ArticleJournal of virology2005
Envelope protein requirements for the assembly of infectious virions of porcine reproductive and respiratory syndrome virus.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 114 papers.
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Who cites it
114 citing papers in PubMed, 240 citations in OpenAlex.
- Evaluation of the contribution of the minor envelope complex glycoprotein 3 ectodomain to the porcine reproductive and respiratory syndrome virus 1 neutralizing antibody response.The Journal of general virology · 2026Article
- The ER-Golgi intermediate compartment: a central hub integrating membrane trafficking and stress responses.EMBO reports · 2026Review
- Research Progress of GP4 Protein of Porcine Reproductive and Respiratory Syndrome Virus.Veterinary sciences · 2026Review
- Porcine Reproductive and Respiratory Syndrome Virus (PRRSV)-Induced Reactive Oxygen Species Inhibit Phagocytosis in Alveolar Macrophages.International journal of molecular sciences · 2026Article
- Signal peptide cleavage and ectodomain regions of GP2 are required for PRRSV infection.The Journal of general virology · 2026Article
- OTUB1 stabilizes PRRSV matrix protein through a non-canonical deubiquitination mechanism to promote viral replication.Journal of virology · 2026Article
- 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
- Advances in the immunosuppression of porcine reproductive and respiratory syndrome virus.Frontiers in veterinary science · 2026Review
- Nationwide emergence and spread of highly virulent PRRSV-2 mutants in Korea.Porcine health management · 2025Article
- A Porcine Monoclonal Antibody Targeting a Conserved GP4 Epitope Protects against In Vivo Infection via the Induction of Broad-Spectrum PRRSV Neutralization.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- The role of immune checkpoint molecules in PRRSV-2-induced immune modulation: insights from comparativeJournal of virology · 2025Article
- LGALS3BP/90K suppresses porcine reproductive and respiratory syndrome virus replication by enhancing GP3 degradation and stimulating innate immunity.Veterinary research · 2025Article
- In Silico Designed Multi-Epitope Vaccine Based on the Conserved Fragments in Viral Proteins for Broad-Spectrum Protection Against Porcine Reproductive and Respiratory Syndrome Virus.Veterinary sciences · 2025Article
- Protective Efficacy of an mRNA Vaccine Against HP-PRRSV Challenge in Piglets.Microorganisms · 2025Article
- A serologic marker attenuated live vaccine protects piglets against highly pathogenic porcine reproductive and respiratory syndrome virus infection.Veterinary research · 2025Article
- Research Progress on the GP3 Protein of Porcine Reproductive and Respiratory Syndrome Virus.Animals : an open access journal from MDPI · 2025Review
- The full-length nsp2 replicase contributes to viral assembly in highly pathogenic PRRSV-2.Journal of virology · 2025Article
- Experimental evidence of vaccine-driven evolution of respiratory syndrome virus type 2.Virus evolution · 2025Article
- The role of major and minor structural proteins of porcine reproductive and respiratory syndrome virus in induction of protective immunity.Frontiers in microbiology · 2025Article
54 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Virions of porcine reproductive and respiratory syndrome virus (PRRSV) contain six membrane proteins: the major proteins GP5 and M and the minor proteins GP2a, E, GP3, and GP4. Here, we studied the envelope protein requirements for PRRSV particle formation and infectivity using full-length cDNA clones in which the genes encoding the membrane proteins were disrupted by site-directed mutagenesis. By transfection of RNAs transcribed from these cDNAs into BHK-21 cells and analysis of the culture medium using ultracentrifugation, radioimmunoprecipitation, and real-time reverse transcription-PCR, we observed that the production of viral particles is dependent on both major envelope proteins; no particles were released when either the GP5 or the M protein was absent. In contrast, particle production was not dependent on the minor envelope proteins. Remarkably, in the absence of any one of the latter proteins, the incorporation of all other minor envelope proteins was affected, indicating that these proteins interact with each other and are assembled into virions as a multimeric complex. Independent evidence for such complexes was obtained by coexpression of the minor envelope proteins in BHK-21 cells using a Semliki Forest virus expression system. By analyzing the maturation of their N-linked oligosaccharides, we found that the glycoproteins were each retained in the endoplasmic reticulum unless expressed together, in which case they were collectively transported through the Golgi complex to the plasma membrane and were even detected in the extracellular medium. As the PRRSV particles lacking the minor envelope proteins are not infectious, we hypothesize that the virion surface structures formed by these proteins function in viral entry by mediating receptor binding and/or virus-cell fusion.
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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.