PMID- 28807563
OWN - NLM
STAT- MEDLINE
DCOM- 20180126
LR  - 20180209
IS  - 1872-7492 (Electronic)
IS  - 0168-1702 (Linking)
VI  - 240
DP  - 2017 Aug 15
TI  - The complex co-translational processing of glycoprotein GP5 of type 1 porcine 
      reproductive and respiratory syndrome virus.
PG  - 112-120
LID - S0168-1702(17)30494-X [pii]
LID - 10.1016/j.virusres.2017.08.004 [doi]
AB  - GP5 and M, the major membrane proteins of porcine reproductive and respiratory 
      syndrome virus (PRRSV), are the driving force for virus budding and a target for 
      antibodies. We studied co-translational processing of GP5 from an European 
      PRRSV-1 strain. Using mass spectrometry, we show that in virus particles of a 
      Lelystad variant, the signal peptide of GP5 was absent due to cleavage between 
      glycine-34 and asparagine-35. This cleavage site removes an epitope for a 
      neutralizing monoclonal antibody, but leaves intact another epitope recognized by 
      neutralizing pig sera. Upon ectopic expression of this GP5 in cells, signal 
      peptide cleavage was however inefficient. Complete cleavage occurred when 
      cysteine-24 was changed to proline or an unused glycosylation site involving 
      asparagine-35 was mutated. Insertion of proline at position 24 also caused 
      carbohydrate attachment to asparagine-35. Glycosylation sites introduced 
      downstream of residue 35 were used, but did not inhibit signal peptide 
      processing. Co-expression of the M protein rescued this processing defect in GP5, 
      suggesting a novel function of M towards GP5. We speculate that a complex 
      interplay of the co-translational modifications of GP5 affect the N-terminal 
      structure of the mature proteins and hence its antigenicity.
CI  - Copyright (c) 2017 Elsevier B.V. All rights reserved.
FAU - Thaa, Bastian
AU  - Thaa B
AD  - Freie Universitat Berlin, Fachbereich Veterinarmedizin, Institut fur Virologie, 
      Robert-von-Ostertag-Strasse 7-13, DE-14163 Berlin, Germany.
FAU - Kaufer, Susanne
AU  - Kaufer S
AD  - Freie Universitat Berlin, Fachbereich Veterinarmedizin, Institut fur Virologie, 
      Robert-von-Ostertag-Strasse 7-13, DE-14163 Berlin, Germany.
FAU - Neumann, Sara A
AU  - Neumann SA
AD  - Freie Universitat Berlin, Fachbereich Veterinarmedizin, Institut fur Virologie, 
      Robert-von-Ostertag-Strasse 7-13, DE-14163 Berlin, Germany.
FAU - Peibst, Bernadett
AU  - Peibst B
AD  - Freie Universitat Berlin, Fachbereich Veterinarmedizin, Institut fur Virologie, 
      Robert-von-Ostertag-Strasse 7-13, DE-14163 Berlin, Germany.
FAU - Nauwynck, Hans
AU  - Nauwynck H
AD  - University of Ghent, Faculty of Veterinary Medicine, Laboratory of Virology, 
      Salisburylaan 133, BE-9820 Merelbeke, Belgium.
FAU - Krause, Eberhard
AU  - Krause E
AD  - Leibniz Institute of Molecular Pharmacology/FMP, Mass Spectrometry Unit, 
      Robert-Rossle-Strasse 10, DE-13125 Berlin-Buch, Germany.
FAU - Veit, Michael
AU  - Veit M
AD  - Freie Universitat Berlin, Fachbereich Veterinarmedizin, Institut fur Virologie, 
      Robert-von-Ostertag-Strasse 7-13, DE-14163 Berlin, Germany. Electronic address: 
      michael.veit@fu-berlin.de.
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
DEP - 20170812
PL  - Netherlands
TA  - Virus Res
JT  - Virus research
JID - 8410979
RN  - 0 (Protein Sorting Signals)
RN  - 0 (Viral Envelope Proteins)
RN  - 0 (glycoprotein 5, PRRSV)
SB  - IM
MH  - Amino Acid Motifs
MH  - Animals
MH  - Glycosylation
MH  - Porcine Reproductive and Respiratory Syndrome/*virology
MH  - Porcine respiratory and reproductive syndrome 
      virus/chemistry/genetics/*metabolism
MH  - Protein Modification, Translational
MH  - Protein Sorting Signals
MH  - Swine
MH  - Viral Envelope Proteins/*chemistry/genetics/*metabolism
OTO - NOTNLM
OT  - Co-translational protein processing
OT  - GP5
OT  - N-glycosylation
OT  - Oligomerisation
OT  - PRRSV
OT  - Signal peptide
EDAT- 2017/08/16 06:00
MHDA- 2018/01/27 06:00
CRDT- 2017/08/16 06:00
PHST- 2017/06/21 00:00 [received]
PHST- 2017/08/07 00:00 [revised]
PHST- 2017/08/08 00:00 [accepted]
PHST- 2017/08/16 06:00 [pubmed]
PHST- 2018/01/27 06:00 [medline]
PHST- 2017/08/16 06:00 [entrez]
AID - S0168-1702(17)30494-X [pii]
AID - 10.1016/j.virusres.2017.08.004 [doi]
PST - ppublish
SO  - Virus Res. 2017 Aug 15;240:112-120. doi: 10.1016/j.virusres.2017.08.004. Epub 
      2017 Aug 12.