The full-length and N-terminal deletion of ORF2 protein of hepatitis E virus can dimerize

Shweta Tyagi, Shahid Jameel, Sunil K. Lal

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12 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)214-221
Number of pages8
JournalBiochemical and Biophysical Research Communications
Issue number1
Publication statusPublished - 2001
Externally publishedYes

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