Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: pneumonia [ICD11:
CA40 
];
urinary tract infections (UTI) [ICD11:
GC08 ];
liver abscess [ICD11:
DB90.0 , ICD11:
SA04 ];
infection due to Klebsiella pneumoniae [ICD11:
XN741 ]
The structure was elucidated in this paperNCBI PubMed ID: 38139119Publication DOI: 10.3390/ijms242417288Journal NLM ID: 101092791Publisher: Basel, Switzerland: MDPI
Correspondence: A.A. Lukianova <a.al.lukianova
gmail.com>; M.M. Shneider <mm_shn
mail.ru>
Institutions: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Miklukho-Maklaya Str. 16/10, 117997 Moscow, Russia, Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Leninsky prosp. 47, 119991 Moscow, Russia, Lopukhin Federal Research and Clinical Center of Physical-Chemical Medicine, Federal Medical Biological Agency, Malaya Pirogovskaya Str. 1, 119435 Moscow, Russia
Klebsiella pneumoniae is a pathogen associated with various infection types, which often exhibits multiple antibiotic resistance. Phages, or bacterial viruses, have an ability to specifically target and destroy K. pneumoniae, offering a potential means of combatting multidrug-resistant infections. Phage enzymes are another promising therapeutic agent that can break down bacterial capsular polysaccharide, which shields K. pneumoniae from the immune response and external factors. In this study, Klebsiella phage K5 was isolated; this phage is active against Klebsiella pneumoniae with the capsular type K21. It was demonstrated that the phage can effectively lyse the host culture. The adsorption apparatus of the phage has revealed two receptor-binding proteins (RBPs) with predicted polysaccharide depolymerising activity. A recombinant form of both RBPs was obtained and experiments showed that one of them depolymerised the capsular polysaccharide K21. The structure of this polysaccharide and its degradation fragments were analysed. The second receptor-binding protein showed no activity on capsular polysaccharide of any of the 31 capsule types tested, so the substrate for this enzyme remains to be determined in the future. Klebsiella phage K5 may be considered a useful agent against Klebsiella infections.
capsular polysaccharide, Klebsiella pneumoniae, bacteriophage, phage depolymerases
Structure type: polymer chemical repeating unit
Location inside paper: table 2, Fig. 9, K21 CPS
Compound class: CPS, EPS
Contained glycoepitopes: IEDB_115136,IEDB_130701,IEDB_136044,IEDB_136104,IEDB_136906,IEDB_137472,IEDB_140630,IEDB_141794,IEDB_143632,IEDB_144983,IEDB_151528,IEDB_151770,IEDB_152206,IEDB_190606,IEDB_983930,SB_136,SB_165,SB_166,SB_187,SB_195,SB_196,SB_44,SB_67,SB_7,SB_72,SB_88
Methods: 13C NMR, 1H NMR, depyruvation, NMR-2D, PCR, sugar analysis, DNA techniques, GLC, Smith degradation, HPLC, GPC, phylogenetic analysis, HR-ESI-MS, phage characterization, genome analysis, genome sequencing, annotation, VIRIDIC analysis
Comments, role: published polymerization frame was shifted for conformity with other records; published erroneous NMR chemical shift of C4 #2_aDManp (74.5) was removed by CSDB staff.
Related record ID(s): 25966, 25967, 25968, 25969
NCBI Taxonomy refs (TaxIDs): 573
Show glycosyltransferases
NMR conditions: in D2O at 328 K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
2,3,3 bDGalp 104.2 71.2 77.8 65.9 76.4 62.3
2,3,4,6 xRPyr 176.3 101.6 26.4
2,3,4 aDGalp 100.7 69.5 69.2 72.6 63.9 66.1
2,3 aDGlcpA 101.5 73.2 80.5 71.3 74.1 175.1
2 aDManp 103.3 70.9 79.6 ? 74.6 62.3
aDManp 95.9 80.3 71.4 68.3 76.8 62.3
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6
2,3,3 bDGalp 4.85 3.66 3.76 4.13 3.64 3.87
2,3,4,6 xRPyr - - 1.44
2,3,4 aDGalp 5.50 3.88 3.84 4.17 3.72 3.85-3.98
2,3 aDGlcpA 5.25 3.87 4.31 3.92 4.21 -
2 aDManp 5.02 4.19 3.91 3.79 3.71 3.74-3.85
aDManp 5.23 4.01 3.97 3.68 3.90 3.74-3.85
1H/13C HSQC data:
Linkage Residue C1/H1 C2/H2 C3/H3 C4/H4 C5/H5 C6/H6
2,3,3 bDGalp 104.2/4.85 71.2/3.66 77.8/3.76 65.9/4.13 76.4/3.64 62.3/3.87
2,3,4,6 xRPyr 26.4/1.44
2,3,4 aDGalp 100.7/5.50 69.5/3.88 69.2/3.84 72.6/4.17 63.9/3.72 66.1/3.85-3.98
2,3 aDGlcpA 101.5/5.25 73.2/3.87 80.5/4.31 71.3/3.92 74.1/4.21
2 aDManp 103.3/5.02 70.9/4.19 79.6/3.91 ?/3.79 74.6/3.71 62.3/3.74-3.85
aDManp 95.9/5.23 80.3/4.01 71.4/3.97 68.3/3.68 76.8/3.90 62.3/3.74-3.85
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 |
|---|
| 2,3,3 | bDGalp | 4.85 | 3.66 | 3.76 | 4.13 | 3.64 | 3.87 |
| 2,3,4,6 | xRPyr |
|
| 1.44 | |
| 2,3,4 | aDGalp | 5.50 | 3.88 | 3.84 | 4.17 | 3.72 | 3.85
3.98 |
| 2,3 | aDGlcpA | 5.25 | 3.87 | 4.31 | 3.92 | 4.21 |
|
| 2 | aDManp | 5.02 | 4.19 | 3.91 | 3.79 | 3.71 | 3.74
3.85 |
| | aDManp | 5.23 | 4.01 | 3.97 | 3.68 | 3.90 | 3.74
3.85 |
|
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
|---|
| 2,3,3 | bDGalp | 104.2 | 71.2 | 77.8 | 65.9 | 76.4 | 62.3 |
| 2,3,4,6 | xRPyr | 176.3 | 101.6 | 26.4 | |
| 2,3,4 | aDGalp | 100.7 | 69.5 | 69.2 | 72.6 | 63.9 | 66.1 |
| 2,3 | aDGlcpA | 101.5 | 73.2 | 80.5 | 71.3 | 74.1 | 175.1 |
| 2 | aDManp | 103.3 | 70.9 | 79.6 | ? | 74.6 | 62.3 |
| | aDManp | 95.9 | 80.3 | 71.4 | 68.3 | 76.8 | 62.3 |
|
![](nmr_drawer.py?width=750&height=130&nucleus=C&rotate_labels=false&spectrum=[{"s":104.2,"l":"1","c":[0,0,225]},{"s":71.2,"l":"2","c":[0,0,225]},{"s":77.8,"l":"3","c":[0,0,225]},{"s":65.9,"l":"4","c":[0,0,225]},{"s":76.4,"l":"5","c":[0,0,225]},{"s":62.3,"l":"6","c":[0,0,225]},{"s":176.3,"l":"1","c":[230,0,30]},{"s":101.6,"l":"2","c":[230,0,30]},{"s":26.4,"l":"3","c":[230,0,30]},{"s":100.7,"l":"1","c":[0,165,0]},{"s":69.5,"l":"2","c":[0,165,0]},{"s":69.2,"l":"3","c":[0,165,0]},{"s":72.6,"l":"4","c":[0,165,0]},{"s":63.9,"l":"5","c":[0,165,0]},{"s":66.1,"l":"6","c":[0,165,0]},{"s":101.5,"l":"1","c":[120,0,225]},{"s":73.2,"l":"2","c":[120,0,225]},{"s":80.5,"l":"3","c":[120,0,225]},{"s":71.3,"l":"4","c":[120,0,225]},{"s":74.1,"l":"5","c":[120,0,225]},{"s":175.1,"l":"6","c":[120,0,225]},{"s":103.3,"l":"1","c":[0,192,255]},{"s":70.9,"l":"2","c":[0,192,255]},{"s":79.6,"l":"3","c":[0,192,255]},{"s":74.6,"l":"5","c":[0,192,255]},{"s":62.3,"l":"6","c":[0,192,255]},{"s":95.9,"l":"1","c":[220,0,180]},{"s":80.3,"l":"2","c":[220,0,180]},{"s":71.4,"l":"3","c":[220,0,180]},{"s":68.3,"l":"4","c":[220,0,180]},{"s":76.8,"l":"5","c":[220,0,180]},{"s":62.3,"l":"6","c":[220,0,180]}])
The spectrum also has 1 signal at unknown position (not plotted). |
There is only one chemically distinct structure:
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Found 1 record.
Displayed record 1
