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Multiple o-glycoforms on the spore coat protein sp96 in dictyostelium discoideum - fuc(alpha 1-3)glcnac-alpha-1-p-ser is the major modification

Academic Article
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Overview

authors

  • Mreyen, M.
  • Champion, A.
  • Srinivasan, Supriya
  • Karuso, P.
  • Williams, K. L.
  • Packer, N. H.

publication date

  • April 2000

journal

  • Journal of Biological Chemistry  Journal

abstract

  • A decreased level of fucosylation on certain spore coat proteins of Dictyostelium discoideum alters the permeability of the spore coat. Here the post-translational modifications of a major spore coat protein, SP96, are studied in a wild type strain (X22) and a fucosylation-defective mutant (HU2470). A novel phosphoglycan structure on SP96 of the wild type strain, consisting of Fuc(alpha1-3)GlcNAc-alpha-1-P-Ser(,) was identified by electrospray ionization mass spectrometry and NMR. It was shown using monosaccharide and gas chromatography mass spectrometry analysis that SP96 in the mutant HU2470 contained approximately 20% of wild type levels of fucose, as a result of a missing terminal fucose on the novel glycan structure. The results support previous predictions, based on inhibition studies on different fucose-deficient strains, about the nature of monoclonal antibody epitopes identified by monoclonal antibodies MUD62 and MUD166, which are known to identify O-linked glycans (Champion, A., Griffiths, K., Gooley, A. A., Gonzalez, B. Y., Gritzali, M., West, C. M., and Williams, K. L. (1995) Microbiology 141, 785-797). Quantitative studies on wild type SP96 indicated that there were approximately 60 sites with phosphodiester-linked N-acetylglucosamine-fucose disaccharide units and a further approximately 20 sites with fucose directly linked to the protein. Over 70% of the serine sites are modified, with less than 1% of these sites as phosphoserine. Threonine and tyrosine residues were not found to be modified.

subject areas

  • Amino Acids
  • Animals
  • Antibodies, Monoclonal
  • Carbohydrate Sequence
  • Chromatography, Liquid
  • Dictyostelium
  • Fucose
  • Models, Chemical
  • Molecular Sequence Data
  • Molecular Weight
  • Permeability
  • Phosphoamino Acids
  • Phosphorylation
  • Protein Processing, Post-Translational
  • Protozoan Proteins
  • Spectrometry, Mass, Secondary Ion
  • Structure-Activity Relationship
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Identity

International Standard Serial Number (ISSN)

  • 0021-9258

Digital Object Identifier (DOI)

  • 10.1074/jbc.275.16.12164

PubMed ID

  • 10766852
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Additional Document Info

start page

  • 12164

end page

  • 12174

volume

  • 275

issue

  • 16

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