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Journal of Bacteriology, September 2006, p. 6195-6206, Vol. 188, No. 17
0021-9193/06/$08.00+0     doi:10.1128/JB.00466-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Separate Pathways for O Acetylation of Polymeric and Monomeric Sialic Acids and Identification of Sialyl O-Acetyl Esterase in Escherichia coli K1

Susan M. Steenbergen,1 Young-Choon Lee,1,2 Willie F. Vann,3 Justine Vionnet,3 Lori F. Wright,4 and Eric R. Vimr1*

Laboratory of Sialobiology and Comparative Metabolomics, Department of Pathobiology, University of Illinois at Urbana-Champaign, Urbana, Illinois,1 Department of Biotechnology, Dong-A University, Busan, South Korea,2 Center for Biologics Evaluation and Research, U.S. Food and Drug Administration, Bethesda, Maryland,3 Department of Microbiology and Immunology, University of Rochester, Rochester, New York4

Received 4 April 2006/ Accepted 15 June 2006

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.

* Corresponding author. Mailing address: Laboratory of Sialobiology, Department of Pathobiology, University of Illinois at Urbana-Champaign, 2522 VMBSB, 2001 South Lincoln Avenue, Urbana, IL 61802. Phone: (217) 244-7421. Fax: (217) 333-8502. E-mail: ervimr{at}uiuc.edu.

Journal of Bacteriology, September 2006, p. 6195-6206, Vol. 188, No. 17
0021-9193/06/$08.00+0     doi:10.1128/JB.00466-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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