ArticleJournal of virology2012
N-linked glycosylation of GP5 of porcine reproductive and respiratory syndrome virus is critically important for virus replication in vivo.
Article in Journal of virology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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Who cites it
42 citing papers in PubMed, 80 citations in OpenAlex.
- The S32 amino acid deletion in the GP5 protein modulates the infectivity of porcine reproductive and respiratory syndrome virus.Virulence · 2026Article
- EscaPRRS-ORF5: a structure-aware evolutionary framework for prioritizing immune escape-prone variants in porcine reproductive and respiratory syndrome virus.Bioinformatics (Oxford, England) · 2026Article
- Protein nanoparticles assemble in plants, display antigenic viral peptides, and produce an epitope-specific immune response.The FEBS journal · 2026Article
- Cross-Protection in PRRSV: Mechanisms, Limitations, and Implications for Vaccine Design.Pathogens (Basel, Switzerland) · 2026Review
- Molecular Characterization of a Recombinant NADC30-like PRRSV Strain with a Novel Gene Deletion Pattern in Nsp2 Gene.Veterinary sciences · 2025Article
- Molecular characterization of porcine reproductive and respiratory syndrome virus in Henan and Shanxi, China, during 2023-2024.Archives of virology · 2025Article
- Epidemiology and genetic characterization of porcine reproductive and respiratory syndrome virus in Fujian Province, China, from 2023 to 2024.Frontiers in veterinary science · 2025Article
- Temporal transcriptomic atlas reveals sequential engagement of classical and emerging regulated cell death pathways during PRRSV infection.Frontiers in veterinary science · 2025Article
- Prevalence and genetic diversity ofFrontiers in veterinary science · 2025Article
- Understanding Post-Translational Modifications in Porcine Reproductive and Respiratory Syndrome Virus Infection.Veterinary sciences · 2024Review
- A Comprehensive Review on Porcine Reproductive and Respiratory Syndrome Virus with Emphasis on Immunity.Vaccines · 2024Review
- PRRSV GP5 inhibits the antivirus effects of chaperone-mediated autophagy by targeting LAMP2A.mBio · 2024Article
- Investigation of the distribution and origin of porcine reproductive and respiratory syndrome virus 1 in the swine production chain: A retrospective study of three farms in Thailand.Veterinary world · 2024Article
- Role of N-linked glycosylation in porcine reproductive and respiratory syndrome virus (PRRSV) infection.The Journal of general virology · 2024Article
- Mass Spectrometry-Based Proteomic Analysis of Potential Host Proteins Interacting with GP5 in PRRSV-Infected PAMs.International journal of molecular sciences · 2024Article
- Sequence analysis of the GP5 protein of porcine reproductive and respiratory syndrome virus in Vietnam from 2007 to 2023.Frontiers in microbiology · 2024Article
- Molecular Characteristics and Pathogenicity of Porcine Reproductive and Respiratory Syndrome Virus (PRRSV) 1 in Taiwan during 2019-2020.Life (Basel, Switzerland) · 2023Article
- Porcine Reproductive and Respiratory Syndrome Virus Engineered by Serine Substitution on the 44th Amino Acid of GP5 Resulted in a Potential Vaccine Candidate with the Ability to Produce High Levels of Neutralizing Antibody.Veterinary sciences · 2023Article
- Research Progress on Glycoprotein 5 of Porcine Reproductive and Respiratory Syndrome Virus.Animals : an open access journal from MDPI · 2023Review
- Plant production of a virus-like particle-based vaccine candidate against porcine reproductive and respiratory syndrome.Frontiers in plant science · 2023Article
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
It has been proposed that the N-linked glycan addition at certain sites in GP5 of porcine reproductive and respiratory syndrome virus (PRRSV) is important for production of infectious viruses and viral infectivity. However, such specific N-linked glycosylation sites do not exist in some field PRRSV isolates. This implies that the existence of GP5-associated glycan per se is not vital to the virus life cycle. In this study, we found that mutation of individual glycosylation sites at N30, N35, N44, and N51 in GP5 did not affect virus infectivity in cultured cells. However, the mutants carrying multiple mutations at N-linked glycosylation sites in GP5 had significantly reduced virus yields compared with the wild-type (wt) virus. As a result, no viremia and antibody response were detected in piglets that were injected with a mutant without all N-linked glycans in GP5. These results suggest that the N-linked glycosylation of GP5 is critically important for virus replication in vivo. The study also showed that removal of N44-linked glycan from GP5 increased the sensitivity of mutant virus to convalescent-phase serum samples but did not elicit a high-level neutralizing antibody response to wt PRRSV. The results obtained from the present study have made significant contributions to better understanding the importance of glycosylation of GP5 in the biology of PRRSV.
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