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The proteins were visualized by three specific antisera directed against the MT, HEL and POL domains.<jats:italic>In vitro<\/jats:italic>translation of full-length pORF1 yielded smaller quantities of two fragments. However, these fragments were not observed after pORF1 expression and pulse\u2013chase studies in human cells, and their production was not dependent on the predicted protease domain in pORF1. The weight of evidence supports the proposition that pORF1 is not subjected to specific proteolytic processing, which is unusual among animal positive-strand RNA viruses but common for plant viruses. pORF1 was membrane associated in cells and localized to a perinuclear region, where it partially overlapped with localization of the endoplasmic reticulum (ER) marker BAP31 and was closely interspersed with staining of the ER\u2013Golgi intermediate compartment marker protein ERGIC-53. Co-localization with BAP31 was enhanced by treatment with brefeldin A. Therefore, HEV may utilize modified early secretory pathway membranes for replication.<\/jats:p>","DOI":"10.1099\/vir.0.049577-0","type":"journal-article","created":{"date-parts":[[2012,12,20]],"date-time":"2012-12-20T10:14:27Z","timestamp":1355998467000},"page":"807-816","source":"Crossref","is-referenced-by-count":77,"title":["Early secretory pathway localization and lack of processing for hepatitis E virus replication protein pORF1"],"prefix":"10.1099","volume":"94","author":[{"given":"Julia","family":"Perttil\u00e4","sequence":"first","affiliation":[{"name":"Institute of Biotechnology, University of Helsinki, Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Pirjo","family":"Spuul","sequence":"additional","affiliation":[{"name":"Institute of Biotechnology, University of Helsinki, Helsinki, Finland"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tero","family":"Ahola","sequence":"additional","affiliation":[{"name":"Institute of 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