Found 4 structures.
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1. Compound ID: 12253
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a-D-GlcpNAc-(1-3)-+
|
/Variants 0/-a-Legp5Ac-(2-6)-+ |
| |
-4)-b-D-Galp-(1-6)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-
/Variants 0/ is:
S-3HOBut-(1-7)-
OR (exclusively)
Ac-7)- |
Show graphically |
Structure type: polymer chemical repeating unit
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_141807,IEDB_147450,IEDB_151531,IEDB_153201,IEDB_156493,IEDB_190606,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_25,SB_7,SB_8,SB_88
The structure is contained in the following publication(s):
- Article ID: 4874
Shashkov AS, Kenyon JJ, Senchenkova SN, Shneider MM, Popova AV, Arbatsky NP, Miroshnikov KA, Volozhantsev NV, Hall RM, Knirel YA "Acinetobacter baumannii K27 and K44 capsular polysaccharides have the same K unit but different structures due to the presence of distinct wzy genes in otherwise closely related K gene clusters" -
Glycobiology 26(5) (2016) 501-508
Capsular polysaccharides (CPSs), from Acinetobacter baumannii isolates 1432, 4190 and NIPH 70, which have related gene content at the K locus, were examined, and the chemical structures established using 2D(1)H and(13)C NMR spectroscopy. The three isolates produce the same pentasaccharide repeat unit, which consists of 5-N-acetyl-7-N-[(S)-3-hydroxybutanoyl] (major) or 5,7-di-N-acetyl (minor) derivatives of 5,7-diamino-3,5,7,9-tetradeoxy-D-glycero-D-galacto-non-2-ulosonic (legionaminic) acid (Leg5Ac7R), D-galactose, N-acetyl-D-galactosamine and N-acetyl-D-glucosamine. However, the linkage between repeat units in NIPH 70 was different to that in 1432 and 4190, and this significantly alters the CPS structure. The KL27 gene cluster in 4190 and KL44 gene cluster in NIPH 70 are organized identically and contain lga genes for Leg5Ac7R synthesis, genes for the synthesis of the common sugars, as well as anitrA2 initiating transferase and four glycosyltransferases genes. They share high-level nucleotide sequence identity for corresponding genes, but differ in the wzy gene encoding the Wzy polymerase. The Wzy proteins, which have different lengths and share no similarity, would form the unrelated linkages in the K27 and K44 structures. The linkages formed by the four shared glycosyltransferases were predicted by comparison with gene clusters that synthesize related structures. These findings unambiguously identify the linkages formed by WzyK27 and WzyK44, and show that the presence of different wzy genes in otherwise closely related K gene clusters changes the structure of the CPS. This may affect its capacity as a protective barrier for A. baumannii.
Acinetobacter baumannii, capsular polysaccharide, gene cluster, legionaminic acid, Wzy polymerase, K locus
NCBI PubMed ID: 26711304Publication DOI: 10.1093/glycob/cwv168Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: johanna.kenyon@qut.edu.au
Institutions: Russian Academy of Sciences, N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, School of Molecular Bioscience, The University of Sydney, Sydney, Australia School of Biomedical Sciences, Queensland University of Technology, Brisbane, Australia, Russian Academy of Sciences, M. M. Shemyakin & Y. A. Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia, Moscow Institute of Physics and Technology, Dolgoprudny, Moscow, Russia State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow, Russia
Methods: 13C NMR, 1H NMR, NMR-2D, PCR, DNA sequencing, sugar analysis, DNA techniques, ESI-MS, acid hydrolysis, GLC, mild acid hydrolysis, GPC, function analysis of gene clusters
- Article ID: 5792
Knirel YA, Shneider MM, Popova AV, Kasimova AA, Senchenkova SN, Shashkov AS, Chizhov AO "Mechanisms of Acinetobacter baumannii Capsular Polysaccharide Cleavage by Phage Depolymerases" -
Biochemistry (Moscow) 85(5) (2020) 567-574
Aerobic gram-negative bacterium Acinetobacter baumannii has recently become one of the most relevant pathogens associated with hospital-acquired infections worldwide. A. baumannii produces a capsule around the cell, which represents a thick viscous layer of structurally variable capsular polysaccharide (CPS). The capsule protects the bacteria against unfavorable environmental factors and biological systems, including bacteriophages and host immune system. Many A. baumannii phages have structural depolymerases (tailspikes) that specifically recognize and digest bacterial CPS. In this work, we studied the interaction of tailspike proteins of four lytic depolymerase-carrying phages with A. baumannii CPS. Depolymerases of three bacteriophages (Fri1, AS12, and BS46) were identified as specific glycosidases that cleave the CPS of A. baumannii strains 28, 1432, and B05, respectively, by the hydrolytic mechanism. The gp54 depolymerase from bacteriophage AP22 was characterized as a polysaccharide lyase that cleaves the CPS of A. baumannii strain 1053 by β-elimination at hexuronic acid (ManNAcA) residues.
Acinetobacter baumannii, capsular polysaccharide, NMR spectroscopy, bacteriophage, Polysaccharide lyase, Tailspike, depolymerase, glycosidase, hexuronic acid, receptor binding protein
NCBI PubMed ID: 32571186Publication DOI: 10.1134/S0006297920050053Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: yknirel@gmail.com
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow Region, 142279, Russia, Higher Chemical College of the Russian Academy of Sciences, D. I. Mendeleev University of Chemical Technology of Russia, Moscow, Russia, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia, Institute of Antimicrobial Chemotherapy, Smolensk State Medical University, Smolensk, 214019, Russia, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, Moscow Region, 141701, Russia
Methods: 13C NMR, 1H NMR, NMR-2D, DNA techniques, GPC, enzymatic digestion, HR-ESI-MS
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2. Compound ID: 14745
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a-D-GlcpNAc-(1-3)-+
|
/Variants 0/-a-Legp5Ac-(2-6)-b-D-Galp-(1-6)-b-D-Galp-(1-3)-a-D-GalpNAc
/Variants 0/ is:
S-3HOBut-(1-7)-
OR (exclusively)
Ac-7)- |
Show graphically |
Structure type: oligomer
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391963,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_143260,IEDB_151531,IEDB_153201,IEDB_156493,IEDB_190606,IEDB_885822,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_88
The structure is contained in the following publication(s):
- Article ID: 5792
Knirel YA, Shneider MM, Popova AV, Kasimova AA, Senchenkova SN, Shashkov AS, Chizhov AO "Mechanisms of Acinetobacter baumannii Capsular Polysaccharide Cleavage by Phage Depolymerases" -
Biochemistry (Moscow) 85(5) (2020) 567-574
Aerobic gram-negative bacterium Acinetobacter baumannii has recently become one of the most relevant pathogens associated with hospital-acquired infections worldwide. A. baumannii produces a capsule around the cell, which represents a thick viscous layer of structurally variable capsular polysaccharide (CPS). The capsule protects the bacteria against unfavorable environmental factors and biological systems, including bacteriophages and host immune system. Many A. baumannii phages have structural depolymerases (tailspikes) that specifically recognize and digest bacterial CPS. In this work, we studied the interaction of tailspike proteins of four lytic depolymerase-carrying phages with A. baumannii CPS. Depolymerases of three bacteriophages (Fri1, AS12, and BS46) were identified as specific glycosidases that cleave the CPS of A. baumannii strains 28, 1432, and B05, respectively, by the hydrolytic mechanism. The gp54 depolymerase from bacteriophage AP22 was characterized as a polysaccharide lyase that cleaves the CPS of A. baumannii strain 1053 by β-elimination at hexuronic acid (ManNAcA) residues.
Acinetobacter baumannii, capsular polysaccharide, NMR spectroscopy, bacteriophage, Polysaccharide lyase, Tailspike, depolymerase, glycosidase, hexuronic acid, receptor binding protein
NCBI PubMed ID: 32571186Publication DOI: 10.1134/S0006297920050053Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: yknirel@gmail.com
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow Region, 142279, Russia, Higher Chemical College of the Russian Academy of Sciences, D. I. Mendeleev University of Chemical Technology of Russia, Moscow, Russia, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia, Institute of Antimicrobial Chemotherapy, Smolensk State Medical University, Smolensk, 214019, Russia, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, Moscow Region, 141701, Russia
Methods: 13C NMR, 1H NMR, NMR-2D, DNA techniques, GPC, enzymatic digestion, HR-ESI-MS
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3. Compound ID: 14746
|
a-D-GlcpNAc-(1-3)-+
|
/Variants 0/-a-Legp5Ac-(2-6)-b-D-Galp-(1-6)-b-D-Galp-(1-3)-b-D-GalpNAc
/Variants 0/ is:
S-3HOBut-(1-7)-
OR (exclusively)
Ac-7)- |
Show graphically |
Structure type: oligomer
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_141807,IEDB_147450,IEDB_151531,IEDB_153201,IEDB_156493,IEDB_190606,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_7,SB_8,SB_88
The structure is contained in the following publication(s):
- Article ID: 5792
Knirel YA, Shneider MM, Popova AV, Kasimova AA, Senchenkova SN, Shashkov AS, Chizhov AO "Mechanisms of Acinetobacter baumannii Capsular Polysaccharide Cleavage by Phage Depolymerases" -
Biochemistry (Moscow) 85(5) (2020) 567-574
Aerobic gram-negative bacterium Acinetobacter baumannii has recently become one of the most relevant pathogens associated with hospital-acquired infections worldwide. A. baumannii produces a capsule around the cell, which represents a thick viscous layer of structurally variable capsular polysaccharide (CPS). The capsule protects the bacteria against unfavorable environmental factors and biological systems, including bacteriophages and host immune system. Many A. baumannii phages have structural depolymerases (tailspikes) that specifically recognize and digest bacterial CPS. In this work, we studied the interaction of tailspike proteins of four lytic depolymerase-carrying phages with A. baumannii CPS. Depolymerases of three bacteriophages (Fri1, AS12, and BS46) were identified as specific glycosidases that cleave the CPS of A. baumannii strains 28, 1432, and B05, respectively, by the hydrolytic mechanism. The gp54 depolymerase from bacteriophage AP22 was characterized as a polysaccharide lyase that cleaves the CPS of A. baumannii strain 1053 by β-elimination at hexuronic acid (ManNAcA) residues.
Acinetobacter baumannii, capsular polysaccharide, NMR spectroscopy, bacteriophage, Polysaccharide lyase, Tailspike, depolymerase, glycosidase, hexuronic acid, receptor binding protein
NCBI PubMed ID: 32571186Publication DOI: 10.1134/S0006297920050053Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: yknirel@gmail.com
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow Region, 142279, Russia, Higher Chemical College of the Russian Academy of Sciences, D. I. Mendeleev University of Chemical Technology of Russia, Moscow, Russia, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia, Institute of Antimicrobial Chemotherapy, Smolensk State Medical University, Smolensk, 214019, Russia, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, Moscow Region, 141701, Russia
Methods: 13C NMR, 1H NMR, NMR-2D, DNA techniques, GPC, enzymatic digestion, HR-ESI-MS
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4. Compound ID: 14747
|
a-D-GlcpNAc-(1-3)-+
|
a-D-GlcpNAc-(1-3)-+ /Variants 0/-a-Legp5Ac-(2-6)-+ |
| | |
/Variants 1/-a-Legp5Ac-(2-6)-b-D-Galp-(1-6)-b-D-Galp-(1-3)-b-D-GalpNAc-(1-4)-b-D-Galp-(1-6)-b-D-Galp-(1-3)-D-GalpNAc
/Variants 0/ is:
S-3HOBut-(1-7)-
OR (exclusively)
Ac-7)-
/Variants 1/ is:
S-3HOBut-(1-7)-
OR (exclusively)
Ac-7)- |
Show graphically |
Structure type: oligomer
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_134627,IEDB_136044,IEDB_137340,IEDB_137472,IEDB_137473,IEDB_1391961,IEDB_1391963,IEDB_141584,IEDB_141794,IEDB_141807,IEDB_143260,IEDB_147450,IEDB_151531,IEDB_153201,IEDB_156493,IEDB_190606,IEDB_885822,SB_165,SB_166,SB_187,SB_195,SB_23,SB_24,SB_25,SB_7,SB_8,SB_88
The structure is contained in the following publication(s):
- Article ID: 5792
Knirel YA, Shneider MM, Popova AV, Kasimova AA, Senchenkova SN, Shashkov AS, Chizhov AO "Mechanisms of Acinetobacter baumannii Capsular Polysaccharide Cleavage by Phage Depolymerases" -
Biochemistry (Moscow) 85(5) (2020) 567-574
Aerobic gram-negative bacterium Acinetobacter baumannii has recently become one of the most relevant pathogens associated with hospital-acquired infections worldwide. A. baumannii produces a capsule around the cell, which represents a thick viscous layer of structurally variable capsular polysaccharide (CPS). The capsule protects the bacteria against unfavorable environmental factors and biological systems, including bacteriophages and host immune system. Many A. baumannii phages have structural depolymerases (tailspikes) that specifically recognize and digest bacterial CPS. In this work, we studied the interaction of tailspike proteins of four lytic depolymerase-carrying phages with A. baumannii CPS. Depolymerases of three bacteriophages (Fri1, AS12, and BS46) were identified as specific glycosidases that cleave the CPS of A. baumannii strains 28, 1432, and B05, respectively, by the hydrolytic mechanism. The gp54 depolymerase from bacteriophage AP22 was characterized as a polysaccharide lyase that cleaves the CPS of A. baumannii strain 1053 by β-elimination at hexuronic acid (ManNAcA) residues.
Acinetobacter baumannii, capsular polysaccharide, NMR spectroscopy, bacteriophage, Polysaccharide lyase, Tailspike, depolymerase, glycosidase, hexuronic acid, receptor binding protein
NCBI PubMed ID: 32571186Publication DOI: 10.1134/S0006297920050053Journal NLM ID: 0376536Publisher: Nauka/Interperiodica
Correspondence: yknirel@gmail.com
Institutions: Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow Region, 142279, Russia, Higher Chemical College of the Russian Academy of Sciences, D. I. Mendeleev University of Chemical Technology of Russia, Moscow, Russia, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Moscow, Russia, Institute of Antimicrobial Chemotherapy, Smolensk State Medical University, Smolensk, 214019, Russia, Moscow Institute of Physics and Technology (National Research University), Dolgoprudny, Moscow Region, 141701, Russia
Methods: 13C NMR, 1H NMR, NMR-2D, DNA techniques, GPC, enzymatic digestion, HR-ESI-MS
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