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J Biol Chem, Vol. 273, Issue 14, 8454-8458, April 3, 1998
From the Department of Biochemistry and Molecular Biology,
University of Oklahoma Health Sciences Center, Oklahoma City, Oklahoma
73104 and the § Department of Biochemistry and Molecular
Biology, University of Arkansas for Medical Sciences,
Little Rock, Arkansas 72205
Type A Pasteurella multocida, a
prevalent animal pathogen, employs a hyaluronan [HA] polysaccharide
capsule to avoid host defenses. We utilized transposon insertional
mutagenesis to identify the P. multocida HA synthase, the
enzyme that polymerizes HA. A DNA fragment from a wild-type genomic
library could direct HA production in vivo in
Escherichia coli, a bacterium that normally does not
produce HA. Analysis of truncated plasmids derived from the original
clone indicated that an open reading frame encoding a 972-residue
protein was responsible for HA polymerization. This identification was
confirmed by expression cloning in E. coli; we observed HA
capsule formation in vivo and detected activity in membrane
preparations in vitro. The polypeptide size was verified by
photoaffinity labeling of the native P. multocida HA
synthase with azido-UDP sugar analogs. Overall, the P. multocida sequence is not very similar to the other known HA
synthases from streptococci, PBCV-1 virus, or vertebrates. Instead, a
portion of the central region of the new enzyme is more homologous to
the amino termini of other bacterial glycosyltransferases that produce
different capsular polysaccharides or lipopolysaccharides. In summary,
we have discovered a unique HA synthase that differs in sequence and
predicted topology from the other known enzymes.
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