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1. (CSDB ID: 23738) | report error |
| -4)-b-L-GalpNAc3NAcA6(17%)NH2-(1- | Show graphically |
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Bordetella bronchiseptica RB50
(NCBI TaxID 257310,
species name lookup)
]; infection due to Bordetella bronchiseptica [ICD11: XN173 ]
gmail.comBordetella bronchiseptica is a pathogen of humans and animals that colonizes the respiratory tract. It produces a lipopolysaccharide O antigen that contains a homopolymer of 2,3-dideoxy-2,3-diacetamido-l-galacturonic acid (l-GalNAc3NAcA). Some of these sugars are found in the uronamide form (l-GalNAc3NAcAN), and there is no discernible pattern in the distribution of amides along the chain. A B. bronchiseptica wbmE mutant expresses an O polysaccharide unusually rich in uronamides. The WbmE protein localizes to the periplasm and catalyzes the deamidation of uronamide-rich O chains in lipopolysaccharide purified from the mutant, to attain a wild-type uronamide/uronic acid ratio. WbmE is a member of the papain-like transglutaminase superfamily, and this categorization is consistent with a deamidase role. The periplasmic location of WbmE and its acceptance of complete lipopolysaccharide as substrate indicate that it operates at a late stage in lipopolysaccharide biosynthesis, after polymerization and export of the O chain from the cytoplasm. This is the first report of such a modification of O antigen after assembly. The expression of wbmE is controlled by the Bordetella virulence gene two-component regulatory system, BvgAS, suggesting that this deamidation is a novel mechanism by which these bacteria modify their cell surface charge in response to environmental stimuli.
lipopolysaccharide biosynthesis, O polysaccharide, modification, Bordetella bronchiseptica, periplasm, WbmE
Structure type: homopolymer|
2. (CSDB ID: 24025) | report error |
| Lac2Me-(1-4)-{{{-b-L-GalpNAc3NAcA6(%)NH2-(1-4)-}}}b-D-ManpNAc3NAcA6NH2-(1-4)-b-D-GlcpNAc3NAcA6NH2-(1-4)-a-D-GalpNAc-(1-4)-b-D-ManpNAc3NAcA-(1-3)-b-D-FucpNAc4NMe-(1-6)-a-D-GlcpNAc-(1-4)-b-D-ManpNAc3NAcA-(1-3)-b-D-FucpNAc4NMe-(1-6)-a-D-GlcpN-(1--/core oligosaccharide/ | Show graphically |
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Bordetella bronchiseptica
(NCBI TaxID 518,
species name lookup)
]; infection due to Bordetella bronchiseptica [ICD11: XN173 ]gmail.comBordetella bronchiseptica is a pathogen of humans and animals that colonizes the respiratory tract. It produces a lipopolysaccharide O antigen that contains a homopolymer of 2,3-dideoxy-2,3-diacetamido-l-galacturonic acid (l-GalNAc3NAcA). Some of these sugars are found in the uronamide form (l-GalNAc3NAcAN), and there is no discernible pattern in the distribution of amides along the chain. A B. bronchiseptica wbmE mutant expresses an O polysaccharide unusually rich in uronamides. The WbmE protein localizes to the periplasm and catalyzes the deamidation of uronamide-rich O chains in lipopolysaccharide purified from the mutant, to attain a wild-type uronamide/uronic acid ratio. WbmE is a member of the papain-like transglutaminase superfamily, and this categorization is consistent with a deamidase role. The periplasmic location of WbmE and its acceptance of complete lipopolysaccharide as substrate indicate that it operates at a late stage in lipopolysaccharide biosynthesis, after polymerization and export of the O chain from the cytoplasm. This is the first report of such a modification of O antigen after assembly. The expression of wbmE is controlled by the Bordetella virulence gene two-component regulatory system, BvgAS, suggesting that this deamidation is a novel mechanism by which these bacteria modify their cell surface charge in response to environmental stimuli.
lipopolysaccharide biosynthesis, O polysaccharide, modification, Bordetella bronchiseptica, periplasm, WbmE
Structure type: oligomer| New query | Export IDs | Home | Help |
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