ArticleJournal of virology2019
Article in Journal of virology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
38 citing papers in PubMed.
- Article
- Site-Specific Glycosylation Profiling of Protein Subunit and Inactivated Virus Vaccines.Vaccines · 2026Article
- Glycan-reactive antibodies isolated from human HIV-1 vaccine trial participants show broad pathogen cross-reactivity.Journal of virology · 2025Article
- Article
- Future Sequon Finder - A novel approach for predicting future N-linked glycosylation sequon locations on viral surface proteins.PloS one · 2025Article
- Multivalent interactions between fully glycosylated influenza virus hemagglutinins mediated by glycans at distinct N-glycosylation sites.Npj viruses · 2024Article
- A Complex-TypeInternational journal of molecular sciences · 2024Article
- Glycoproteomic Analyses of Influenza A Viruses Using timsTOF Pro MS.Journal of proteome research · 2023Article
- Glycosylation of H4 influenza strains with pandemic potential and susceptibilities to lung surfactant SP-D.Frontiers in molecular biosciences · 2023Article
- Message in a bottle: mRNA vaccination for influenza.The Journal of general virology · 2022Article
- Development of a Mouse Model to Explore CD4 T Cell Specificity, Phenotype, and Recruitment to the Lung after Influenza B Infection.Pathogens (Basel, Switzerland) · 2022Article
- Current view on novel vaccine technologies to combat human infectious diseases.Applied microbiology and biotechnology · 2022Review
- Analysis of the avian coronavirus spike protein reveals heterogeneity in the glycans present.The Journal of general virology · 2021Article
- Comparison of N-linked glycosylation on hemagglutinins derived from chicken embryos and MDCK cells: a case of the production of a trivalent seasonal influenza vaccine.Applied microbiology and biotechnology · 2021Article
- Site-specific N-glycosylation analysis of animal cell culture-derived Zika virus proteins.Scientific reports · 2021Article
- A cross-neutralizing antibody between HIV-1 and influenza virus.PLoS pathogens · 2021Article
- Article
- Mass Spectrometry-Based Structural Virology.Analytical chemistry · 2021Review
- Article
- Impact of Protein Glycosylation on the Design of Viral Vaccines.Advances in biochemical engineering/biotechnology · 2021Review
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.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Prior to each annual flu season, health authorities recommend three or four virus strains for inclusion in the annual influenza vaccine: a type A:H1N1 virus, a type A:H3N2 virus, and one or two type B viruses. Antigenic differences between strains are found in the glycosylation patterns of the major influenza virus antigen, hemagglutinin (HA). Here we examine the glycosylation patterns of seven reference antigens containing HA used in influenza vaccine potency testing. These reagents are supplied by the Center for Biologics Evaluation and Research (CBER) or the National Institute for Biological Standards and Control (NIBSC) for use in vaccine testing. Those produced in hen egg, Madin-Darby canine kidney (MDCK), and insect (Sf9) expression systems were examined. They are closely related or identical to antigens used in commercial vaccines. The reference antigens studied were used in the 2014-2015 influenza season and included A/California/07/2009 H1N1, A/Texas/50/2012 H3N2, and B/Massachusetts/02/2012. Released glycan and HA-specific glycopeptide glycosylation patterns were examined. We also examined the sensitivity of the single radial immunodiffusion (SRID) potency test to differences in HA antigen glycosylation. Based on deglycosylation studies applied using standard assay procedures, the SRID assay was not sensitive to any HA antigen glycosylation status from any cell system. Mapping of glycosites with their occupying glycan to functional regions, including antigenic sites, lectin interaction regions, and fusion domains, was performed and has implications for immune processing, immune responses, and antigenic shielding. Differences in glycosylation patterns, as dictated by the cell system used for expression, may impact these functions.
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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.