Complete Nucleotide and Deduced Protein Sequence of CMP-NeuAc: Poly-alpha-2,8 Sialosyl Sialyltransferase of Escherichia Coli K1

Overview

Journal Glycobiology

Date 1991 Sep 1

PMID 1820197

Citations 6

Authors

C Weisgerber

A Hansen

M Frosch

Affiliations

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Abstract

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.

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