Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: diarrhea [ICD11:
ME05.1 
, ICD11:
SA55 ]
The structure was elucidated in this paperNCBI PubMed ID: 22230711Publication DOI: 10.1016/j.carres.2011.12.012Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: olga.ovchinnikova
gmail.com
Institutions: N.D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, Department of Immunobiology of Bacteria, Institute of Microbiology, Biotechnology and Immunology, University of Lodz, PL 90-237 Lodz, Poland
An acidic polysaccharide was isolated from Providencia rustigianii O11 by the phenol-water extraction. The polysaccharide was cleaved by solvolysis with triflic acid to yield disaccharides with uronic acid derivatives at the non-reducing end. The polysaccharide and the disaccharides were studied by chemical analyses, high-resolution ESI MS, and 2D (1)H and (13)C NMR spectroscopy, and the following structure of the tetrasaccharide repeating unit of the polysaccharide was established: where GalNAcA stands for 2-acetamido-2-deoxygalacturonic acid, GalNAcA6GluAla for N-(2-acetamido-2-deoxygalacturonoyl)-l-glutam-1-yl-l-alanine, QuiNAc4NAcyl for 2-acetamido-4-[(S)-3-hydroxybutanoylamino]-2,4,6-trideoxyglucose (~75%) or 2,4-diacetamido-2,4,6-trideoxyglucose (~25%); the d configuration of GalNA and QuiN4N was ascribed tentatively. To the best of our knowledge, this is for the first time that an amide of uronic acid with a dipeptide is found in bacterial polysaccharides.
Lipopolysaccharide, bacterial polysaccharide structure, Providencia rustigianii, 2-acetamido-2-deoxygalacturonamide, dipeptide
Structure type: polymer chemical repeating unit
Location inside paper: abstract, p.100, chart 2
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_885822
Methods: 13C NMR, 1H NMR, GLC-MS, NMR-2D, de-O-acylation, ESI-MS, acid hydrolysis, composition analysis, methanolysis, GPC, triflic acid solvolysis
Comments, role: the D configuration of GalNA and QuiN4N was ascribed tentatively
Related record ID(s): 28542, 28543, 28544, 28545, 28546, 28547, 28548, 28549, 28550, 28551, 31084
NCBI Taxonomy refs (TaxIDs): 158850
Show glycosyltransferases
NMR conditions: in D2O at 333 K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
3,2 Ac 174.7-175.9 23.3-23.9
3,4,4,6,1 xLAla? 177.4 50.1 17.6
3,4,4,6 xLGlu 173.6 53.6 27.8 31.1 178.1
3,4,4,2 Ac 174.7-175.9 23.3-23.9
3,4,4 aDGalpNA 99.5 51.0 68.3 70.1 72.8 172.4
3,4,2 Ac 174.7-175.9 23.3-23.9
3,4 aDGalpN 97.3 51.1 67.6 77.1 71.7 60.6
3 aDGalpNA 98.0 49.0 75.1 75.7 71.3 ?
2 Ac 174.7-175.9 23.3-23.9
bDQuipN4N 103.1 55.8 76.0 58.2 72.1 18.1
4 25%Ac 174.7-175.9 23.3-23.9
4 75%lS3HOBut ? 46.1 65.9 23.6
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6
3,2 Ac - 1.90-2.13
3,4,4,6,1 xLAla? - 4.37 1.42
3,4,4,6 xLGlu - 4.48 2.01-2.18 2.50 -
3,4,4,2 Ac - 1.90-2.13
3,4,4 aDGalpNA 5.16 4.29 4.10 4.33 4.97 -
3,4,2 Ac - 1.90-2.13
3,4 aDGalpN 5.05 4.20 4.02 4.19 4.48 3.69-3.81
3 aDGalpNA 5.19 4.35 3.78 4.59 4.17 -
2 Ac - 1.90-2.13
bDQuipN4N 4.47 3.81 3.85 3.83 3.45 1.21
4 25%Ac - 1.90-2.13
4 75%lS3HOBut - 2.33 4.15 1.20
1H/13C HSQC data:
Linkage Residue C1/H1 C2/H2 C3/H3 C4/H4 C5/H5 C6/H6
3,2 Ac 23.3-23.9/1.90-2.13
3,4,4,6,1 xLAla? 50.1/4.37 17.6/1.42
3,4,4,6 xLGlu 53.6/4.48 27.8/2.01-2.18 31.1/2.50
3,4,4,2 Ac 23.3-23.9/1.90-2.13
3,4,4 aDGalpNA 99.5/5.16 51.0/4.29 68.3/4.10 70.1/4.33 72.8/4.97
3,4,2 Ac 23.3-23.9/1.90-2.13
3,4 aDGalpN 97.3/5.05 51.1/4.20 67.6/4.02 77.1/4.19 71.7/4.48 60.6/3.69-3.81
3 aDGalpNA 98.0/5.19 49.0/4.35 75.1/3.78 75.7/4.59 71.3/4.17
2 Ac 23.3-23.9/1.90-2.13
bDQuipN4N 103.1/4.47 55.8/3.81 76.0/3.85 58.2/3.83 72.1/3.45 18.1/1.21
4 25%Ac 23.3-23.9/1.90-2.13
4 75%lS3HOBut 46.1/2.33 65.9/4.15 23.6/1.20
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 |
|---|
| 3,2 | Ac |
| 1.90
2.13 | |
| 3,4,4,6,1 | xLAla? |
| 4.37 | 1.42 | |
| 3,4,4,6 | xLGlu |
| 4.48 | 2.01
2.18 | 2.50 |
| |
| 3,4,4,2 | Ac |
| 1.90
2.13 | |
| 3,4,4 | aDGalpNA | 5.16 | 4.29 | 4.10 | 4.33 | 4.97 |
|
| 3,4,2 | Ac |
| 1.90
2.13 | |
| 3,4 | aDGalpN | 5.05 | 4.20 | 4.02 | 4.19 | 4.48 | 3.69
3.81 |
| 3 | aDGalpNA | 5.19 | 4.35 | 3.78 | 4.59 | 4.17 |
|
| 2 | Ac |
| 1.90
2.13 | |
| | bDQuipN4N | 4.47 | 3.81 | 3.85 | 3.83 | 3.45 | 1.21 |
| 4 | 25%Ac |
| 1.90
2.13 | |
| 4 | 75%lS3HOBut |
| 2.33 | 4.15 | 1.20 | |
|
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
|---|
| 3,2 | Ac | 174.7
175.9 | 23.3
23.9 | |
| 3,4,4,6,1 | xLAla? | 177.4 | 50.1 | 17.6 | |
| 3,4,4,6 | xLGlu | 173.6 | 53.6 | 27.8 | 31.1 | 178.1 | |
| 3,4,4,2 | Ac | 174.7
175.9 | 23.3
23.9 | |
| 3,4,4 | aDGalpNA | 99.5 | 51.0 | 68.3 | 70.1 | 72.8 | 172.4 |
| 3,4,2 | Ac | 174.7
175.9 | 23.3
23.9 | |
| 3,4 | aDGalpN | 97.3 | 51.1 | 67.6 | 77.1 | 71.7 | 60.6 |
| 3 | aDGalpNA | 98.0 | 49.0 | 75.1 | 75.7 | 71.3 | ? |
| 2 | Ac | 174.7
175.9 | 23.3
23.9 | |
| | bDQuipN4N | 103.1 | 55.8 | 76.0 | 58.2 | 72.1 | 18.1 |
| 4 | 25%Ac | 174.7
175.9 | 23.3
23.9 | |
| 4 | 75%lS3HOBut | ? | 46.1 | 65.9 | 23.6 | |
|
![](nmr_drawer.py?width=750&height=130&nucleus=C&rotate_labels=false&spectrum=[{"s":175.3,"l":"1","c":[0,0,0]},{"s":23.6,"l":"2","c":[0,0,0]},{"s":177.4,"l":"1","c":[0,0,225]},{"s":50.1,"l":"2","c":[0,0,225]},{"s":17.6,"l":"3","c":[0,0,225]},{"s":173.6,"l":"1","c":[230,0,30]},{"s":53.6,"l":"2","c":[230,0,30]},{"s":27.8,"l":"3","c":[230,0,30]},{"s":31.1,"l":"4","c":[230,0,30]},{"s":178.1,"l":"5","c":[230,0,30]},{"s":175.3,"l":"1","c":[0,0,0]},{"s":23.6,"l":"2","c":[0,0,0]},{"s":99.5,"l":"1","c":[0,165,0]},{"s":51,"l":"2","c":[0,165,0]},{"s":68.3,"l":"3","c":[0,165,0]},{"s":70.1,"l":"4","c":[0,165,0]},{"s":72.8,"l":"5","c":[0,165,0]},{"s":172.4,"l":"6","c":[0,165,0]},{"s":175.3,"l":"1","c":[0,0,0]},{"s":23.6,"l":"2","c":[0,0,0]},{"s":97.3,"l":"1","c":[120,0,225]},{"s":51.1,"l":"2","c":[120,0,225]},{"s":67.6,"l":"3","c":[120,0,225]},{"s":77.1,"l":"4","c":[120,0,225]},{"s":71.7,"l":"5","c":[120,0,225]},{"s":60.6,"l":"6","c":[120,0,225]},{"s":98,"l":"1","c":[0,192,255]},{"s":49,"l":"2","c":[0,192,255]},{"s":75.1,"l":"3","c":[0,192,255]},{"s":75.7,"l":"4","c":[0,192,255]},{"s":71.3,"l":"5","c":[0,192,255]},{"s":175.3,"l":"1","c":[0,0,0]},{"s":23.6,"l":"2","c":[0,0,0]},{"s":103.1,"l":"1","c":[220,0,180]},{"s":55.8,"l":"2","c":[220,0,180]},{"s":76,"l":"3","c":[220,0,180]},{"s":58.2,"l":"4","c":[220,0,180]},{"s":72.1,"l":"5","c":[220,0,180]},{"s":18.1,"l":"6","c":[220,0,180]},{"s":175.3,"l":"1","c":[100,160,0]},{"s":23.6,"l":"2","c":[100,160,0]},{"s":46.1,"l":"2","c":[210,210,0]},{"s":65.9,"l":"3","c":[210,210,0]},{"s":23.6,"l":"4","c":[210,210,0]}])
The spectrum also has 2 signals at unknown positions (not plotted). |
There is only one chemically distinct structure:
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Found 1 record.
Displayed record 1
