Dimerization: a structural feature for the protection of hepatitis E virus capsid protein against trypsinization.

ABSTRACT: Orally-transmitted viruses have evolved in a way to resist the extreme conditions of the host's gastrointestinal environment, especially the proteolysis of their structural proteins. However, the mechanisms allowing these viruses to survive these harsh conditions remain unclear. Hepatitis E virus (HEV) is an orally-transmitted human pathogen. Its capsid protein contains three domains S, P1 and P2. The latter forms a homodimer protruding from the virus shell, making it the most exposed part. By combining biochemical and computational methods, we found the trypsin digestion sites to be highly conserved among the HEV strains. Furthermore, the constructs of the HEV capsid protein that contain an extended P2 domain were digested within the extensions leaving the P2 domain intact. The trypsiniza

SUBMITTER: Wei W 

PROVIDER: S-EPMC5788867 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature