Interaction of Decay-Accelerating Factor with Echovirus 7

Author:

Plevka Pavel1,Hafenstein Susan12,Harris Katherine G.1,Cifuente Javier O.2,Zhang Ying1,Bowman Valorie D.1,Chipman Paul R.1,Bator Carol M.1,Lin Feng3,Medof M. Edward3,Rossmann Michael G.1

Affiliation:

1. Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, Indiana 47907-2054

2. Department of Microbiology and Immunology, The Pennsylvania State University College of Medicine, 500 University Drive, Hershey, Pennsylvania 17033

3. Institute of Pathology, Case Western Reserve University, School of Medicine, 2085 Adelbert Road, Room 301, Cleveland, Ohio 44106

Abstract

ABSTRACT Echovirus 7 (EV7) belongs to the Enterovirus genus within the family Picornaviridae . Many picornaviruses use IgG-like receptors that bind in the viral canyon and are required to initiate viral uncoating during infection. However, in addition, some of the enteroviruses use an alternative or additional receptor that binds outside the canyon. Decay-accelerating factor (DAF) has been identified as a cellular receptor for EV7. The crystal structure of EV7 has been determined to 3.1-Å resolution and used to interpret the 7.2-Å-resolution cryo-electron microscopy reconstruction of EV7 complexed with DAF. Each DAF binding site on EV7 is near a 2-fold icosahedral symmetry axis, which differs from the binding site of DAF on the surface of coxsackievirus B3, indicating that there are independent evolutionary processes by which DAF was selected as a picornavirus accessory receptor. This suggests that there is an advantage for these viruses to recognize DAF during the initial process of infection.

Publisher

American Society for Microbiology

Subject

Virology,Insect Science,Immunology,Microbiology

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