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J. Biol. Chem., Vol. 278, Issue 17, 15349-15359, April 25, 2003
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From the Laboratory of Sialobiology, Department of Pathobiology,
University of Illinois, Urbana, Illinois 61802
Polysialic acid (PSA) capsules are
cell-associated homopolymers of The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EBI Data Bank with accession number(s) AF318310, M76370, M88479, AF432602, and U75650.
Functional Relationships of the Sialyltransferases
Involved in Expression of the Polysialic Acid Capsules of
Escherichia coli K1 and K92 and Neisseria
meningitidis Groups B or C*
2,8-, 2,9-, or alternating
2,8/2,9-linked sialic acid residues that function as essential
virulence factors in neuroinvasive diseases caused by certain strains
of Escherichia coli and Neisseria meningitidis.
PSA chains structurally identical to the bacterial 2,8-linked
capsular polysaccharides are also synthesized by the mammalian central
nervous system, where they regulate neuronal function in association
with the neural cell adhesion molecule (NCAM). Despite the structural
identity between bacterial and NCAM PSAs, the respective
polysialyltransferases (polySTs) responsible for polymerizing sialyl
residues from donor CMP-sialic acid are not homologous
glycosyltransferases. To better define the mechanism of capsule
biosynthesis, we established the functional interchangeability of
bacterial polySTs by complementation of a polymerase-deficient E. coli K1 mutant with the polyST genes from groups B or C N. meningitidis and the control E. coli K92 polymerase
gene. The biochemical and immunochemical results demonstrated that
linkage specificity is dictated solely by the source of the polymerase structural gene. To determine the molecular basis for linkage specificity, we created chimeras of the K1 and K92 polySTs by overlap
extension PCR. Exchanging the first 52 N-terminal amino acids of the K1
NeuS with the C terminus of the K92 homologue did not alter specificity
of the resulting chimera, whereas exchanging the first 85 or
reciprocally exchanging the first 100 residues did. These results
demonstrated that linkage specificity is dependent on residues located
between positions 53 and 85 from the N terminus. Site-directed
mutagenesis of the K92 polyST N terminus indicated that no single
residue alteration was sufficient to affect specificity, consistent
with the proposed function of this domain in orienting the acceptor.
The combined results provide the first evidence for residues critical
to acceptor binding and elongation in polysialyltransferase.
*
This work was supported by National Institutes of Health
Grant RO1-AI42015 (to E. R. V.).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: Laboratory of
Sialobiology, Division of Microbiology and Immunology, Dept. of Pathobiology, University of Illinois, 2001 South Lincoln Ave., Urbana,
IL 61802. Tel.: 217-333-8502; Fax: 217-244-7421; E-mail: e-vimr@uiuc.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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