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1. (CSDB ID: 39) | report error |
| -3)-a-L-Rhap-(1-3)-a-L-Rhap-(1-2)-a-L-Rhap-(1-2)-a-L-Rhap-(1-2)-a-L-Rhap-(1- | Show graphically |
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Klebsiella pneumoniae 6
(Ancestor NCBI TaxID 573,
species name lookup)
]A strain of Klebsiella pneumoniae was found as the only isolate with pathogenic potential from the stool of a two-year old patient with diarrhoea. A strong serological cross-reactivity with Shigella flexneri serotype 6 was demonstrated. The cross-reacting antigens were shown to reside in the cell wall lipopolysaccharide. Studies of the pathogenic potential of the Klebsiella strain showed low level of invasion of HEp-2 cells. However, tests for adherence to HEp-2 cells as well as tests for toxin production were negative. The strain had several small plasmids and was multidrug resistant. These data do not form a sufficient basis for estimating the pathogenic potential of the organism. No K antigen was detected. The structure of the O-antigenic polysaccharide from the K. pneumoniae strain was investigated using methylation analysis, NMR spectroscopy, and Smith degradation as the principal methods. The O-antigenic polysaccharide has the following pentasaccharide repeating unit: -3)aLRhap(1-3)aLRhap(1-2)aLRhap(1-2)aLRhap(1-2)aLRhap(1-. This structure is not identical to any of the previously described O-antigens of K. pneumoniae. The strong serological cross-reactivity with the Shigella flexneri serotype 6 O-antigen can most likely be attributed to the structural element a-L-Rhap-(l→2)-a-L-Rhap present in the O-polysaccharide repeating unit of this serotype. Antiserum raised against the K. pneumoniae strain also agglutinated S. dysenteriae serotype 1 and strains of all different serotypes of S. flexneri. The Shigella strains contain the structural element a-L-Rhap-(l→3)-a-L-Rhap in their O-antigen polysaccharides which may be responsible for the observed cross-reactivity.
Lipopolysaccharide, antigen, O-antigenic polysaccharide, Shigella flexneri, Klebsiella pneumoniae, type-specific
Structure type: polymer chemical repeating unit|
2. (CSDB ID: 119) | report error |
| a-L-Rhap-(1-3)-a-L-Rhap-(1-2)-Gro | Show graphically |
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Klebsiella pneumoniae
(NCBI TaxID 573,
species name lookup)
]A strain of Klebsiella pneumoniae was found as the only isolate with pathogenic potential from the stool of a two-year old patient with diarrhoea. A strong serological cross-reactivity with Shigella flexneri serotype 6 was demonstrated. The cross-reacting antigens were shown to reside in the cell wall lipopolysaccharide. Studies of the pathogenic potential of the Klebsiella strain showed low level of invasion of HEp-2 cells. However, tests for adherence to HEp-2 cells as well as tests for toxin production were negative. The strain had several small plasmids and was multidrug resistant. These data do not form a sufficient basis for estimating the pathogenic potential of the organism. No K antigen was detected. The structure of the O-antigenic polysaccharide from the K. pneumoniae strain was investigated using methylation analysis, NMR spectroscopy, and Smith degradation as the principal methods. The O-antigenic polysaccharide has the following pentasaccharide repeating unit: -3)aLRhap(1-3)aLRhap(1-2)aLRhap(1-2)aLRhap(1-2)aLRhap(1-. This structure is not identical to any of the previously described O-antigens of K. pneumoniae. The strong serological cross-reactivity with the Shigella flexneri serotype 6 O-antigen can most likely be attributed to the structural element a-L-Rhap-(l→2)-a-L-Rhap present in the O-polysaccharide repeating unit of this serotype. Antiserum raised against the K. pneumoniae strain also agglutinated S. dysenteriae serotype 1 and strains of all different serotypes of S. flexneri. The Shigella strains contain the structural element a-L-Rhap-(l→3)-a-L-Rhap in their O-antigen polysaccharides which may be responsible for the observed cross-reactivity.
Lipopolysaccharide, antigen, O-antigenic polysaccharide, Shigella flexneri, Klebsiella pneumoniae, type-specific
Structure type: oligomer|
3. (CSDB ID: 7322) | report error |
| a-D-Glcp-(1-3)-b-L-Fucp-(1--/MIC2 (micronemal protein 2)/ | Show graphically |
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Toxoplasma gondii
(NCBI TaxID 5811,
species name lookup)
, ICD11: XN896 ]
wehi.edu.au; goddard-borger.ewehi.edu.au; nichollas.scottunimelb.edu.auToxoplasma gondii is a ubiquitous, obligate intracellular eukaryotic parasite that causes congenital birth defects, disease in immunocompromised individuals, and blindness. Protein glycosylation plays an important role in the infectivity and evasion of immune responses of many eukaryotic parasites and is also of great relevance to vaccine design. Here we demonstrate that micronemal protein 2 (MIC2), a motility-associated adhesin of T. gondii, has highly glycosylated thrombospondin repeat (TSR) domains. Using affinity-purified MIC2 and MS/MS analysis along with enzymatic digestion assays, we observed that at least seven C-linked and three O-linked glycosylation sites exist within MIC2, with >95% occupancy at these O-glycosylation sites. We found that addition of O-glycans to MIC2 is mediated by a protein O-fucosyltransferase 2 homolog (TgPOFUT2) encoded by the TGGT1_273550 gene. Even though POFUT2 homologs are important for stabilizing motility-associated adhesins and for host infection in other apicomplexan parasites, loss of TgPOFUT2 in T. gondii had only a modest impact on MIC2 levels and the wider parasite proteome. Consistent with this, both plaque formation and tachyzoite invasion were broadly similar in the presence or absence of TgPOFUT2. These findings indicate that TgPOFUT2 O-glycosylates MIC2 and that this glycan, in contrast to previous findings in another study, is dispensable in T. gondii tachyzoites and for T. gondii infectivity.
MS, glycosylation, fucosyltransferase, Proteomics, Toxoplasma gondii
Structure type: oligomer|
4. (CSDB ID: 8154) | report error |
| a-D-Manp-(1--/MIC2 (micronemal protein 2)/ | Show graphically |
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Toxoplasma gondii
(NCBI TaxID 5811,
species name lookup)
, ICD11: XN896 ]wehi.edu.au; goddard-borger.ewehi.edu.au; nichollas.scottunimelb.edu.auToxoplasma gondii is a ubiquitous, obligate intracellular eukaryotic parasite that causes congenital birth defects, disease in immunocompromised individuals, and blindness. Protein glycosylation plays an important role in the infectivity and evasion of immune responses of many eukaryotic parasites and is also of great relevance to vaccine design. Here we demonstrate that micronemal protein 2 (MIC2), a motility-associated adhesin of T. gondii, has highly glycosylated thrombospondin repeat (TSR) domains. Using affinity-purified MIC2 and MS/MS analysis along with enzymatic digestion assays, we observed that at least seven C-linked and three O-linked glycosylation sites exist within MIC2, with >95% occupancy at these O-glycosylation sites. We found that addition of O-glycans to MIC2 is mediated by a protein O-fucosyltransferase 2 homolog (TgPOFUT2) encoded by the TGGT1_273550 gene. Even though POFUT2 homologs are important for stabilizing motility-associated adhesins and for host infection in other apicomplexan parasites, loss of TgPOFUT2 in T. gondii had only a modest impact on MIC2 levels and the wider parasite proteome. Consistent with this, both plaque formation and tachyzoite invasion were broadly similar in the presence or absence of TgPOFUT2. These findings indicate that TgPOFUT2 O-glycosylates MIC2 and that this glycan, in contrast to previous findings in another study, is dispensable in T. gondii tachyzoites and for T. gondii infectivity.
MS, glycosylation, fucosyltransferase, Proteomics, Toxoplasma gondii
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