Membrane proteins of arterivirus particles: structure, topology, processing and function

Autor: Anna Karolina Matczuk, Balaji Chandrasekhar Sinhadri, Eberhard Krause, Michael Veit, Bastian Thaa
Rok vydání: 2014
Předmět:
Models
Molecular
Signal peptide
Cancer Research
Glycosylation
Arterivirus
Protein Conformation
CHO
Chinese hamster ovary cells
Gp
glycoprotein
Antibodies
Viral
chemistry.chemical_compound
Epitopes
LC–MS/MS
liquid chromatography–tandem mass spectrometry
OST
oligosaccharyltransferase
Virus Release
GFP
green fluorescent protein
chemistry.chemical_classification
biology
LDV
murine lactate dehydrogenase-elevating virus
BiP
binding immunoglobulin protein
BHK
baby hamster kidney cells
Cell biology
HIV
human immunodeficiency virus
Protein Transport
Infectious Diseases
Membrane topology
Porcine reproductive and respiratory syndrome virus
PNGase F
peptide:N-glycosidase F
SHFV
simian haemorrhagic fever virus
GPI
glycosylphosphatidylinositol
Endo H
endoglycosidase H
CD
cluster of differentiation
EAV
equine arteritis virus
SRP
signal recognition particle
Models
Biological
SPase
signal peptidase
ESCRT
Article
Viral Matrix Proteins
ER
endoplasmic reticulum
Equartevirus
ESCRT
endosomal sorting complexes required for transport
ORF
open reading frame
Viral entry
Equine arteritis virus
Virology
HR
hydrophobic region
PAMs
porcine alveolar macrophages
MHC
major histocompatibility complex
Porcine respiratory and reproductive syndrome virus
SARS
severe acute respiratory syndrome
ComputingMethodologies_COMPUTERGRAPHICS
Virus Internalization
biology.organism_classification
Antibodies
Neutralizing
PI-PLC
phosphatidylinositol-specific phospholipase C
YFP
yellow fluorescent protein
ERGIC
ER–Golgi intermediate compartment
PRRSV
porcine reproductive and respiratory syndrome virus
Membrane protein
chemistry
DTT
dithiothreitol
SP
signal peptide
VLP
virus-like particle
BM2
M2 protein of influenza B
Glycoprotein
TMR
transmembrane region
Protein Modification
Translational
PFU
plaque-forming unit
Zdroj: Virus Research
ISSN: 1872-7492
Popis: Graphical abstract
Highlights • Arteriviruses are important pathogens in veterinary medicine. • We review the structure and processing of their membrane proteins. • Some features are unique from a cell biological point of view. • New data on this topic are also presented. • We speculate on the role of the membrane proteins during virus entry and budding.
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.
Databáze: OpenAIRE
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