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Taxonomic group: bacteria / Firmicutes (Phylum: Firmicutes)

Publication DOI: 10.1093/glycob/cwv087
Journal NLM ID: 9104124
Publisher: IRL Press at Oxford University Press
Correspondence: C.S. <christina.schaeffer

boku.ac.at>; D.K. <daniel.kolarich

mpikg.mpg.de>
Institutions: Institute of Chemistry and Biochemistry, Freie Universitat Berlin, Arnimallee 22, Berlin 14195, Germany, Department of Chemistry, Division of Biochemistry, Universitat fur Bodenkultur Wien, Muthgasse 18, Vienna A-1190, Austria, Department of Biomolecular Systems, Max Planck Institute of Colloids and Interfaces, Potsdam 14424, Germany, Department of NanoBiotechnology, NanoGlycobiology Unit, Universitat fur Bodenkultur Wien, Muthgasse 11, Vienna A-1190, Austria

Flagellin glycosylation impacts, in several documented cases, the functionality of bacterial flagella. The basis of flagellin glycosylation has been studied for various Gram-negative bacteria, but less is known about flagellin glycans of Gram-positive bacteria including Paenibacillus alvei, a secondary invader of honeybee colonies diseased with European foulbrood. Paenibacillus alvei CCM 2051(T) swarms vigorously on solidified culture medium, with swarming relying on functional flagella as evidenced by abolished biofilm formation of a non-motile P. alvei mutant defective in the flagellin protein Hag. Here, the glycobiology of the polar P. alvei flagella was investigated. Analysis on purified flagellin demonstrated that the 30-kDa Hag protein (PAV_2c01710) is modified with an O-linked trisaccharide comprised of one hexose and two N-acetyl-hexosamine residues, at three sites of glycosylation. Downstream of the hag gene on the bacterial chromosome, two open reading frames (PAV_2c01630, PAV_2c01640) encoding putative glycosyltransferases were shown to constitute a flagellin glycosylation island. Mutants defective in these genes exhibited altered migration in sodium dodecyl sulfate polyacrylamide gel electrophoresis as well as loss of extracellular flagella production and bacterial motility. This study reveals that flagellin glycosylation in P. alvei is pivotal to flagella formation and bacterial motility in vivo, and simultaneously identifies flagella glycosylation as a second protein O-glycosylation system in this bacterium, in addition to the well-investigated S-layer tyrosine O-glycosylation pathway.

trisaccharide, Self-assembly, Paenibacillus alvei, Glycoproteomics, flagellum, glycosylation island, protein O-glycosylation

Structure type: polymer chemical repeating unit ; n=23
Location inside paper: p.75
Compound class: S-layer glycan
Contained glycoepitopes: IEDB_136044,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_885813,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

Methods: SDS-PAGE, DNA techniques, MALDI-TOF MS, genetic methods, electron microscopy, glycoproteomics analysis, nanoLC-ESI-IT-MS/MS
Comments, role: repeating units, part of structure S-layer glycan (see ID: 11643)

Related record ID(s): 11643
NCBI Taxonomy refs (TaxIDs): 44250
Reference(s) to other database(s): GTC:G08485BS
Show glycosyltransferases

There is only one chemically distinct structure:

[*]O[C@@H]1[C@@H](O)[C@H](O[C@@H]2[C@@H](CO[C@H]3O[C@H](CO)[C@@H](O)[C@H](O)[C@H]3O)O[C@@H]([*])[C@@H](NC(C)=O)[C@H]2O)O[C@H](CO)[C@@H]1O

SVG MW SMILES 3D mol Ionize

boku.ac.at>; D.K. <daniel.kolarich

trisaccharide, Self-assembly, Paenibacillus alvei, Glycoproteomics, flagellum, glycosylation island, protein O-glycosylation

Structure type: oligomer
Location inside paper: p.75
Compound class: S-layer glycan
Contained glycoepitopes: IEDB_136044,IEDB_136105,IEDB_137472,IEDB_141794,IEDB_142488,IEDB_144998,IEDB_146664,IEDB_190606,IEDB_225177,IEDB_885813,IEDB_885823,IEDB_983931,SB_165,SB_166,SB_187,SB_192,SB_195,SB_7,SB_88

Methods: SDS-PAGE, DNA techniques, MALDI-TOF MS, genetic methods, electron microscopy, glycoproteomics analysis, nanoLC-ESI-IT-MS/MS
Comments, role: an adapter saccharide, part of structure S-layer glycan (see ID: 11272)

Related record ID(s): 11272
NCBI Taxonomy refs (TaxIDs): 44250
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@@H]1[C@H](O[C@@H]2[C@@H](O[C@@H]3O[C@H](CO)[C@@H](OP(=O)(O)OC(CO)C(=O)O)[C@H](O)[C@@H]3NC(C)=O)[C@H](C)O[C@@H](O[C@@H]3[C@@H](O)[C@H](C)O[C@@H](O[C@@H]4[C@@H](O)[C@H](C)O[C@@H](O[C@H]5[C@@H](O)[C@@H](CO)O[C@@H](O)[C@@H]5O)[C@@H]4O)[C@@H]3O)[C@@H]2O)O[C@H](CO[C@H]2O[C@H](CO)[C@@H](O)[C@H](O)[C@H]2O)[C@@H](O[C@@H]2O[C@H](CO)[C@H](O)[C@H](O[C@@H]3O[C@H](CO[C@H]4O[C@H](CO)[C@@H](O)[C@H](O)[C@H]4O)[C@@H](O[C@@H]4O[C@H](CO)[C@H](O)[C@H](O[C@@H]5O[C@H](CO[C@H]6O[C@H](CO)[C@@H](O)[C@H](O)[C@H]6O)[C@@H](O[C@@H]6O[C@H](CO)[C@H](O)[C@H](O[C@@H]7O[C@H](CO[C@H]8O[C@H](CO)[C@@H](O)[C@H](O)[C@H]8O)[C@@H](O[C@@H]8O[C@H](CO)[C@H](O)[C@H](O[C@@H]9O[C@H](CO[C@H]%10O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%10O)[C@@H](O[C@@H]%10O[C@H](CO)[C@H](O)[C@H](O[C@@H]%11O[C@H](CO[C@H]%12O[C@H](CO)[C@@H](O)[C@H](O)[C@H]%12O)[C@@H](O[C@@H]%12O[C@H](CO)[C@H](O)[C@H](O)[C@H]%12O)[C@H](O)[C@@H]%11NC(C)=O)[C@H]%10O)[C@H](O)[C@@H]9NC(C)=O)[C@H]8O)[C@H](O)[C@@H]7NC(C)=O)[C@H]6O)[C@H](O)[C@@H]5NC(C)=O)[C@H]4O)[C@H](O)[C@@H]3NC(C)=O)[C@H]2O)[C@@H]1O

SVG MW SMILES 3D mol Ionize

Warning = sub-repeat ending at bDManpN: large unit count (22) was reduced to 5