Hepatitis A virus capsid structure

DOI: 10.1101/cshperspect.a031807

Authors: David I. Stuart (The Wellcome Trust Centre for Human Genetics, University of Oxford; Diamond Light Source) , Jingshan Ren (The Wellcome Trust Centre for Human Genetics, University of Oxford) , Xiangxi Wang (Institute of Biophysics, Chinese Academy of Science) , Zihe Rao (Institute of Biophysics, Chinese Academy of Science; Tsinghua University) , Elizabeth E. Fry (University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cold Spring Harbor Perspectives In Medicine

State: Published (Approved)
Published: July 2018
Diamond Proposal Number(s): 6387 , 8423

Abstract: Hepatitis A virus (HAV) has been enigmatic, evading detailed structural analysis for many years. Its recently determined high-resolution structure revealed an angular surface without the indentations often characteristic of receptor-binding sites. The viral protein 1 (VP1) β-barrel shows no sign of a pocket factor and the amino terminus of VP2 displays a “domain swap” across the pentamer interface, as in a subset of mammalian picornaviruses and insect picorna-like viruses. Structure-based phylogeny confirms this placement. These differences suggest an uncoating mechanism distinct from that of enteroviruses. An empty capsid structure reveals internal differences in VP0 and the VP1 amino terminus connected with particle maturation. An HAV/Fab complex structure, in which the antigen-binding fragment (Fab) appears to act as a receptor–mimic, clarifies some historical epitope mapping data, but some remain difficult to reconcile. We still have little idea of the structural features of enveloped HAV particles.

Diamond Keywords: Viruses; Hepatitis A Virus; Liver Disease

Subject Areas: Biology and Bio-materials


Instruments: I03-Macromolecular Crystallography , I24-Microfocus Macromolecular Crystallography

Added On: 26/07/2018 09:56

Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)