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Complete nucleotide and deduced protein sequence of CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase of Escherichia coli K1.
Institute für Medizinische Mikrobiologie, Medizinische Hochschule Hannover, FRG.
Poly-alpha-2,8 N-acetylneuraminic acid (polySia) is an important virulence factor in infections caused by Escherichia coli K1 and Neisseria meningitidis B. In E. coli K1 a membranous CMP-NeuAc: poly-alpha-2,8 sialosyl sialyltransferase (polysialyltransferase) complex catalyses the synthesis of linear polySia chains. The complex also elongates sialyl oligomers that serve as exogenous acceptors. The gene encoding a polysialyltransferase of E. coli has been identified by subcloning and DNA sequence analysis. The subcloned DNA fragment codes for a polypeptide with a molecular mass of 47 kDa catalysing the in vitro synthesis of polySia by elongation of exogenous acceptors.
PMID: 1820197 [PubMed - indexed for MEDLINE]
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Cited by 6 PubMed Central articles
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Biochemical characterization of a Neisseria meningitidis polysialyltransferase reveals novel functional motifs in bacterial sialyltransferases.
Freiberger F, Claus H, Günzel A, Oltmann-Norden I, Vionnet J, Mühlenhoff M, Vogel U, Vann WF, Gerardy-Schahn R, Stummeyer K.
Mol Microbiol. 2007 Sep; 65(5):1258-75. Epub 2007 Jul 27.
[Mol Microbiol. 2007]
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Genes associated with meningococcal capsule complex are also found in Neisseria gonorrhoeae.
Petering H, Hammerschmidt S, Frosch M, van Putten JP, Ison CA, Robertson BD.
J Bacteriol. 1996 Jun; 178(11):3342-5.
[J Bacteriol. 1996]
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Molecular cloning and analysis of genes for sialic acid synthesis in Neisseria meningitidis group B and purification of the meningococcal CMP-NeuNAc synthetase enzyme.
Ganguli S, Zapata G, Wallis T, Reid C, Boulnois G, Vann WF, Roberts IS.
J Bacteriol. 1994 Aug; 176(15):4583-9.
[J Bacteriol. 1994]
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