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TranscriptomicsH. pylori G27 HP0518 mutant showed greater motility
Helicobacter pylori is a human gastric pathogen associated with gastric and duodenal ulcers as well as specific gastric cancers. It is well-evidenced that motility is essential for this pathogen to colonize human gastric tissues. We found that the H. pylori G27 HP0518 mutant showed greater motility ...
ORGANISM(S): Helicobacter pylori 
2010-12-22 | E-GEOD-14752 | biostudies-arrayexpress
ProteomicsGlycoproteomics of Flagellin C9LY14 from Selenomonas sputigena
The Gram-negative, flagellated, anaerobic, crescent-shaped bacterium Selenomonas sputigena is a potential human periodontal pathogen. Information on its virulence factors and underlying pathogenicity mechanisms is scarce. Here we show for the first time that S. sputigena produces a diversely and hea...
ORGANISM(S): Escherichia coli Selenomonas sputigena ATCC 35185 
2018-01-24 | PXD005859 | Pride
Lc-msms Glycoproteomics Flagellin glycosylation Glycomics Periodontitis Selenomonas sputigena 
ProteomicsEvolution of paralogous multicomponent systems for site-specific O-sialylation of flagellin in Gram-negative and Gram-positive bacteria
Many bacteria decorate flagellin with sialic acid-like sugars such as pseudaminic acid (Pse) by O-glycosylation on serine or threonine residues. Evidence for sufficiency of sialylation by a conserved flagellin glycosyltransferase (fGT) system is lacking, presumably because of (a) missing component(s...
ORGANISM(S): Shewanella oneidensis (strain MR-1) Caulobacter crescentus (strain NA1000 / CB15N) 
2024-06-18 | PXD051215 | Pride
Pseudaminic acid Bacteria Glfm O-glycosylation Flagellin Maf 
ProteomicsIdentification of O-glycosylation sites in Clostridium botulinum and Geobacillus kaustophilus flagellins
In this study, we identified the O-glycosylation sites in recombinant Clostridium botulinum flagellin (CbFla) and Geobacillus kaustophilus flagellins, GkFlaA1 and GkFlaA2, expressed from the E. coli strains, EV136 and EV240 (K1:K12 strains engineered by Prof. Eric Vimr’s group to accumulate CMP-sial...
ORGANISM(S): Clostridium botulinum F str. Langeland Geobacillus kaustophilus HTA426 
2020-09-07 | PXD018167 | Pride
Ltq orbitrap velos pro ion-trap mass spectrometer Nonulosonic acid O-glycosylation Neu5ac Sialic acid Kdo Clostridium botulinum Gram positive Flagellin Geobacillus kaustophilus Maf 
UnknownFlagellin glycosylation in Paenibacillus alvei CCM 2051T.
Not available
S-EPMC5110117 | biostudies-literature
ProteomicsHarnessing the acceptor substrate promiscuity of Clostridium botulinum Maf glycosyltransferase to glyco-engineer mini-flagellin protein chimeras
In this study, we identified the O-glycosylation sites in deletion constructs of recombinant Clostridium botulinum flagellin (CbFla) expressed from the E. coli strain, EV136 (K1:K12 strains engineered by Prof. Eric Vimr’s group to accumulate CMP-sialic acid in the cytosol). The recombinant flagellin...
ORGANISM(S): Clostridium botulinum str. LANGELAN F 
2024-08-22 | PXD044191 | Pride
Ltq orbitrap velos pro ion-trap mass spectrometer Nonulosonic acid O-glycosylation Neu5ac Sialic acid Kdo Clostridium botulinum Gram positive Flagellin Geobacillus kaustophilus Maf 
UnknownA genomic island in Pseudomonas aeruginosa carries the determinants of flagellin glycosylation.
Not available
S-EPMC55422 | biostudies-literature
ProteomicsRe-annotated role of beta-Galactosidase in Flagellin deglycosylation
Most Eukaryotes recognise flagellin as a signature of bacterial invasion. In contrast to animals, plants do not recognise flagellin proteins, but conserved peptides released from flagellin (Felix et al., 1999). However, these peptides (e.g. flg22) are folded and buried deeply inside the flagellin po...
ORGANISM(S): Nicotiana benthamiana Pseudomonas syringae pv. tomato 
2019-04-15 | PXD010461 | Pride
Viosamine Beta-galactosidase O-glycosylation Pseudomonas syringae Flagellin 
UnknownComparative genomic analysis of the flagellin glycosylation island of the Gram-positive thermophile Geobacillus.
Not available
S-EPMC5109656 | biostudies-literature
UnknownIdentification of the flagellin glycosylation system in Burkholderia cenocepacia and the contribution of glycosylated flagellin to evasion of human innate immune responses.
Not available
S-EPMC4081957 | biostudies-literature
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