Identification and Biosynthesis of Cyclic Enterobacterial Common Antigen in Escherichia coli

Autor: Ninguo Gao, Paul D. Rick, Kevin H. Gardner, Paul J. A. Erbel, Kathleen Barr, Gerrit J. Gerwig
Rok vydání: 2003
Předmět:
Zdroj: Journal of Bacteriology. 185:1995-2004
ISSN: 1098-5530
0021-9193
DOI: 10.1128/jb.185.6.1995-2004.2003
Popis: Phosphoglyceride-linked enterobacterial common antigen (ECA PG ) is a cell surface glycolipid that is synthesized by all gram-negative enteric bacteria. The carbohydrate portion of ECA PG consists of linear heteropolysaccharide chains comprised of the trisaccharide repeat unit Fuc4NAc-ManNAcA-GlcNAc, where Fuc4NAc is 4-acetamido-4,6-dideoxy- d -galactose, ManNAcA is N -acetyl- d -mannosaminuronic acid, and GlcNAc is N -acetyl- d -glucosamine. The potential reducing terminal GlcNAc residue of each polysaccharide chain is linked via phosphodiester linkage to a phosphoglyceride aglycone. We demonstrate here the occurrence of a water-soluble cyclic form of enterobacterial common antigen, ECA CYC , purified from Escherichia coli strains B and K-12 with solution nuclear magnetic resonance (NMR) spectroscopy, electrospray ionization mass spectrometry (ESI-MS), and additional biochemical methods. The ECA CYC molecules lacked an aglycone and contained four trisaccharide repeat units that were nonstoichiometrically substituted with up to four O-acetyl groups. ECA CYC was not detected in mutant strains that possessed null mutations in the wecA , wecF , and wecG genes of the wec gene cluster. These observations corroborate the structural data obtained by NMR and ESI-MS analyses and show for the first time that the trisaccharide repeat units of ECA CYC and ECA PG are assembled by a common biosynthetic pathway.
Databáze: OpenAIRE