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O-glycan structures of gastropods

O-glycan structures of gastropods

Erika Staudacher (ORCID: 0000-0001-8282-1424)
  • Grant DOI 10.55776/P20393
  • Funding program Principal Investigator Projects
  • Status ended
  • Start March 1, 2008
  • End December 31, 2011
  • Funding amount € 158,969
  • Project website

Disciplines

Biology (100%)

Keywords

    Glycosylation, Snail, O-glycan, Gastropod

Abstract Final report

O-glycosylation of proteins is an emerging field in glycobiology research. More and more this kind of posttranslational modification of proteins is found to be essential for the correct transport and function of the proteins and involved in important recognition processes. For a complete understanding of the function and biosynthesis of this structural modification not only vertebrate but also invertebrate organisms have to be investigated for their O-glycosylation potential. As snails take part as an intermediate host in some developmental cycles of human and cattle parasites their glycosylation abilities are extremely interesting for the better understanding of host-parasite recognition processes. In this project we will elucidate the O-glycans of a number of gastropods (land and water snails with or without shell). A new strategy for O-glycosylation analysis has to be established in order to make sure that all possible linkages between sugar and amino acids are cleaved and the glycans can be labelled for further separation and analysis. For the N-glycans it has been already shown that the snails are capable to produce structural elements ranging from those typical in man through to structures similar to those found in schistosomes and therefore will be a valuable model to understand the regulation of glycosylation. For the O-glycans there are already some hints that the spectrum may be similar impressive.

O-glycosylation of proteins is an emerging field in glycobiology research. More and more this kind of posttranslational modification of proteins is found to be essential for the correct transport and function of the proteins and involved in important recognition processes. For a complete understanding of the function and biosynthesis of this structural modification not only vertebrate but also invertebrate organisms have to be investigated for their O-glycosylation potential. As snails take part as an intermediate host in some developmental cycles of human and cattle parasites their glycosylation abilities are extremely interesting for the better understanding of host-parasite recognition processes. In this project we will elucidate the O-glycans of a number of gastropods (land and water snails with or without shell). A new strategy for O-glycosylation analysis has to be established in order to make sure that all possible linkages between sugar and amino acids are cleaved and the glycans can be labelled for further separation and analysis. For the N-glycans it has been already shown that the snails are capable to produce structural elements ranging from those typical in man through to structures similar to those found in schistosomes and therefore will be a valuable model to understand the regulation of glycosylation. For the O-glycans there are already some hints that the spectrum may be similar impressive.

Research institution(s)
  • Universität für Bodenkultur Wien - 100%

Research Output

  • 174 Citations
  • 5 Publications
Publications
  • 2011
    Title Optimization of monosaccharide determination using anthranilic acid and 1-phenyl-3-methyl-5-pyrazolone for gastropod analysis
    DOI 10.1016/j.ab.2011.07.005
    Type Journal Article
    Author Stepan H
    Journal Analytical Biochemistry
    Pages 24-29
    Link Publication
  • 2012
    Title Methylation – an uncommon modification of glycans
    DOI 10.1515/hsz-2012-0132
    Type Journal Article
    Author Staudacher E
    Journal Biological chemistry
    Pages 675-685
    Link Publication
  • 2012
    Title O-Glycosylation of snails
    DOI 10.1007/s10719-012-9391-4
    Type Journal Article
    Author Stepan H
    Journal Glycoconjugate Journal
    Pages 189-198
    Link Publication
  • 2015
    Title Mucin-Type O-Glycosylation in Invertebrates
    DOI 10.3390/molecules200610622
    Type Journal Article
    Author Staudacher E
    Journal Molecules
    Pages 10622-10640
    Link Publication
  • 2010
    Title Determination of 3-O- and 4-O-methylated monosaccharide constituents in snail glycans
    DOI 10.1016/j.carres.2010.03.027
    Type Journal Article
    Author Stepan H
    Journal Carbohydrate Research
    Pages 1504-1507

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