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Papers In Press, published online ahead of print May 18, 2000
Department of Biochem. & Molec. Biol., OUHSC, Oklahoma City, OK 73104
Corresponding Author: paul-deangelis{at}ouhsc.edu
Pasteurella multocida Type F, the minor fowl cholera pathogen, produces an extracellular polysaccharide capsule that is a putative virulence factor. It was reported that the capsule was removed by treating microbes with chondroitin AC lyase. We found by acid hydrolysis that the polysaccharide contained galactosamine and glucuronic acid. We molecularly cloned a Type F polysaccharide synthase and characterized its enzymatic activity. The 965-residue enzyme, called pmCS, is 87% identical at the nucleotide and the amino acid level to the hyaluronan synthase, pmHAS, from P. multocida Type A. A recombinant Escherichia coli-derived truncated, soluble version of pmCS (residues 1-704) was shown to catalyze the repetitive addition of sugars from UDP-GalNAc and UDP-GlcUA to chondroitin oligosaccharide acceptors in vitro. Other structurally related sugar nucleotide precursors did not substitute in the elongation reaction. Polymer molecules composed of ~103 sugar residues were produced as measured by gel filtration chromatography. The polysaccharide synthesized in vitro was sensitive to the action of chondroitin AC lyase but resistant to the action of hyaluronan lyase. This is the first report identifying a glycosyltransferase that forms a polysaccharide composed of chondroitin disaccharide repeats, [
J. Biol. Chem, 10.1074/jbc.M003385200
Submitted on April 20, 2000
Accepted on May 18, 2000
Identification and molecular cloning of a chondroitin synthase from pasteurella multocida type F
(1,4)GlcUA-(1,3)GalNAc]n. In analogy to known hyaluronan synthases, a single polypeptide species, pmCS, possesses both transferase activities.
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