ArticleJournal of proteome research2013
Comparative glycomics analysis of influenza Hemagglutinin (H5N1) produced in vaccine relevant cell platforms.
Article in Journal of proteome research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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
42 citing papers in PubMed, 62 citations in OpenAlex.
- Repeat vaccination reduces antibody affinity maturation across different influenza vaccine platforms in humans.Nature communications · 2019Trial
- INAAC: An affinity chromatography strategy enabling characterization and quantification of influenza neuraminidase antigens in vaccines.The Journal of biological chemistry · 2026Article
- Low-level human memory T and B cells recognising avian influenza hemagglutinins are poorly responsive to existing seasonal influenza vaccines.Clinical & translational immunology · 2025Article
- Antibody-independent surface plasmon resonance assays for influenza vaccine quality control.Applied microbiology and biotechnology · 2024Review
- Article
- Arbidol: The current demand, strategies, and antiviral mechanisms.Immunity, inflammation and disease · 2023Review
- Glycosylation of H4 influenza strains with pandemic potential and susceptibilities to lung surfactant SP-D.Frontiers in molecular biosciences · 2023Article
- Antibodies targeting the neuraminidase active site inhibit influenza H3N2 viruses with an S245N glycosylation site.Nature communications · 2022Article
- Antigenic characterization of influenza and SARS-CoV-2 viruses.Analytical and bioanalytical chemistry · 2022Review
- Messenger RNA-Based Vaccines Against Infectious Diseases.Current topics in microbiology and immunology · 2022Review
- An Overview of Influenza Viruses and Vaccines.Vaccines · 2021Review
- Analysis of the avian coronavirus spike protein reveals heterogeneity in the glycans present.The Journal of general virology · 2021Article
- Impact of Expressing Cells on Glycosylation and Glycan of the SARS-CoV-2 Spike Glycoprotein.ACS omega · 2021Article
- Animal Cell Expression Systems.Advances in biochemical engineering/biotechnology · 2021Article
- Glycobiotechnology of the Insect Cell-Baculovirus Expression System Technology.Advances in biochemical engineering/biotechnology · 2021Article
- Multiscale Simulations Examining Glycan Shield Effects on Drug Binding to Influenza Neuraminidase.Biophysical journal · 2020Article
- Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition.Scientific reports · 2020Article
- Comparison of Human H3N2 Antibody Responses Elicited by Egg-Based, Cell-Based, and Recombinant Protein-Based Influenza Vaccines During the 2017-2018 Season.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2020Article
- Glycomics and glycoproteomics of viruses: Mass spectrometry applications and insights toward structure-function relationships.Mass spectrometry reviews · 2020Review
- Analysis of the SARS-CoV-2 spike protein glycan shield: implications for immune recognition.bioRxiv : the preprint server for biology · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 2 institutions in 1 country.
Funding
Abstract
Hemagglutinin (HA) is the major antigen in influenza vaccines, and glycosylation is known to influence its antigenicity. Embryonated hen eggs are traditionally used for influenza vaccine production, but vaccines produced in mammalian and insect cells were recently licensed. This raises the concern that vaccines produced with different cell systems might not be equivalent due to differences in their glycosylation patterns. Thus, we developed an analytical method to monitor vaccine glycosylation through a combination of nanoLC/MS(E) and quantitative MALDI-TOF MS permethylation profiling. We then used this method to examine glycosylation of HAs from two different influenza H5N1 strains produced in five different platforms, including hen eggs, three different insect cell lines (High Five, expresSF+ and glycoengineered expresSF+), and a human cell line (HEK293). Our results demonstrated that (1) sequon utilization is not necessarily equivalent in different cell types, (2) there are quantitative and qualitative differences in the overall N-glycosylation patterns and structures produced by different cell types, (3) ∼20% of the N-glycans on the HAs produced by High Five cells are core α1,3-fucosylated structures, which may be allergenic in humans, and (4) our method can be used to monitor differences in glycosylation during the cellular glycoengineering stages of vaccine development.
Indexed as
Identifiers
What OpenQuestion holds
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.