The cellular receptor for enterovirus 71.

Yue Liu,Michael G Rossmann

doi:10.1007/s13238-014-0092-6

Abstract

The cellular receptor for enterovirus 71.

Highlights

X-ray crystallography (Hogle et al, 1985; Rossmann et al, 1985), cryo-electron microscopy (Olson et al, 1993; Bubeck et al, 2005b) and molecular biology have unraveled some of the molecular mechanisms of EV cell entry (Tuthill et al, 2010)
Human SCARB2 binds to enterovirus 71 (EV71) but induces EV71 uncoating in a low pH environment (Yamayoshi et al, 2013), which is consistent with the finding that endosomal acidification is essential for EV71 infection (Lin et al, 2012)
Human SCARB2 structures at both neutral and acidic conditions were determined by X-ray crystallography, showing a pH-dependent conformational change of the three-helix bundle

Summary

Introduction

X-ray crystallography (Hogle et al, 1985; Rossmann et al, 1985), cryo-electron microscopy (cryo-EM) (Olson et al, 1993; Bubeck et al, 2005b) and molecular biology have unraveled some of the molecular mechanisms of EV cell entry (Tuthill et al, 2010). In essence, either the receptor or the pocket factor can bind to the virus, but not both (Smith et al, 1986; Rossmann, 1989).

Results

Conclusion