Linked Life Data

10766852

Source:http://linkedlifedata.com/resource/pubmed/id/10766852

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
16
pubmed:dateCreated
2000-5-10
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
21
pubmed:volume
275
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
12164-74
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:10766852-Amino Acids, pubmed-meshheading:10766852-Animals, pubmed-meshheading:10766852-Antibodies, Monoclonal, pubmed-meshheading:10766852-Carbohydrate Sequence, pubmed-meshheading:10766852-Chromatography, Liquid, pubmed-meshheading:10766852-Dictyostelium, pubmed-meshheading:10766852-Fucose, pubmed-meshheading:10766852-Models, Chemical, pubmed-meshheading:10766852-Molecular Sequence Data, pubmed-meshheading:10766852-Molecular Weight, pubmed-meshheading:10766852-Permeability, pubmed-meshheading:10766852-Phosphoamino Acids, pubmed-meshheading:10766852-Phosphorylation, pubmed-meshheading:10766852-Protein Processing, Post-Translational, pubmed-meshheading:10766852-Protozoan Proteins, pubmed-meshheading:10766852-Spectrometry, Mass, Secondary Ion, pubmed-meshheading:10766852-Structure-Activity Relationship
pubmed:year
2000
pubmed:articleTitle
Multiple O-glycoforms on the spore coat protein SP96 in Dictyostelium discoideum. Fuc(alpha1-3)GlcNAc-alpha-1-P-Ser is the major modification.
pubmed:affiliation
Macquarie University Centre for Analytical Biotechnology, Department of Biological Sciences, Macquarie University, Sydney, New South Wales 2109, Australia.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, Non-U.S. Gov't