title: Degradation and aggresome formation of the Gn tail of the apathogenic Tula hantavirus.
abstract: The cytoplasmic tails of envelope glycoprotein Gn of pathogenic hantaviruses but not of the apathogenic Prospect Hill virus (PHV) were recently reported to be proteasomally degraded in simian COS7 cells. Here, we show that the cytoplasmic tails of the glycoproteins of the apathogenic hantaviruses Tula virus (TULV) and PHV are also degraded through the ubiquitin-proteasome pathway, both in human HEK-293 and in simian Vero E6 cells. TULV Gn tails formed aggresomes in cells with proteasomal inhibitors. We conclude that degradation upon aggregation of Gn tails, which may represent a general cellular response to misfolded protein used by hantaviruses to control maturation of virions, is unrelated to pathogenicity.
authors.affiliation: Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland.
authors.forename: Hao
authors.initials: H
authors.lastname: Wang
authors.affiliation: Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland.
authors.forename: Tomas
authors.initials: T
authors.lastname: Strandin
authors.affiliation: Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland.
authors.forename: Jussi
authors.initials: J
authors.lastname: Hepojoki
authors.affiliation: Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland.
authors.forename: Hilkka
authors.initials: H
authors.lastname: Lankinen
authors.affiliation: Department of Virology, Haartman Institute, PO Box 21, FIN-00014 University of Helsinki, Finland.
authors.forename: Antti
authors.initials: A
authors.lastname: Vaheri
mesh_terms: D000818:Animals; D002460:Cell Line; D002522:Chlorocebus aethiops; D003593:Cytoplasm / Q000378:metabolism; D004847:Epithelial Cells / Q000821:virology; D015686:Gene Products, env / Q000235:genetics / Q000378:metabolism*; D006476:Orthohantavirus / Q000378:metabolism / Q000472:pathogenicity* / Q000502:physiology / Q000648:ultrastructure; D006801:Humans; D007181:Inclusion Bodies, Viral / Q000378:metabolism*; D007668:Kidney / Q000166:cytology / Q000821:virology; D018613:Microscopy, Confocal; D046988:Proteasome Endopeptidase Complex / Q000378:metabolism; D014162:Transfection; D025801:Ubiquitin / Q000378:metabolism; D014709:Vero Cells / Q000821:virology
chemical_list: D015686:Gene Products, env; D025801:Ubiquitin; D046988:Proteasome Endopeptidase Complex