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Journal of Virology, March 2001, p. 2493-2498, Vol. 75, No. 5
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.5.2493-2498.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Self-Association and Mapping of the Interaction Domain of Hepatitis E Virus ORF3 Protein

Shweta Tyagi, Shahid Jameel, and Sunil K. Lal*

Virology Group, International Centre for Genetic Engineering & Biotechnology, Aruna Asaf Ali Marg, New Delhi 110067, India

Received 18 September 2000/Accepted 30 November 2000

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.

* Corresponding author. Mailing address: Virology Group, International Centre for Genetic Engineering & Biotechnology, P.O. Box 10504, Aruna Asaf Ali Marg, New Delhi 110067, India. Phone: 91 (11) 6176680. Fax: 91 (11) 6162316. E-mail: sunillal{at}icgeb.res.in.

Journal of Virology, March 2001, p. 2493-2498, Vol. 75, No. 5
0022-538X/01/$04.00+0   DOI: 10.1128/JVI.75.5.2493-2498.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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