The complex co-translational processing of glycoprotein GP5 of type 1 porcine reproductive and respiratory syndrome virus

The complex co-translational processing of glycoprotein GP5 of type 1 porcine reproductive and... 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 http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Virus Research Elsevier

The complex co-translational processing of glycoprotein GP5 of type 1 porcine reproductive and respiratory syndrome virus

Loading next page...
 
/lp/elsevier/the-complex-co-translational-processing-of-glycoprotein-gp5-of-type-1-ou00ZNG0RL
Publisher
Elsevier
Copyright
Copyright © 2017 Elsevier B.V.
ISSN
0168-1702
D.O.I.
10.1016/j.virusres.2017.08.004
Publisher site
See Article on Publisher Site

Abstract

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

Journal

Virus ResearchElsevier

Published: Aug 15, 2017

References

You’re reading a free preview. Subscribe to read the entire article.


DeepDyve is your
personal research library

It’s your single place to instantly
discover and read the research
that matters to you.

Enjoy affordable access to
over 18 million articles from more than
15,000 peer-reviewed journals.

All for just $49/month

Explore the DeepDyve Library

Search

Query the DeepDyve database, plus search all of PubMed and Google Scholar seamlessly

Organize

Save any article or search result from DeepDyve, PubMed, and Google Scholar... all in one place.

Access

Get unlimited, online access to over 18 million full-text articles from more than 15,000 scientific journals.

Your journals are on DeepDyve

Read from thousands of the leading scholarly journals from SpringerNature, Elsevier, Wiley-Blackwell, Oxford University Press and more.

All the latest content is available, no embargo periods.

See the journals in your area

DeepDyve

Freelancer

DeepDyve

Pro

Price

FREE

$49/month
$360/year

Save searches from
Google Scholar,
PubMed

Create lists to
organize your research

Export lists, citations

Read DeepDyve articles

Abstract access only

Unlimited access to over
18 million full-text articles

Print

20 pages / month

PDF Discount

20% off