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| Content Provider | PubMed Central |
|---|---|
| Author | Steenbergen, Susan M. Lee, Young-choon Vann, Willie F. Vionnet, Justine Wright, Lori F. Vimr, Eric R. |
| Copyright Year | 2006 |
| Abstract | O acetylation at carbon positions 7 or 9 of the sialic acid residues in the polysialic acid capsule of Escherichia coli K1 is catalyzed by a phase-variable contingency locus, neuO, carried by the K1-specific prophage, CUS-3. Here we describe a novel method for analyzing polymeric sialic acid O acetylation that involves the release of surface sialic acids by endo-N-acetylneuraminidase digestion, followed by fluorescent labeling and detection of quinoxalinone derivatives by chromatography. The results indicated that NeuO is responsible for the majority of capsule modification that takes place in vivo. However, a minor neuO-independent O acetylation pathway was detected that is dependent on the bifunctional polypeptide encoded by neuD. This pathway involves O acetylation of monomeric sialic acid and is regulated by another bifunctional enzyme, NeuA, which includes N-terminal synthetase and C-terminal sialyl O-esterase domains. A homologue of the NeuA C-terminal domain (Pm1710) in Pasteurella multocida was also shown to be an esterase, suggesting that it functions in the catabolism of acetylated environmental sialic acids. Our combined results indicate a previously unexpected complexity in the synthesis and catabolism of microbial sialic and polysialic acids. These findings are key to understanding the biological functions of modified sialic acids in E. coli K1 and other species and may provide new targets for drug or vaccine development. |
| Related Links | http://dx.doi.org/10.1128/jb.00466-06 |
| Ending Page | 6206 |
| Page Count | 12 |
| Starting Page | 6195 |
| File Format | |
| ISSN | 00219193 |
| e-ISSN | 10985530 |
| Journal | Journal of Bacteriology |
| Issue Number | 17 |
| Volume Number | 188 |
| Language | English |
| Publisher | American Society for Microbiology |
| Publisher Date | 2006-09-01 |
| Access Restriction | Open |
| Rights Holder | American Society for Microbiology |
| Subject Keyword | Molecular Biology Microbiology Research in Higher Education |
| Content Type | Text |
| Resource Type | Article |
| Subject | Molecular Biology Microbiology |
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