title: The full-length and N-terminal deletion of ORF2 protein of hepatitis E virus can dimerize.
abstract: Hepatitis E virus is a human RNA virus containing three open reading frames. Of these ORF2 encodes, the major capsid protein (pORF2), may possess regulatory functions, in addition to a structural one. In this study, we have shown using the yeast two-hybrid system and in vitro immobilization experiments that full-length pORF2 is capable of self-association, thus forming a homodimer. Using mutational analysis we have studied dimerization of various truncated versions of the ORF2 capsid protein using the yeast two-hybrid system and supported our findings with in vitro immobilization experiments. Deletions of pORF2 reveal a loss of the dimerization potential for all deletions except an N-terminal 127-amino-acid deletion. Our studies suggest that the dimerization property of pORF2 may not be amino-acid sequence-dependent but instead a complex formation of a specific tertiary structure that imparts pORF2 its property to self-associate.
authors.affiliation: Virology Group, International Centre for Genetic Engineering and Biotechnology, Aruna Asaf Ali Road, New Delhi 110067, India.
authors.forename: S
authors.initials: S
authors.lastname: Tyagi
authors.forename: S
authors.initials: S
authors.lastname: Jameel
authors.forename: S K
authors.initials: SK
authors.lastname: Lal
mesh_terms: D000596:Amino Acids / Q000737:chemistry; D002213:Capsid / Q000737:chemistry*; D036022:Capsid Proteins; D019281:Dimerization; D006023:Glycoproteins / Q000737:chemistry*; D016752:Hepatitis E virus / Q000737:chemistry*; D017384:Sequence Deletion
chemical_list: D000596:Amino Acids; D036022:Capsid Proteins; D006023:Glycoproteins