report error
Found 4 records.
Displayed records from 1 to 4
|
1. (CSDB ID: 12606) | report error |
| b-D-GlcpNAc3NAcA-(1-4)-+ | -3)-a-D-Galp-(1-6)-b-D-Glcp-(1-3)-b-D-GlcpNAc-(1- | b-D-GlcpNAc-(1-6)-+ | Show graphically |
|
Show legend Show as text |
Acinetobacter baumannii 17978 ∆pglc
(Ancestor NCBI TaxID 470,
species name lookup)
]; urinary tract infections (UTI) [ICD11: GC08 ]; infection due to Acinetobacter baumannii [ICD11: XN8LS ]
wustl.eduAcinetobacter baumannii is an opportunistic human pathogen with the highest reported rates of multidrug resistance among Gram-negative pathogens. The capsular polysaccharide of A. baumannii is considered one of its most significant virulence factors providing resistance against complemented-mediated killing. Capsule synthesis in A. baumannii is usually initiated by the phosphoglycosyltransferase PglC. PglC transfers a phosphosugar from a nucleotide diphosphate-sugar to a polyprenol phosphate generating a polyprenol diphosphate-linked monosaccharide. Traditionally, PglC was thought to have stringent specificity towards UDP-N-N'-diacetylbacillosamine (UDP-diNAcBac). In this work we demonstrate that A. baumannii PglC has the ability to utilize three different UDP-sugar substrates: UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-N-acetylgalactosamine (UDP-GalNAc) or UDP-diNAcBac. Using phylogenetic analyses, we first demonstrate that A. baumannii PglC orthologs separate into three distinct clades. Moreover, all members within a clade are predicted to have the same preference for one of the three possible sugar substrates. To experimentally determine the substrate specificity of each clade, we utilized in vivo complementation models and NMR analysis. We demonstrate that UDP-diNAcBac is accommodated by all PglC orthologs, but some orthologs evolved to utilize UDP-GlcNAc or UDP-GalNAc in a clade-dependent manner. Furthermore, we show that a single point mutation can modify the sugar specificity of a PglC ortholog specific for UDP-diNAcBac and that introduction of a non-native PglC ortholog into A. baumannii can generate a new capsule serotype. Collectively, these studies begin to explain why A. baumannii strains have such highly diverse glycan repertoires.
serotype, Acinetobacter baumannii, capsular polysaccharide, capsule, PglC, phosphoglycosyltransferase
Structure type: polymer chemical repeating unit|
2. (CSDB ID: 12607) | report error |
| a-D-Glcp-(1-6)-+ | -2)-b-D-Galf-(1-6)-a-D-Glcp-(1-3)-a-L-Rhap2Ac-(1-3)-a-D-GlcpNAc-(1- | Show graphically |
|
Show legend Show as text |
Escherichia coli O16
(NCBI TaxID 1010799,
species name lookup)
Escherichia coli CLM37 ΔwecA
(Ancestor NCBI TaxID 562,
species name lookup)
]wustl.eduAcinetobacter baumannii is an opportunistic human pathogen with the highest reported rates of multidrug resistance among Gram-negative pathogens. The capsular polysaccharide of A. baumannii is considered one of its most significant virulence factors providing resistance against complemented-mediated killing. Capsule synthesis in A. baumannii is usually initiated by the phosphoglycosyltransferase PglC. PglC transfers a phosphosugar from a nucleotide diphosphate-sugar to a polyprenol phosphate generating a polyprenol diphosphate-linked monosaccharide. Traditionally, PglC was thought to have stringent specificity towards UDP-N-N'-diacetylbacillosamine (UDP-diNAcBac). In this work we demonstrate that A. baumannii PglC has the ability to utilize three different UDP-sugar substrates: UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-N-acetylgalactosamine (UDP-GalNAc) or UDP-diNAcBac. Using phylogenetic analyses, we first demonstrate that A. baumannii PglC orthologs separate into three distinct clades. Moreover, all members within a clade are predicted to have the same preference for one of the three possible sugar substrates. To experimentally determine the substrate specificity of each clade, we utilized in vivo complementation models and NMR analysis. We demonstrate that UDP-diNAcBac is accommodated by all PglC orthologs, but some orthologs evolved to utilize UDP-GlcNAc or UDP-GalNAc in a clade-dependent manner. Furthermore, we show that a single point mutation can modify the sugar specificity of a PglC ortholog specific for UDP-diNAcBac and that introduction of a non-native PglC ortholog into A. baumannii can generate a new capsule serotype. Collectively, these studies begin to explain why A. baumannii strains have such highly diverse glycan repertoires.
serotype, Acinetobacter baumannii, capsular polysaccharide, capsule, PglC, phosphoglycosyltransferase
Structure type: suggested polymer biological repeating unit|
3. (CSDB ID: 12608) | report error |
| b-D-QuipNAc4NAc-(1-7)-L-gro-a-D-manHepp-(1-6)-a-D-Glcp-(1-2)-a-D-Glcp-(1-3)-a-D-Glcp | Show graphically |
|
Show legend Show as text |
Escherichia coli K-12
(NCBI TaxID 83333,
species name lookup)
Escherichia coli CLM37 PglC
(Ancestor NCBI TaxID 562,
species name lookup)
]wustl.eduAcinetobacter baumannii is an opportunistic human pathogen with the highest reported rates of multidrug resistance among Gram-negative pathogens. The capsular polysaccharide of A. baumannii is considered one of its most significant virulence factors providing resistance against complemented-mediated killing. Capsule synthesis in A. baumannii is usually initiated by the phosphoglycosyltransferase PglC. PglC transfers a phosphosugar from a nucleotide diphosphate-sugar to a polyprenol phosphate generating a polyprenol diphosphate-linked monosaccharide. Traditionally, PglC was thought to have stringent specificity towards UDP-N-N'-diacetylbacillosamine (UDP-diNAcBac). In this work we demonstrate that A. baumannii PglC has the ability to utilize three different UDP-sugar substrates: UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-N-acetylgalactosamine (UDP-GalNAc) or UDP-diNAcBac. Using phylogenetic analyses, we first demonstrate that A. baumannii PglC orthologs separate into three distinct clades. Moreover, all members within a clade are predicted to have the same preference for one of the three possible sugar substrates. To experimentally determine the substrate specificity of each clade, we utilized in vivo complementation models and NMR analysis. We demonstrate that UDP-diNAcBac is accommodated by all PglC orthologs, but some orthologs evolved to utilize UDP-GlcNAc or UDP-GalNAc in a clade-dependent manner. Furthermore, we show that a single point mutation can modify the sugar specificity of a PglC ortholog specific for UDP-diNAcBac and that introduction of a non-native PglC ortholog into A. baumannii can generate a new capsule serotype. Collectively, these studies begin to explain why A. baumannii strains have such highly diverse glycan repertoires.
serotype, Acinetobacter baumannii, capsular polysaccharide, capsule, PglC, phosphoglycosyltransferase
Structure type: fragment of a bigger structure|
4. (CSDB ID: 12909) | report error |
| b-D-GlcpNAc3NAcA-(1-4)-+ | -6)-b-D-Glcp-(1-3)-b-D-GalpNAc-(1-3)-a-D-Galp-(1- | b-D-GlcpNAc-(1-6)-+ | Show graphically |
|
Show legend Show as text |
Acinetobacter baumannii 17978
(Ancestor NCBI TaxID 470,
species name lookup)
]; urinary tract infections (UTI) [ICD11: GC08 ]; infection due to Acinetobacter baumannii [ICD11: XN8LS ]wustl.eduAcinetobacter baumannii is an opportunistic human pathogen with the highest reported rates of multidrug resistance among Gram-negative pathogens. The capsular polysaccharide of A. baumannii is considered one of its most significant virulence factors providing resistance against complemented-mediated killing. Capsule synthesis in A. baumannii is usually initiated by the phosphoglycosyltransferase PglC. PglC transfers a phosphosugar from a nucleotide diphosphate-sugar to a polyprenol phosphate generating a polyprenol diphosphate-linked monosaccharide. Traditionally, PglC was thought to have stringent specificity towards UDP-N-N'-diacetylbacillosamine (UDP-diNAcBac). In this work we demonstrate that A. baumannii PglC has the ability to utilize three different UDP-sugar substrates: UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-N-acetylgalactosamine (UDP-GalNAc) or UDP-diNAcBac. Using phylogenetic analyses, we first demonstrate that A. baumannii PglC orthologs separate into three distinct clades. Moreover, all members within a clade are predicted to have the same preference for one of the three possible sugar substrates. To experimentally determine the substrate specificity of each clade, we utilized in vivo complementation models and NMR analysis. We demonstrate that UDP-diNAcBac is accommodated by all PglC orthologs, but some orthologs evolved to utilize UDP-GlcNAc or UDP-GalNAc in a clade-dependent manner. Furthermore, we show that a single point mutation can modify the sugar specificity of a PglC ortholog specific for UDP-diNAcBac and that introduction of a non-native PglC ortholog into A. baumannii can generate a new capsule serotype. Collectively, these studies begin to explain why A. baumannii strains have such highly diverse glycan repertoires.
serotype, Acinetobacter baumannii, capsular polysaccharide, capsule, PglC, phosphoglycosyltransferase
Structure type: polymer chemical repeating unit| New query | Export IDs | Home | Help |
Execution: <1 sec