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1. (CSDB ID: 23658) | report error |
| L-gro-a-D-manHepp-(1-2)-+ | EtN-(1--P--3)--L-gro-a-D-manHepp-(1-3)-+ | b-D-Glcp-(1-4)-+ | EtN-(1---P---P---4)-+ | | | a-D-GalpNAc-(1-3)-b-D-GalpNAc-(1-3)-a-D-Galp-(1-4)-b-D-Galp-(1-4)-b-D-Glcp-(1-6)-L-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ | a-D-Glcp-(1-6)-+ | Show graphically |
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Pasteurella multocida Pm70
(Ancestor NCBI TaxID 747,
species name lookup)
]; bovine hemorrhagic septicemia; swine atrophic rhinitis; infection due to Pasteurella multocida [ICD11: XN30D ]
med.monash.edu.auWe 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|
2. (CSDB ID: 23973) | report error |
| EtN-(1-0)-?%P---P--4)-+ | L-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-+ | | | Cho-(1--P--3)--b-D-Galp-(1-6)-+ | | | | | Cho-(1--P--3)--b-D-Galp-(1-4)-L-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ | a-D-Glcp-(1-6)-+ | Show graphically |
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Pasteurella multocida VP161
(Ancestor NCBI TaxID 747,
species name lookup)
]; bovine hemorrhagic septicemia; swine atrophic rhinitis; infection due to Pasteurella multocida [ICD11: XN30D ]med.monash.edu.auWe 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|
3. (CSDB ID: 23974) | report error |
| L-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-+ | Cho-(1--P--3)--b-D-Galp-(1-6)-+ | a-Kdop-(2-4)-+ | | | Cho-(1--P--3)--b-D-Galp-(1-4)-L-gro-a-D-manHepp-(1-6)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ | Show graphically |
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Pasteurella multocida VP161
(Ancestor NCBI TaxID 747,
species name lookup)
]; bovine hemorrhagic septicemia; swine atrophic rhinitis; infection due to Pasteurella multocida [ICD11: XN30D ]med.monash.edu.auWe 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|
4. (CSDB ID: 23975) | report error |
| L-gro-a-D-manHepp-(1-2)-L-gro-a-D-manHepp-(1-3)-+ a-Kdop-(2-4)-+ | | b-D-Galp-(1-4)-b-D-GlcpNAc-(1-3)-b-D-Galp-(1-3)-b-D-GlcpNAc-(1-4)-b-D-Glcp-(1-4)-L-gro-a-D-manHepp-(1-5)-a-Kdop-(2--/lipid A/ | Show graphically |
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Pasteurella multocida VP161 hptE
(Ancestor NCBI TaxID 747,
species name lookup)
]; bovine hemorrhagic septicemia; swine atrophic rhinitis; infection due to Pasteurella multocida [ICD11: XN30D ]med.monash.edu.auWe 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
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