ArticleVirology journal2011
Mutation of putative N-linked glycosylation sites in Japanese encephalitis virus premembrane and envelope proteins enhances humoral immunity in BALB/C mice after DNA vaccination.
Article in Virology journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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.
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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
19 citing papers in PubMed, 32 citations in OpenAlex.
- Complete Genome Sequences of Human Japanese Encephalitis Virus Genotype V Isolates in Korea Reveal Genotype-Specific Amino Acid Signatures.Pathogens (Basel, Switzerland) · 2025Article
- The Sweet Aspects of Orthoflavivirus Treatment Design and Vaccine Development.Journal of medical virology · 2025Review
- Epidemiology, Transmission, and Evolution of Japanese Encephalitis Virus.Microorganisms · 2025Article
- Research Progress on the GP3 Protein of Porcine Reproductive and Respiratory Syndrome Virus.Animals : an open access journal from MDPI · 2025Review
- Article
- Molecular Detection and Genetic Characterization of Japanese Encephalitis Virus in Animals from 11 Provinces in China.Viruses · 2023Article
- Glycosylation of viral proteins: Implication in virus-host interaction and virulence.Virulence · 2022Review
- Genomic Characteristics and E Protein Bioinformatics Analysis of JEV Isolates from South China from 2011 to 2018.Vaccines · 2022Article
- A unified route for flavivirus structures uncovers essential pocket factors conserved across pathogenic viruses.Nature communications · 2021Article
- Article
- DC-SIGN Binding Contributed by an Extra N-Linked Glycosylation on Japanese Encephalitis Virus Envelope Protein Reduces the Ability of Viral Brain Invasion.Frontiers in cellular and infection microbiology · 2018Article
- Mx Is Not Responsible for the Antiviral Activity of Interferon-α against Japanese Encephalitis Virus.Viruses · 2017Article
- Entry of Classical Swine Fever Virus into PK-15 Cells via a pH-, Dynamin-, and Cholesterol-Dependent, Clathrin-Mediated Endocytic Pathway That Requires Rab5 and Rab7.Journal of virology · 2016Article
- Capsid-Targeted Viral Inactivation: A Novel Tactic for Inhibiting Replication in Viral Infections.Viruses · 2016Review
- Comparative genomic analysis of pre-epidemic and epidemic Zika virus strains for virological factors potentially associated with the rapidly expanding epidemic.Emerging microbes & infections · 2016Article
- Evaluation of the Impact of Codon Optimization and N-Linked Glycosylation on Functional Immunogenicity of Pfs25 DNA Vaccines Delivered by In Vivo Electroporation in Preclinical Studies in Mice.Clinical and vaccine immunology : CVI · 2015Article
- A Japanese encephalitis virus genotype 5 molecular clone is highly neuropathogenic in a mouse model: impact of the structural protein region on virulence.Journal of virology · 2015Article
- West Nile virus genome with glycosylated envelope protein and deletion of alpha helices 1, 2, and 4 in the capsid protein is noninfectious and efficiently secretes subviral particles.Journal of virology · 2013Article
- Biomarkers in Japanese encephalitis: a review.BioMed research international · 2013Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Swine are an important host of Japanese encephalitis virus (JEV). The two membrane glycoproteins of JEV, prM and E, each contain a potential N-linked glycosylation site, at positions N15 and N154, respectively. We constructed plasmids that contain the genes encoding wild-type prME (contain the signal of the prM, the prM, and the E coding regions) and three mutant prME proteins, in which the putative N-linked glycosylation sites are mutated individually or in combination, by site-directed mutagenesis. The recombinant plasmids were used as DNA vaccines in mice. Our results indicate that immunizing mice with DNA vaccines that contain the N154A mutation results in elevated levels of interleukin-4 secretion, induces the IgG1 antibody isotype, generates greater titers of anti-JEV antibodies, and shows complete protection against JEV challenge. We conclude that mutation of the putative N-glycosylation site N154 in the E protein of JEV significantly enhances the induced humoral immune response and suggest that this mutant should be further investigated as a potential DNA vaccine against JEV.
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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.