Document Detail


Separate pathways for O acetylation of polymeric and monomeric sialic acids and identification of sialyl O-acetyl esterase in Escherichia coli K1.
MedLine Citation:
PMID:  16923886     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Susan M Steenbergen; Young-Choon Lee; Willie F Vann; Justine Vionnet; Lori F Wright; Eric R Vimr
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Journal of bacteriology     Volume:  188     ISSN:  0021-9193     ISO Abbreviation:  J. Bacteriol.     Publication Date:  2006 Sep 
Date Detail:
Created Date:  2006-08-22     Completed Date:  2006-10-02     Revised Date:  2013-06-07    
Medline Journal Info:
Nlm Unique ID:  2985120R     Medline TA:  J Bacteriol     Country:  United States    
Other Details:
Languages:  eng     Pagination:  6195-206     Citation Subset:  IM    
Affiliation:
Laboratory of Sialobiology, Department of Pathobiology, University of Illinois at Urbana-Champaign, 2522 VMBSB, 2001 South Lincoln Avenue, Urbana, IL 61802, USA.
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MeSH Terms
Descriptor/Qualifier:
Acetylation
Acetylesterase / analysis,  metabolism*
Acetyltransferases / analysis,  genetics,  metabolism
Amino Acid Sequence
Chromatography, Thin Layer / methods
Escherichia coli / growth & development,  metabolism*
Escherichia coli Proteins / analysis,  genetics,  metabolism*
Molecular Sequence Data
N-Acetylneuraminic Acid / metabolism*
Quinoxalines
Sequence Alignment
Grant Support
ID/Acronym/Agency:
R01 AI042015/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Escherichia coli Proteins; 0/Quinoxalines; 131-48-6/N-Acetylneuraminic Acid; EC 2.3.1.-/Acetyltransferases; EC 2.3.1.-/NeuD protein, E coli; EC 2.3.1.136/NeuO protein, E coli; EC 2.3.1.138/NeuA protein, E coli; EC 3.1.1.6/AES protein, E coli; EC 3.1.1.6/Acetylesterase
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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