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    Signal peptide cleavage from GP3 enabled by removal of adjacent glycosylation sites does not impair replication of equine arteritis virus in cell culture, but the hydrophobic C-terminus is essential (2014)

    Art
    Zeitschriftenartikel / wissenschaftlicher Beitrag
    Autoren
    Matczuk, Anna Karolina (WE 5)
    Veit, Michael (WE 5)
    Quelle
    Virus research; 183 — S. 107–111
    ISSN: 0168-1702
    Sprache
    Englisch
    Verweise
    DOI: 10.1016/j.virusres.2014.02.005
    Pubmed: 24556360
    Kontakt
    Institut für Virologie

    Robert-von-Ostertag-Str. 7-13
    Gebäude 35
    14163 Berlin
    Tel. +49 30 838 51833 Fax. +49 30 838 451847
    email:viro@zedat.fu-berlin.de

    Abstract / Zusammenfassung

    The disulphide-linked GP2/3/4 spike of equine arteritis virus (EAV) is essential for virus entry. We showed recently that in transfected cells carbohydrates attached adjacent to the signal peptide of GP3 inhibit cleavage. Here we confirm this unique phenomenon in recombinant viruses with disabled glycosylation sites. Surprisingly, the infectivity of EAV containing GP3 with cleaved signal peptide was not impaired and GP3 with cleaved signal peptide associates with GP2/4 in virus particles. In contrast, viruses containing GP3 with deleted hydrophobic C-terminus rapidly reverted back to wild type. The data support our model that the signal peptide is exposed to the lumen of the ER and the C-terminus peripherally attaches GP3 to membranes.