ArticleThe Journal of biological chemistry2013
Co-translational processing of glycoprotein 3 from equine arteritis virus: N-glycosylation adjacent to the signal peptide prevents cleavage.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- An alternative reverse genetics system for PRRS virus and its application to define the role of endocytic sorting signal in GP3 protein intracellular trafficking.Frontiers in microbiology · 2026Article
- Computational modelling of the equine arteritis virus GP5/M Dimer: Implications for immune evasion and virulence.PloS one · 2026Article
- Deglycosylation and truncation in the neuraminidase stalk are functionally equivalent in enhancing the pathogenicity of a high pathogenicity avian influenza virus in chickens.Journal of virology · 2025Article
- Using Alphafold2 to Predict the Structure of the Gp5/M Dimer of Porcine Respiratory and Reproductive Syndrome Virus.International journal of molecular sciences · 2022Article
- Expression of the Heterotrimeric GP2/GP3/GP4 Spike of an Arterivirus in Mammalian Cells.Viruses · 2022Article
- An archaellum filament composed of two alternating subunits.Nature communications · 2022Article
- Article
- Glycoprotein 3 of Porcine Reproductive and Respiratory Syndrome Virus Exhibits an Unusual Hairpin-Like Membrane Topology.Journal of virology · 2018Article
- Membrane proteins of arterivirus particles: structure, topology, processing and function.Virus research · 2014Review
- Sensing of immature particles produced by dengue virus infected cells induces an antiviral response by plasmacytoid dendritic cells.PLoS pathogens · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Signal peptide cleavage and N-glycosylation of proteins are co-translational processes, but little is known about their interplay if they compete for adjacent sites. Here we report two unique findings for processing of glycoprotein 3 of equine arteritis virus. Glycoprotein 3 (Gp3) contains an N-terminal signal peptide, which is not removed, although bioinformatics predicts cleavage with high probability. There is an overlapping sequon, NNTT, adjacent to the signal peptide that we show to be glycosylated at both asparagines. Exchanging the overlapping sequon and blocking glycosylation allows signal peptide cleavage, indicating that carbohydrate attachment inhibits processing of a potentially cleavable signal peptide. Bioinformatics analyses suggest that a similar processing scheme may exist for some cellular proteins. Membrane fractionation and secretion experiments revealed that the signal peptide of Gp3 does not act as a membrane anchor, indicating that it is completely translocated into the lumen of the endoplasmic reticulum. Membrane attachment is caused by the hydrophobic C terminus of Gp3, which, however, does not span the membrane but rather attaches the protein peripherally to endoplasmic reticulum membranes.
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Registered trials
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