Virus Research 240 (2017) 112–120 Contents lists available at ScienceDirect Virus Research journal homepage: www.elsevier.com/locate/virusres The complex co-translational processing of glycoprotein GP5 of type 1 MARK porcine reproductive and respiratory syndrome virus a,1 a,1 a a b Bastian Thaa , Susanne Kaufer , Sara A. Neumann , Bernadett Peibst , Hans Nauwynck , c a, Eberhard Krause , Michael Veit Freie Universität Berlin, Fachbereich Veterinärmedizin, Institut für Virologie, Robert-von-Ostertag-Straße 7–13, DE-14163 Berlin, Germany University of Ghent, Faculty of Veterinary Medicine, Laboratory of Virology, Salisburylaan 133, BE-9820 Merelbeke, Belgium Leibniz Institute of Molecular Pharmacology/FMP, Mass Spectrometry Unit, Robert-Rössle-Straße 10, DE-13125 Berlin-Buch, Germany ARTICLE I NFO ABSTRACT Keywords: GP5 and M, the major membrane proteins of porcine reproductive and respiratory syndrome virus (PRRSV), are PRRSV the driving force for virus budding and a target for antibodies. We studied co-translational processing of GP5 GP5 from an European PRRSV-1 strain. Using mass spectrometry, we show that in virus particles of a Lelystad Signal peptide variant, the signal peptide of GP5 was absent due to cleavage between glycine-34 and asparagine-35. This Co-translational protein processing cleavage site removes an epitope for a neutralizing monoclonal antibody, but leaves intact another epitope N-glycosylation recognized by neutralizing pig
Virus Research – Elsevier
Published: Aug 15, 2017
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