Document Detail


Sialic Acid metabolism and systemic pasteurellosis.
MedLine Citation:
PMID:  15731025     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Pasteurella multocida subsp. multocida is a commensal and opportunistic pathogen of food animals, wildlife, and pets and a zoonotic cause of human infection arising from contacts with these animals. Here, an investigation of multiple serotype A strains demonstrated the occurrence of membrane sialyltransferase. Although P. multocida lacks the genes for the two earliest steps in de novo sialic acid synthesis, adding sialic acid to the growth medium resulted in uptake, activation, and subsequent transfer of sialic acid to a membrane acceptor resembling lipooligosaccharide. Two candidate-activating enzymes with homology to Escherichia coli cytidine 5'-monophospho-N-acetylneuraminate synthetase were overproduced as histidine-tagged polypeptides. The synthetase encoded by pm0187 was at least 37 times more active than the pm1710 gene product, suggesting pm0187 encodes the primary sialic acid cytidylyltransferase in P. multocida. A sialate aldolase (pm1715) mutant unable to initiate dissimilation of internalized sialic acid was not attenuated in the CD-1 mouse model of systemic pasteurellosis, indicating that the nutritional function of sialate catabolism is not required for systemic disease. In contrast, the attenuation of a sialate uptake-deficient mutant supports the essential role in pathogenesis of a sialylation mechanism that is dependent on an environmental (host) supply of sialic acid. The combined results provide the first direct evidence of sialylation by a precursor scavenging mechanism in pasteurellae and of a potential tripartite ATP-independent periplasmic sialate transporter in any species.
Authors:
Susan M Steenbergen; Carol A Lichtensteiger; Ruth Caughlan; Jackie Garfinkle; Troy E Fuller; Eric R Vimr
Related Documents :
1213985 - Characterization of two glycoasparagines isolated from the urine of patients with aspar...
10372965 - Acidic glycosphingolipids of cock testis elucidated by mass spectrometry and nmr spectr...
4748825 - Kinetic studies on the acid hydrolysis of the methyl ketoside of unsubstituted and o-ac...
7535695 - The filamentous brush border glycocalyx, a mucin-like marker of enterocyte hyper-polari...
17325385 - On the mechanism of cerebral accumulation of cholestanol in patients with cerebrotendin...
22028855 - Lipoteichoic acid in streptomyces hygroscopicus: structural model and immunomodulatory ...
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, P.H.S.    
Journal Detail:
Title:  Infection and immunity     Volume:  73     ISSN:  0019-9567     ISO Abbreviation:  Infect. Immun.     Publication Date:  2005 Mar 
Date Detail:
Created Date:  2005-02-25     Completed Date:  2005-04-01     Revised Date:  2013-06-09    
Medline Journal Info:
Nlm Unique ID:  0246127     Medline TA:  Infect Immun     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1284-94     Citation Subset:  IM    
Affiliation:
Laboratory of Sialobiology, Department of Pathobiology, Universityof Illinois at Urbana-Champaign, Urbana, IL 61802, USA.
Export Citation:
APA/MLA Format     Download EndNote     Download BibTex
MeSH Terms
Descriptor/Qualifier:
Animals
Animals, Outbred Strains
Cattle
Cytidine Monophosphate N-Acetylneuraminic Acid / metabolism
Disease Models, Animal
Female
Fructose-Bisphosphate Aldolase / genetics,  metabolism
Humans
Mice
Open Reading Frames / genetics
Pasteurella Infections / metabolism*,  microbiology
Pasteurella multocida / enzymology*,  genetics,  pathogenicity*
Sialic Acids / metabolism*
Sialyltransferases / genetics,  metabolism*
Virulence
Grant Support
ID/Acronym/Agency:
2R01 AI42015/AI/NIAID NIH HHS
Chemical
Reg. No./Substance:
0/Sialic Acids; 3063-71-6/Cytidine Monophosphate N-Acetylneuraminic Acid; EC 2.4.99.-/Sialyltransferases; EC 4.1.2.13/Fructose-Bisphosphate Aldolase
Comments/Corrections

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


Previous Document:  Vibrio parahaemolyticus disruption of epithelial cell tight junctions occurs independently of toxin ...
Next Document:  The StcE protease contributes to intimate adherence of enterohemorrhagic Escherichia coli O157:H7 to...