Chen Man1,Leung Sherman1,Graepel Kevin W.1,Du Xiulian1,Yang Yongping1,Zhou Tongqing1,Baxa Ulrich2,Yasuda Etsuko3,Beaumont Tim3,Kumar Azad1,Modjarrad Kayvon1,Zheng Zizheng4,Zhao Min4,Xia Ningshao4,Kwong Peter D.1,Graham Barney S.1

Affiliation:

1. Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA.

2. Electron Microscopy Laboratory, Advanced Technology Program, SAIC-Frederick, Inc, Frederick National Laboratory for Cancer Research, Frederick, MD 21702, USA.

3. AIMM Therapeutics, Academic Medical Center, Amsterdam, Netherlands.

4. National Institute of Diagnostics and Vaccine Development in Infectious Diseases, Xiamen University, Xiamen, China, 361005.

Abstract

Building Better Vaccines Vaccines are one of the most effective tools to protect against infectious diseases. Unfortunately, vaccines for diseases with the highest global health burdens, such as HIV, malaria, and tuberculosis, are not yet available. Koff et al. (p. 1064 ) review the latest advances in vaccine development and why these particular diseases remain such a challenge. Respiratory syncytial virus (RSV) is a serious cause of morbidity and mortality in infants and young children worldwide. Although a prophylactic antibody is available for children at high risk, a vaccine is much needed. As a potential step toward this goal, McLellan et al. (p. 1113 , published online 25 April) solved the cocrystal structure of a neutralizing antibody (D25) bound to the prefusion F protein of RSV. Knowledge of the structure of the prefusion protein should help to guide vaccine design and the development of additional therapeutics.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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