Self-association and mapping of the interaction domain of hepatitis E virus ORF3 protein

S. Tyagi, S. Jameel, S. K. Lal

Research output: Contribution to journalArticleResearchpeer-review

36 Citations (Scopus)

Abstract

Hepatitis E virus (HEV) is a major human pathogen in the developing world. In the absence of an in vitro culture system, very little information on the basic biology of the virus exists. A small protein (∼13.5 kDa) of unknown function, pORF3, is encoded by the third open reading frame of HEV. The N-terminal region of pORF3 is associated with the cytoskeleton using one of its hydrophobic domains. The C-terminal half of pORF3 is rich in proline residues and contains a putative src homology 3 (SH3) binding domain and a mitogen-activated protein kinase phosphorylation site. In this study, we demonstrate that pORF3 can homodimerize in vivo, using the yeast two-hybrid system. We have isolated a 43-amino-acid interaction domain of pORF3 which is capable of self-association in vivo and in vitro. The overlap of the dimerization domain with the SH3 binding and phosphorylation domains suggests that pORF3 may have a dimerization-dependent regulatory role to play in the signal transduction pathway.

Original languageEnglish
Pages (from-to)2493-2498
Number of pages6
JournalJournal of Virology
Volume75
Issue number5
DOIs
Publication statusPublished - 2001
Externally publishedYes

Cite this