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J. Virol. doi:10.1128/JVI.02039-06
Copyright (c) 2007, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Cytoplasmic localization of the ORF2 protein of hepatitis E virus is dependent on its ability to undergo retro-translocation from the endoplasmic reticulum

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

^* To whom correspondence should be addressed. Email: sunillal{at}icgeb.res.in.

	Abstract

Hepatitis E virus (HEV) is a positive strand RNA virus prevalent in much of the developing world. ORF2 is the major capsid protein of HEV. Although ORF2 is an N-linked glycoprotein it is abundantly located in the cytoplasm in addition to membrane and surface localization. The mechanism by which ORF2 protein gets access to the cytoplasm is unknown. In this report, we prove that initially all ORF2 protein is present in the ER and a fraction of it gets retro-translocated to the cytoplasm. The ability of ORF2 to get retro-translocated is dependent on its glycosylation status and follows the canonical dislocation pathway. However, in contrast to general substrates of the dislocation pathway, retro-translocated ORF2 protein is not a substrate of the 26S proteasome complex and is readily detectable in the cytoplasm in the absence of any protease inhbitor, suggesting that the retrotranslocated protein is stable in the cytoplasm. This study thus defines the pathway by which ORF2 gets access to the cytoplasm.

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