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J. Biol. Chem., Vol. 275, Issue 31, 24124-24129, August 4, 2000
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From the Department of Biochemistry and Molecular Biology,
University of Oklahoma Health Sciences Center,
Oklahoma City, Oklahoma 73104
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 P. multocida chondroitin
synthase (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,
[ The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF195517.
Identification and Molecular Cloning of a Chondroitin
Synthase from Pasteurella multocida Type F*
and
(1,4)GlcUA-(1,3)GalNAc]n. In analogy to known hyaluronan synthases, a single polypeptide species, pmCS, possesses both transferase activities.
*
This work was supported by National Institutes of Health
Grant GM56497 and National Science Foundation Grant MCB-9876193 (to P. L. D.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of Biochemistry
and Molecular Biology, University of Oklahoma Health Sciences Center,
940 Stanton L. Young Blvd., Oklahoma City, OK 73104. Tel.: 405-271-2227; Fax: 405-271-3092; E-mail:
paul-deangelis@ouhsc.edu.
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