Structure and inhibition of EV-D68, a virus that causes respiratory illness in children

Author:

Liu Yue1,Sheng Ju1,Fokine Andrei1,Meng Geng1,Shin Woong-Hee1,Long Feng1,Kuhn Richard J.1,Kihara Daisuke12,Rossmann Michael G.1

Affiliation:

1. Department of Biological Sciences, Hockmeyer Hall of Structural Biology, 240 South Martin Jischke Drive, Purdue University, West Lafayette, IN 47907, USA.

2. Department of Computer Science, 305 North University Street, Purdue University, West Lafayette, IN 47907, USA.

Abstract

Targeting EV-D68, a respiratory virus A recent outbreak of respiratory illness in U.S. children was caused by entorovirus D68 (EV-D68). Enteroviruses also include human pathogens such as human rhinovirus, which causes the common cold, and poliovirus. Most of these viruses are stabilized by a factor that binds in a hydrophobic pocket of the capsid protein VP1, and antiviral compounds can act by displacing this factor. Liu et al. report the crystal structure of EV-D68 and its complex with the antiviral compound peconaril. In EV-D68, the hydrophobic pocket contained a fatty acid that was displaced by peconaril. Peconaril efficiently inhibited EV-D68 infection of cells, making it a possible drug candidate against EV-D68. Science , this issue p. 71

Funder

NIH

National Institutes of Health, National Center for Research Resources (NIH/NCRR)

U.S. Department of Energy, Office of Science, Office of Basic Energy Sciences

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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