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N-glycan epitopes in bivalve self/non-self recognition

N-glycan epitopes in bivalve self/non-self recognition

Katharina Paschinger (ORCID: 0000-0002-3594-7136)
  • Grant DOI 10.55776/P32572
  • Funding program Principal Investigator Projects
  • Status ended
  • Start December 1, 2019
  • End November 30, 2024
  • Funding amount € 408,055
  • Project website
  • E-mail

Disciplines

Biology (100%)

Keywords

    Glycomics, Glycophylogeny, Glycan Array, Invertebrate

Abstract Final report

Great advances have been made in recent years as regards genomic comparisons between organisms due to the large number of genome sequencing projects. In part these studies have altered our view of the phylogeny of organisms. However, the comparison of protein-linked carbohydrates, e.g., N-linked glycans, between organisms continues to lag behind due to the complicated nature of glycan analyses. On the other hand, glycans in their various types have key roles in fertilisation, development, morphogenesis and host-pathogen interactions as they cover the surfaces of all cells and so are involved in a wide range of cell-cell and self/non-self interactions In this project, it is proposed to focus on the N-linked glycans of selected bivalves, a group of predominantly marine organisms including oysters and clams as a human food source, they have economic importance; on the other hand, as filter feeders they are of high ecological relevance. Furthermore, they harbour human pathogens, but are also susceptible to their own pathogens; invasive species (such as the pacific oyster, Crassostrea gigas) can be more resistant to these than the native bivalves. Glycans of bivalves representing different families and habitats (including the pacific oyster and clams) will be examined. The fine detail of the N-glycans of these organisms will be assessed by mass spectrometric and other analyses. Correlations between the loss or gain of carbohydrate epitopes will be made with genomic and lectin binding data; for the latter, a tailor-made array of glycans from different species and tissues will be developed and promises to drive forward our functional knowledge about the self/non-self recognition between lectins and glycans. The result of this study will be a deeper understanding of a group of key post- translational modifications in a class of organisms of environmental and economic importance and their contribution to self vs. non-self recognition as models for innate immunity.

Great advances have been made in recent years as regards genomic comparisons between organisms due to the large number of genome sequencing projects. In part these studies have altered our view of the phylogeny of organisms. However, the comparison of protein-linked carbohydrates, e.g., N-linked glycans, between organisms continues to lag behind due to the complicated nature of glycan analyses. On the other hand, glycans in their various types have key roles in fertilisation, development, morphogenesis and host-pathogen interactions as they cover the surfaces of all cells and so are involved in a wide range of cell-cell and self/non-self interactions. In this project, the focus was on the N-linked glycans of selected invertebrates and protists.The fine detail of the N-glycans of certain bivalves, nematodes, slime moulds and insects was assessed by mass spectrometric and other analyses. Correlations between the loss or gain of carbohydrate epitopes were made with lectin binding data; for the latter, a tailor-made array of glycans from different species were developed and these data promise to drive forward our functional knowledge about the self/non-self recognition between lectins and glycans. This study results in a deeper understanding of a group of key post-translational modifications and their contribution to self vs. non-self recognition in innate immunity.

Research institution(s)
  • Universität für Bodenkultur Wien - 100%
International project participants
  • Linsheng Song, Dalian Ocean University - China
  • Niclas G. Karlsson, Oslo Metropolitan University - Norway
  • Gerardo R. Vasta, University of Maryland - USA

Research Output

  • 39 Citations
  • 9 Publications
  • 6 Datasets & models
  • 2 Scientific Awards
  • 1 Fundings
Publications
  • 2025
    Title Glycoproteomic and Single-Protein Glycomic Analyses Reveal Zwitterionic N-Glycans on Natural and Recombinant Proteins Derived From Insect Cells
    DOI 10.1016/j.mcpro.2025.100981
    Type Journal Article
    Author Yan S
    Journal Molecular & Cellular Proteomics
    Pages 100981
    Link Publication
  • 2024
    Title Analysis of Caenorhabditis Protein Glycosylation
    DOI 10.1007/978-1-0716-3666-4_8
    Type Book Chapter
    Author Paschinger K
    Publisher Springer Nature
    Pages 123-138
  • 2024
    Title Recognition of Highly Branched N-Glycans of the Porcine Whipworm by the Immune System
    DOI 10.1016/j.mcpro.2024.100711
    Type Journal Article
    Author Eckmair B
    Journal Molecular & Cellular Proteomics
    Pages 100711
    Link Publication
  • 2023
    Title N-glycan antennal modifications are altered in Caenorhabditis elegans lacking the HEX-4 N-acetylgalactosamine-specific hexosaminidase
    DOI 10.1016/j.jbc.2023.103053
    Type Journal Article
    Author Paschinger K
    Journal Journal of Biological Chemistry
    Pages 103053
    Link Publication
  • 2023
    Title Increasing Complexity of the N-Glycome During Caenorhabditis Development
    DOI 10.1016/j.mcpro.2023.100505
    Type Journal Article
    Author Wilson I
    Journal Molecular & Cellular Proteomics
    Pages 100505
    Link Publication
  • 2025
    Title New insights into the N-glycomes of Dictyostelium species
    DOI 10.1016/j.bbadva.2025.100142
    Type Journal Article
    Author Hykollari A
    Journal BBA Advances
    Pages 100142
    Link Publication
  • 2024
    Title Core Tri-fucosylation of Nematode N-glycans Requires Golgi a-mannosidase III Activity that Impacts Animal Growth and Behaviours
    DOI 10.1101/2024.07.18.600072
    Type Preprint
    Author Kendler J
    Pages 2024.07.18.600072
  • 2024
    Title N-glycan core tri-fucosylation requires Golgi a-mannosidase III activity that impacts nematode growth and behavior
    DOI 10.1016/j.jbc.2024.107944
    Type Journal Article
    Author Kendler J
    Journal Journal of Biological Chemistry
    Pages 107944
    Link Publication
  • 2021
    Title Negative-mode mass spectrometry in the analysis of invertebrate, fungal, and protist N-glycans
    DOI 10.1002/mas.21693
    Type Journal Article
    Author Hykollari A
    Journal Mass Spectrometry Reviews
    Pages 945-963
    Link Publication
Datasets & models
  • 2024 Link
    Title Trichuris suis glycome
    DOI 10.50821/glycopost-gpst000360
    Type Database/Collection of data
    Public Access
    Link Link
  • 2024
    Title Recombinant proteins from insect cells are modified with zwitterionic N-glycans
    DOI 10.50821/glycopost-gpst000369
    Type Database/Collection of data
    Public Access
  • 2024
    Title New insights into the N-glycomes of Dictyostelium species
    DOI 10.50821/glycopost-gpst000532
    Type Database/Collection of data
    Public Access
  • 2024 Link
    Title Nematode mannosidase III
    DOI 10.50821/glycopost-gpst000395
    Type Database/Collection of data
    Public Access
    Link Link
  • 2023 Link
    Title Stage-specific N-glycosylation of C. elegans
    DOI 10.50821/glycopost-gpst000294
    Type Database/Collection of data
    Public Access
    Link Link
  • 2023 Link
    Title N-acetylgalactosamine as a chain termination signal in nematode N-glycan biosynthesis: Impact of ablation of a hexosaminidase
    DOI 10.50821/glycopost-gpst000200
    Type Database/Collection of data
    Public Access
    Link Link
Scientific Awards
  • 2023
    Title Invited Speaker
    Type Personally asked as a key note speaker to a conference
    Level of Recognition Continental/International
  • 2019
    Title Invited Speaker
    Type Personally asked as a key note speaker to a conference
    Level of Recognition Continental/International
Fundings
  • 2021
    Title Immunomodulatory products of the Siberian fluke Opisthorchis
    Type Research grant (including intramural programme)
    Start of Funding 2021
    Funder Austrian Science Fund (FWF)

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