Novel, Specific O-Glycosylation of Secreted Flavobacterium meningosepticum Proteins

Autor: Charles R. Hauer, Anthony L. Tarentino, T.H. Plummer
Rok vydání: 1995
Předmět:
Zdroj: Journal of Biological Chemistry. 270:13192-13196
ISSN: 0021-9258
DOI: 10.1074/jbc.270.22.13192
Popis: A new type of O-linked oligosaccharide has been discovered on several proteins secreted by the Gram-negative bacterium Flavobacterium meningosepticum, including Endo F2 (three sites), Endo F3 (one site), and a P40 protease (one site). The oligosaccharide moiety is covalently attached via a mannose residue to a serine or threonine at consensus sites corresponding to Asp-Ser∗ or Asp-Thr∗-Thr. Preliminary characterization by mass spectroscopy revealed an oligosaccharide of 1244 Da at each of the proposed glycosylation sites. Collision-associated dissociation analysis showed a characteristic daughter ion series of m/z 218, 394, and 556, indicative of a common Flavobacterium oligosaccharide. Compositional analysis demonstrated an unusual profile of monosaccharides, including hexoses, methylated hexoses, and uronic acid derivatives.
Databáze: OpenAIRE