Document Detail

Protein glycosylation in Helicobacter pylori: beyond the flagellins?
MedLine Citation:
PMID:  21984942     Owner:  NLM     Status:  MEDLINE    
Glycosylation of flagellins by pseudaminic acid is required for virulence in Helicobacter pylori. We demonstrate that, in H. pylori, glycosylation extends to proteins other than flagellins and to sugars other than pseudaminic acid. Several candidate glycoproteins distinct from the flagellins were detected via ProQ-emerald staining and DIG- or biotin- hydrazide labeling of the soluble and outer membrane fractions of wild-type H. pylori, suggesting that protein glycosylation is not limited to the flagellins. DIG-hydrazide labeling of proteins from pseudaminic acid biosynthesis pathway mutants showed that the glycosylation of some glycoproteins is not dependent on the pseudaminic acid glycosylation pathway, indicating the existence of a novel glycosylation pathway. Fractions enriched in glycoprotein candidates by ion exchange chromatography were used to extract the sugars by acid hydrolysis. High performance anion exchange chromatography with pulsed amperometric detection revealed characteristic monosaccharide peaks in these extracts. The monosaccharides were then identified by LC-ESI-MS/MS. The spectra are consistent with sugars such as 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid (Pse5Ac7Ac) previously described on flagellins, 5-acetamidino-7-acetamido-3,5,7,9-tetradeoxy-L-glycero-L-manno-nonulosonic acid (Pse5Am7Ac), bacillosamine derivatives and a potential legionaminic acid derivative (Leg5AmNMe7Ac) which were not previously identified in H. pylori. These data open the way to the study of the mechanism and role of protein glycosylation on protein function and virulence in H. pylori.
Patrick S Hopf; Rachel S Ford; Najwa Zebian; Alexandra Merkx-Jacques; Somalinga Vijayakumar; Dinath Ratnayake; Jacqueline Hayworth; Carole Creuzenet
Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2011-09-30
Journal Detail:
Title:  PloS one     Volume:  6     ISSN:  1932-6203     ISO Abbreviation:  PLoS ONE     Publication Date:  2011  
Date Detail:
Created Date:  2011-10-10     Completed Date:  2012-03-05     Revised Date:  2013-06-27    
Medline Journal Info:
Nlm Unique ID:  101285081     Medline TA:  PLoS One     Country:  United States    
Other Details:
Languages:  eng     Pagination:  e25722     Citation Subset:  IM    
Infectious Diseases Research Group, Department of Microbiology and Immunology, The University of Western Ontario, London, Ontario, Canada.
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MeSH Terms
Bacterial Proteins / chemistry,  metabolism*
Chromatography, Ion Exchange
Helicobacter pylori / metabolism*
Sialic Acids / metabolism
Spectrometry, Mass, Electrospray Ionization
Grant Support
MOP-62775//Canadian Institutes of Health Research
Reg. No./Substance:
0/5,7-diacetamido-3,5,7,9-tetradeoxynon-2-ulosonic acid; 0/Bacterial Proteins; 0/Sialic Acids

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

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