ArticleVirology2015
N-glycosylation profiling of porcine reproductive and respiratory syndrome virus envelope glycoprotein 5.
Article in Virology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Protein nanoparticles assemble in plants, display antigenic viral peptides, and produce an epitope-specific immune response.The FEBS journal · 2026Article
- Role of N-linked glycosylation in porcine reproductive and respiratory syndrome virus (PRRSV) infection.The Journal of general virology · 2024Article
- Epitope screening and vaccine molecule design of PRRSV GP3 and GP5 protein based on immunoinformatics.Journal of cellular and molecular medicine · 2024Article
- Genetic variation and recombination analysis of theFrontiers in veterinary science · 2024Article
- Predicting Antigenic Distance from Genetic Data for PRRSV-Type 1: Applications of Machine Learning.Microbiology spectrum · 2023Article
- Plant production of a virus-like particle-based vaccine candidate against porcine reproductive and respiratory syndrome.Frontiers in plant science · 2023Article
- Potential Novel N-Glycosylation Patterns Associated with the Emergence of New Genetic Variants of PRRSV-2 in the U.S.Vaccines · 2022Article
- Using Alphafold2 to Predict the Structure of the Gp5/M Dimer of Porcine Respiratory and Reproductive Syndrome Virus.International journal of molecular sciences · 2022Article
- Genetic diversity of imported PRRSV-2 strains, 2005-2020, Hungary.Frontiers in veterinary science · 2022Article
- Phylogenetic Structure and Sequential Dominance of Sub-Lineages of PRRSV Type-2 Lineage 1 in the United States.Vaccines · 2021Article
- Palmitoylation of the envelope membrane proteins GP5 and M of porcine reproductive and respiratory syndrome virus is essential for virus growth.PLoS pathogens · 2021Article
- Article
- Griffithsin inhibits porcine reproductive and respiratory syndrome virus infection in vitro.Archives of virology · 2018Article
- Surface-displayed porcine reproductive and respiratory syndrome virus from cell culture onto gram-positive enhancer matrix particles.Journal of industrial microbiology & biotechnology · 2018Article
- Preferential use of Siglec-1 or Siglec-10 by type 1 and type 2 PRRSV strains to infect PK15Veterinary research · 2018Article
- Geographic distribution and molecular analysis of porcine reproductive and respiratory syndrome viruses circulating in swine farms in the Republic of Korea between 2013 and 2016.BMC veterinary research · 2018Article
- Molecular evolution of type 2 porcine reproductive and respiratory syndrome viruses circulating in Vietnam from 2007 to 2015.BMC veterinary research · 2016Article
- Analysis of genetic variation of porcine reproductive and respiratory syndrome virus (PRRSV) isolates in Central China.The Journal of veterinary medical science · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Porcine reproductive and respiratory syndrome virus (PRRSV) is a positive-sense ssRNA virus whose envelope contains four glycoproteins and three nonglycosylated proteins. Glycans of major envelope glycoprotein 5 (GP5) are proposed as important for virus assembly and entry into permissive cells. Structural characterization of GP5 glycans would facilitate the mechanistic understanding of these processes. Thus, we purified the PRRSV type 2 prototype strain, VR2332, and analyzed the virion-associated glycans by both biochemical and mass spectrometric methods. Endoglycosidase digestion showed that GP5 was the primary protein substrate, and that the carbohydrate moieties were primarily complex-type N-glycans. Mass spectrometric analysis (HPLC-ESI-MS/MS) of GP5 N-glycans revealed an abundance of N-acetylglucosamine (GlcNAc) and N-acetyllactosamine (LacNAc) oligomers in addition to sialic acids. GlcNAc and LacNAc accessibility to ligands was confirmed by lectin co-precipitation. Our findings help to explain PRRSV infection of cells lacking sialoadhesin and provide a glycan database to facilitate molecular structural studies of PRRSV.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.