Escherichia coli K1 polysialic acid O-acetyltransferase gene, neuO, and the mechanism of capsule form variation involving a mobile contingency locus.

@article{Deszo2005EscherichiaCK,
  title={Escherichia coli K1 polysialic acid O-acetyltransferase gene, neuO, and the mechanism of capsule form variation involving a mobile contingency locus.},
  author={Eric L. Deszo and Susan M. Steenbergen and Dar{\'o}n I Freedberg and Eric R. Vimr},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2005},
  volume={102 15},
  pages={5564-9}
}
Potential O-acetylation of the sialic acid residues of Escherichia coli K1, groups W-135, Y, and C meningococci, and group B Streptococcus capsular polysaccharides modifies their immunogenicity and susceptibility to glycosidases. Despite the biological importance of O-acetylation, no sialic or polysialic acid O-acetyltransferase has been identified in any system. Here we show that the E. coli K1 O-acetyltransferase encoded by neuO is genetically linked to the endo-neuraminidase tail protein… CONTINUE READING
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