Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Escherichia coli [ICD11:
XN6P4 
];
infection due to Shigella flexneri [ICD11:
XN7Y2 ]
The structure was elucidated in this paperNCBI PubMed ID: 20546712Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: A.V. Perepelov <perepel
ioc.ac.ru>
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia
O-Polysaccharides (O-antigens) were isolated from Escherichia coli O13, O129, and O135 and studied by chemical analyses along with 2D (1)H and (13)C NMR spectroscopy. They were found to possess a common →2)-l-Rha-(α1→2)-l-Rha-(α1→3)-l-Rha-(α1→3)-d-GlcNAc-(β1→ backbone, which is a characteristic structural motif of the O-polysaccharides of Shigella flexneri types 1-5. In both the bacterial species, the backbone is decorated with lateral glucose residues or/and O-acetyl groups. In E. coli O13, a new site of glycosylation on 3-substituted Rha was revealed and the following O-polysaccharide structure was established: The structure of the E. coli O129 antigen was found to be identical to the O-antigen structure of S. flexneri type 5a specified in this work and that of E. coli O135 to S. flexneri type 4b reported earlier.
O-antigen, Escherichia coli, Shigella flexneri, O-acetylation, bacterial polysaccharide structure, Glucosylation site
Structure type: suggested polymer biological repeating unit
Location inside paper: abstract, p.1597,chart 1
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_125613,IEDB_125614,IEDB_127514,IEDB_130422,IEDB_133752,IEDB_133753,IEDB_133754,IEDB_135813,IEDB_135849,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_141815,IEDB_141816,IEDB_142488,IEDB_143253,IEDB_144998,IEDB_146664,IEDB_151531,IEDB_153213,IEDB_225177,IEDB_885823,IEDB_983931,SB_192
Methods: 13C NMR, 1H NMR, NMR-2D, sugar analysis, acid hydrolysis, GLC, de-O-acetylation
Related record ID(s): 329, 23916, 24173, 25391, 25804
NCBI Taxonomy refs (TaxIDs): 2184073,
623Reference(s) to other database(s): GTC:G36735BW, GlycomeDB:
37319
Show glycosyltransferases
NMR conditions: in D2O at 313 K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
3,3,2 aLRhap 102.4 80.0 71.1 73.6 69.6 18.0
3,3 aLRhap 102.4 79.3 71.3 73.3 70.7 17.7
3,2 Ac 174.3 21.6
3 aLRhap 99.7 73.6 77.5 73.0 70.4 17.9
2 Ac 175.9 23.8
6 aDGlcp 99.5 72.9 74.5 71.0 73.3 62.0
bDGlcpN 103.6 56.9 83.2 70.7 75.7 67.2
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6
3,3,2 aLRhap 5.09 4.13 3.86 3.30 3.66 1.23
3,3 aLRhap 5.09 4.02 3.74 3.44 3.57 1.27
3,2 Ac - 2.17
3 aLRhap 4.91 5.01 3.94 3.59 4.07 1.26
2 Ac - 2.05
6 aDGlcp 4.97 3.55 3.74 3.41 3.71 3.76-3.86
bDGlcpN 4.74 3.86 3.62 3.67 3.62 3.78-3.96
1H/13C HSQC data:
Linkage Residue C1/H1 C2/H2 C3/H3 C4/H4 C5/H5 C6/H6
3,3,2 aLRhap 102.4/5.09 80.0/4.13 71.1/3.86 73.6/3.30 69.6/3.66 18.0/1.23
3,3 aLRhap 102.4/5.09 79.3/4.02 71.3/3.74 73.3/3.44 70.7/3.57 17.7/1.27
3,2 Ac 21.6/2.17
3 aLRhap 99.7/4.91 73.6/5.01 77.5/3.94 73.0/3.59 70.4/4.07 17.9/1.26
2 Ac 23.8/2.05
6 aDGlcp 99.5/4.97 72.9/3.55 74.5/3.74 71.0/3.41 73.3/3.71 62.0/3.76-3.86
bDGlcpN 103.6/4.74 56.9/3.86 83.2/3.62 70.7/3.67 75.7/3.62 67.2/3.78-3.96
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 |
|---|
| 3,3,2 | aLRhap | 5.09 | 4.13 | 3.86 | 3.30 | 3.66 | 1.23 |
| 3,3 | aLRhap | 5.09 | 4.02 | 3.74 | 3.44 | 3.57 | 1.27 |
| 3,2 | Ac |
| 2.17 | |
| 3 | aLRhap | 4.91 | 5.01 | 3.94 | 3.59 | 4.07 | 1.26 |
| 2 | Ac |
| 2.05 | |
| 6 | aDGlcp | 4.97 | 3.55 | 3.74 | 3.41 | 3.71 | 3.76
3.86 |
| | bDGlcpN | 4.74 | 3.86 | 3.62 | 3.67 | 3.62 | 3.78
3.96 |
|
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
|---|
| 3,3,2 | aLRhap | 102.4 | 80.0 | 71.1 | 73.6 | 69.6 | 18.0 |
| 3,3 | aLRhap | 102.4 | 79.3 | 71.3 | 73.3 | 70.7 | 17.7 |
| 3,2 | Ac | 174.3 | 21.6 | |
| 3 | aLRhap | 99.7 | 73.6 | 77.5 | 73.0 | 70.4 | 17.9 |
| 2 | Ac | 175.9 | 23.8 | |
| 6 | aDGlcp | 99.5 | 72.9 | 74.5 | 71.0 | 73.3 | 62.0 |
| | bDGlcpN | 103.6 | 56.9 | 83.2 | 70.7 | 75.7 | 67.2 |
|
There is only one chemically distinct structure:
Found 
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