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

scientific article published on 11 August 2017

The complex co-translational processing of glycoprotein GP5 of type 1 porcine reproductive and respiratory syndrome virus is …
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scholarly articleQ13442814

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P356DOI10.1016/J.VIRUSRES.2017.08.004
P698PubMed publication ID28807563

P50authorHans J NauwynckQ74988006
P2093author name stringMichael Veit
Bastian Thaa
Eberhard Krause
Bernadett Peibst
Sara A Neumann
Susanne Kaufer
P2860cites workStructure of the Sec61 channel opened by a signal sequenceQ27330079
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The M/GP(5) glycoprotein complex of porcine reproductive and respiratory syndrome virus binds the sialoadhesin receptor in a sialic acid-dependent mannerQ33525023
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Antigenic and Biological Characterization of ORF2-6 Variants at Early Times Following PRRSV InfectionQ33753971
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The primary GP5 neutralization epitope of North American isolates of porcine reproductive and respiratory syndrome virusQ45559394
Identification of an immunodominant epitope in the C terminus of glycoprotein 5 of porcine reproductive and respiratory syndrome virusQ45737829
Use of site-directed mutagenesis to define the limits of sequence variation tolerated for processing of the M13 procoat protein by the Escherichia coli leader peptidaseQ67780874
Lelystad virus, the causative agent of porcine epidemic abortion and respiratory syndrome (PEARS), is related to LDV and EAV.Q34062068
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Reorganization and expansion of the nidoviral family ArteriviridaeQ34503121
Signal Peptide Cleavage from GP5 of PRRSV: A Minor Fraction of Molecules Retains the Decoy Epitope, a Presumed Molecular Cause for Viral PersistenceQ34766625
Immune evasion of porcine reproductive and respiratory syndrome virus through glycan shielding involves both glycoprotein 5 as well as glycoprotein 3.Q34982599
Discovery of a small arterivirus gene that overlaps the GP5 coding sequence and is important for virus productionQ35114649
Novel structural protein in porcine reproductive and respiratory syndrome virus encoded by an alternative ORF5 present in all arterivirusesQ35114654
N-glycosylation profiling of porcine reproductive and respiratory syndrome virus envelope glycoprotein 5Q35189378
Cotranslational and posttranslocational N-glycosylation of proteins in the endoplasmic reticulumQ35639884
A single amino acid deletion in the matrix protein of porcine reproductive and respiratory syndrome virus confers resistance to a polyclonal swine antibody with broadly neutralizing activityQ35760446
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Purifying selection in porcine reproductive and respiratory syndrome virus ORF5a protein influences variation in envelope glycoprotein 5 glycosylation.Q37419512
Structural protein requirements in equine arteritis virus assemblyQ37596453
Signal peptidase I: Cleaving the way to mature proteinsQ37949867
Pathogenesis of porcine reproductive and respiratory syndrome virusQ38019627
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Membrane proteins of arterivirus particles: structure, topology, processing and function.Q38256285
Envelope protein requirements for the assembly of infectious virions of porcine reproductive and respiratory syndrome virusQ38321106
PRRS virus receptors and their role for pathogenesis.Q38442017
Signal peptide cleavage from GP3 enabled by removal of adjacent glycosylation sites does not impair replication of equine arteritis virus in cell culture, but the hydrophobic C-terminus is essential.Q39022117
N-Linked Glycosylation of GP5 of Porcine Reproductive and Respiratory Syndrome Virus Is Critically Important for Virus Replication In VivoQ39320224
GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) as a target for homologous and broadly neutralizing antibodiesQ39320804
GP4 of porcine reproductive and respiratory syndrome virus contains a neutralizing epitope that is susceptible to immunoselection in vitroQ39755506
Disulfide bonds between two envelope proteins of lactate dehydrogenase-elevating virus are essential for viral infectivityQ39868567
Identification of virulence determinants of porcine reproductive and respiratory syndrome virus through construction of chimeric clonesQ39944050
Neutralizing antibody responses of pigs infected with natural GP5 N-glycan mutants of porcine reproductive and respiratory syndrome virusQ40260080
The major envelope protein, GP5, of a European porcine reproductive and respiratory syndrome virus contains a neutralization epitope in its N-terminal ectodomain.Q40644350
ORF5 of porcine reproductive and respiratory syndrome virus (PRRSV) is a target of diversifying selection as infection progresses from acute infection to virus rebound.Q40761208
Monoclonal antibodies to the GP5 of porcine reproductive and respiratory syndrome virus are more effective in virus neutralization than monoclonal antibodies to the GP4.Q40956755
Isolation of swine infertility and respiratory syndrome virus (isolate ATCC VR-2332) in North America and experimental reproduction of the disease in gnotobiotic pigsQ41630101
Mystery swine disease in the Netherlands: The isolation of Lelystad virusQ41677026
Co-translational processing of glycoprotein 3 from equine arteritis virus: N-glycosylation adjacent to the signal peptide prevents cleavage.Q42261006
Highly Pathogenic Porcine Reproductive and Respiratory Syndrome Virus, AsiaQ42553042
GP5 ectodomain epitope of porcine reproductive and respiratory syndrome virus, strain Lelystad virusQ43856216
The primary neutralization epitope of porcine respiratory and reproductive syndrome virus strain VR-2332 is located in the middle of the GP5 ectodomainQ44255304
Influence of N-linked glycosylation of minor proteins of porcine reproductive and respiratory syndrome virus on infectious virus recovery and receptor interactionQ44401528
P921main subjectporcine reproductive and respiratory syndrome virusQ1760147
porcine reproductive and respiratory syndromeQ2275037
P304page(s)112-120
P577publication date2017-08-11
P1433published inVirus ResearchQ15749215
P1476titleThe complex co-translational processing of glycoprotein GP5 of type 1 porcine reproductive and respiratory syndrome virus
P478volume240

Reverse relations

Q47305713Differences in signal peptide processing between GP3 glycoproteins of Arteriviridae.cites workP2860

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