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

Tyagi, Shweta ; Jameel, Shahid ; Lal, Sunil K. (2001) The full-length and N-terminal deletion of ORF2 protein of hepatitis E virus can dimerize Biochemical and Biophysical Research Communications, 286 (1). pp. 214-221. ISSN 0006-291X

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00062...

Related URL: http://dx.doi.org/10.1006/bbrc.2001.5256

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.

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ID Code:13125
Deposited On:11 Nov 2010 06:49
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