A pH-dependent molecular switch for virion uncoating.

Satoshi Koike

doi:10.1007/s13238-014-0094-4

Abstract

A pH-dependent molecular switch for virion uncoating.

Highlights

Native virions of enteroviruses are composed of a positive-stranded RNA genome and 60 copies of each capsid protein; namely VP1, VP2, VP3 and VP4
The binding interfaces of scavenger receptor class B member 2 (SCARB2) and EV71 have not been determined, SCARB2 is suggested to bind to the “canyon” of EV71 particles like other uncoating receptors, and importance of acidic pH conditions in establishment of infection was unclear
It is known that SCARB2 plays a physiologically important role in transporting newly synthesized β-glucocerebrosidase (β-GCase) to lysosomal compartments. β-GCase binds to SCARB2 in the endoplasmic reticulum at neutral pH and β-GCase dissociates from SCARB2 in lysosomes at acidic pH, suggesting that the conformation of SCARB2 under neutral and acidic pH conditions is different

Summary

Introduction

Native virions of enteroviruses are composed of a positive-stranded RNA genome and 60 copies of each capsid protein; namely VP1, VP2, VP3 and VP4. The natural lipid called “pocket factor” is harbored in the hydrophobic pocket of the VP1 capsid protein and plays an important role in stabilizing the native virion structure. Enterovirus infection is initiated by the binding of virions to their respective receptors followed by their internalization into the cells. The internalized virion undergoes serial structural changes that lead to a release of viral genomic RNA into the cytoplasm.

Results

Conclusion