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Taxonomic group: bacteria / Proteobacteria (Phylum: Proteobacteria)
Host organism: Gallus; Bos taurus
Associated disease: fowl cholera [ICD11: XN30D

]; bovine hemorrhagic septicemia; swine atrophic rhinitis; infection due to Pasteurella multocida [ICD11: XN30D

]

NCBI PubMed ID: 19168738
Journal NLM ID: 0246127
Publisher: American Society for Microbiology
Correspondence: Ben.Adler

med.monash.edu.au
Institutions: Australian Research Council Centre of Excellence in Structural and Functional Microbial Genomics, Monash University, Melbourne, Australia

We previously determined the structure of the Pasteurella multocida Heddleston type 1 lipopolysaccharide (LPS) molecule and characterized some of the transferases essential for LPS biosynthesis. We also showed that P. multocida strains expressing truncated LPS display reduced virulence. Here, we have identified all of the remaining glycosyltransferases required for synthesis of the oligosaccharide extension of the P. multocida Heddleston type 1 LPS, including a novel α-1,6 glucosyltransferase, a β-1,4 glucosyltransferase, a putative bifunctional galactosyltransferase, and two heptosyltransferases. In addition, we identified a novel oligosaccharide extension expressed only in a heptosyltransferase (hptE) mutant background. All of the analyzed mutants expressing LPS with a truncated main oligosaccharide extension displayed reduced virulence, but those expressing LPS with an intact heptose side chain were able to persist for long periods in muscle tissue. The hptC mutant, which expressed LPS with the shortest oligosaccharide extension and no heptose side chain, was unable to persist on the muscle or cause any disease. Furthermore, all of the mutants displayed increased sensitivity to the chicken antimicrobial peptide fowlicidin 1, with mutants expressing highly truncated LPS being the most sensitive

Lipopolysaccharide, biosynthesis, virulence, glycosyltransferases, Pasteurella multocida, chickens

Structure type: oligomer
Location inside paper: p.1533, fig.1, A
Aglycon: lipid A
Compound class: LPS
Contained glycoepitopes: IEDB_120354,IEDB_123890,IEDB_130648,IEDB_130650,IEDB_130651,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_137777,IEDB_137779,IEDB_138949,IEDB_1391961,IEDB_1391964,IEDB_140087,IEDB_140088,IEDB_140090,IEDB_141582,IEDB_141584,IEDB_141794,IEDB_142487,IEDB_142488,IEDB_144987,IEDB_144998,IEDB_146664,IEDB_151528,IEDB_152217,IEDB_153207,IEDB_153208,IEDB_190606,IEDB_2189047,IEDB_423106,IEDB_423127,IEDB_742247,IEDB_885822,IEDB_983931,SB_165,SB_166,SB_167,SB_178,SB_187,SB_192,SB_195,SB_21,SB_31,SB_6,SB_62,SB_7,SB_88

Methods: 13C NMR, 1H NMR, methylation, GLC-MS, ESI-MS, composition analysis, genetic methods, CE-MS, mild hydrazinolysis
Biological activity: virulence
Biosynthesis and genetic data: genetic data

Related record ID(s): 23973, 23974, 23975
NCBI Taxonomy refs (TaxIDs): 747
Reference(s) to other database(s): GTC:G18787AM
Show glycosyltransferases

There is only one chemically distinct structure:

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

SVG MW SMILES 3D mol Ionize