PMID- 25278143
OWN - NLM
STAT- MEDLINE
DCOM- 20150717
LR  - 20211021
IS  - 1872-7492 (Electronic)
IS  - 0168-1702 (Print)
IS  - 0168-1702 (Linking)
VI  - 194
DP  - 2014 Dec 19
TI  - Membrane proteins of arterivirus particles: structure, topology, processing and 
      function.
PG  - 16-36
LID - S0168-1702(14)00397-9 [pii]
LID - 10.1016/j.virusres.2014.09.010 [doi]
AB  - Arteriviruses, such as equine arteritis virus (EAV) and porcine reproductive and 
      respiratory syndrome virus (PRRSV), are important pathogens in veterinary 
      medicine. Despite their limited genome size, arterivirus particles contain a 
      multitude of membrane proteins, the Gp5/M and the Gp2/3/4 complex, the small and 
      hydrophobic E protein and the ORF5a protein. Their function during virus entry 
      and budding is understood only incompletely. We summarize current knowledge of 
      their primary structure, membrane topology, (co-translational) processing and 
      intracellular targeting to membranes of the exocytic pathway, which are the 
      budding site. We profoundly describe experimental data that led to widely 
      believed conceptions about the function of these proteins and also report new 
      results about processing steps for each glycoprotein. Further, we depict the 
      location and characteristics of epitopes in the membrane proteins since the late 
      appearance of neutralizing antibodies may lead to persistence, a characteristic 
      hallmark of arterivirus infection. Some molecular features of the arteriviral 
      proteins are rare or even unique from a cell biological point of view, 
      particularly the prevention of signal peptide cleavage by co-translational 
      glycosylation, discovered in EAV-Gp3, and the efficient use of overlapping 
      sequons for glycosylation. This article reviews the molecular mechanisms of these 
      cellular processes. Based on this, we present hypotheses on the structure and 
      variability of arteriviral membrane proteins and their role during virus entry 
      and budding.
CI  - Copyright (c) 2014 Elsevier B.V. All rights reserved.
FAU - Veit, Michael
AU  - Veit M
AD  - Institut fur Virologie, Veterinarmedizin, Freie Universitat Berlin, Germany. 
      Electronic address: mveit@zedat.fu-berlin.de.
FAU - Matczuk, Anna Karolina
AU  - Matczuk AK
AD  - Institut fur Virologie, Veterinarmedizin, Freie Universitat Berlin, Germany.
FAU - Sinhadri, Balaji Chandrasekhar
AU  - Sinhadri BC
AD  - Institut fur Virologie, Veterinarmedizin, Freie Universitat Berlin, Germany.
FAU - Krause, Eberhard
AU  - Krause E
AD  - Leibniz Institute of Molecular Pharmacology (FMP), Berlin, Germany.
FAU - Thaa, Bastian
AU  - Thaa B
AD  - Institut fur Virologie, Veterinarmedizin, Freie Universitat Berlin, Germany.
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20140930
PL  - Netherlands
TA  - Virus Res
JT  - Virus research
JID - 8410979
RN  - 0 (Antibodies, Neutralizing)
RN  - 0 (Antibodies, Viral)
RN  - 0 (Epitopes)
RN  - 0 (Viral Matrix Proteins)
SB  - IM
MH  - Antibodies, Neutralizing/immunology
MH  - Antibodies, Viral/immunology
MH  - Epitopes/immunology
MH  - Equartevirus/genetics/immunology/*physiology
MH  - Models, Biological
MH  - Models, Molecular
MH  - Porcine respiratory and reproductive syndrome virus/chemistry/*physiology
MH  - Protein Conformation
MH  - *Protein Modification, Translational
MH  - Protein Transport
MH  - Viral Matrix Proteins/genetics/immunology/*metabolism
MH  - *Virus Internalization
MH  - *Virus Release
PMC - PMC7172906
OTO - NOTNLM
OT  - Arterivirus
OT  - Equine arteritis virus
OT  - Glycosylation
OT  - Membrane topology
OT  - Porcine reproductive and respiratory syndrome virus
OT  - Signal peptide
EDAT- 2014/10/04 06:00
MHDA- 2015/07/18 06:00
PMCR- 2014/09/30
CRDT- 2014/10/04 06:00
PHST- 2014/08/11 00:00 [received]
PHST- 2014/09/20 00:00 [revised]
PHST- 2014/09/23 00:00 [accepted]
PHST- 2014/10/04 06:00 [entrez]
PHST- 2014/10/04 06:00 [pubmed]
PHST- 2015/07/18 06:00 [medline]
PHST- 2014/09/30 00:00 [pmc-release]
AID - S0168-1702(14)00397-9 [pii]
AID - 10.1016/j.virusres.2014.09.010 [doi]
PST - ppublish
SO  - Virus Res. 2014 Dec 19;194:16-36. doi: 10.1016/j.virusres.2014.09.010. Epub 2014 
      Sep 30.