Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Oncorhynchus mykiss
Organ / tissue: kidneyAssociated disease: motile aeromonad septicemia (MAS)
The structure was elucidated in this paperNCBI PubMed ID: 25037826Publication DOI: 10.1016/j.carres.2014.06.011Journal NLM ID: 0043535Publisher: Elsevier
Correspondence: aturska
hektor.umcs.lublin.pl
Institutions: Department of Genetics and Microbiology, M. Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland, Department of Fish Diseases, National Veterinary Research Institute, Partyzantów 57, 24-100 Pulawy, Poland, Division of Structural Biochemistry, Research Center Borstel, Leibniz-Center for Medicine and Biosciences, Parkallee 4a/c, D-23845 Borstel, Germany
The O-specific polysaccharide (OPS) obtained by mild-acid degradation of the lipopolysaccharide from Aeromonas sobria strain Pt312 was studied by sugar and methylation analyses along with 1H and 13C NMR spectroscopy, including 2D 1H,1H COSY, TOCSY, NOESY, 1H-detected 1H,13C HSQC, and HMBC experiments. The sequence of the sugar residues was determined using 1H,1H NOESY and 1H,13C HMBC experiments. It was found that the OPS was built up of disaccharide repeating units composed of GlcpNAc and non-stoichiometrically O-acetylated Rhap residues, and had the structure.
Lipopolysaccharide, NMR, O-specific polysaccharide, O-acetylation, Fish pathogen, Aeromonas sobria
Structure type: polymer chemical repeating unit
Location inside paper: p.144, table 1
Trivial name: repeating unit
Compound class: O-polysaccharide, O-antigen
Contained glycoepitopes: IEDB_135813,IEDB_135849,IEDB_136105,IEDB_137340,IEDB_141807,IEDB_151531,IEDB_225177,IEDB_885823
Methods: 13C NMR, 1H NMR, methylation, GLC-MS, NMR-2D, sugar analysis, acid hydrolysis, GLC, de-O-acetylation, NMR-1D, GPC, SDS-Tricine-PAGE
Comments, role: O-deacetylated OPS of A. sobria strain Pt312
Related record ID(s): 11074, 11203
NCBI Taxonomy refs (TaxIDs): 646Reference(s) to other database(s): GTC:G35373OX, GlycomeDB:
25158
Show glycosyltransferases
NMR conditions: in D2O at 300 K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
3 aLRhap 102.20 72.00 71.52 81.20 68.32 18.00
2 Ac 175.64 23.2
bDGlcpN 102.38 56.67 82.74 69.34 76.86 61.68
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6
3 aLRhap 4.84 3.73 3.81 3.59 3.99 1.26
2 Ac - 2.06
bDGlcpN 4.79 3.78 3.59 3.49 3.42 3.75-3.92
1H/13C HSQC data:
Linkage Residue C1/H1 C2/H2 C3/H3 C4/H4 C5/H5 C6/H6
3 aLRhap 102.20/4.84 72.00/3.73 71.52/3.81 81.20/3.59 68.32/3.99 18.00/1.26
2 Ac 23.2/2.06
bDGlcpN 102.38/4.79 56.67/3.78 82.74/3.59 69.34/3.49 76.86/3.42 61.68/3.75-3.92
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 |
|---|
| 3 | aLRhap | 4.84 | 3.73 | 3.81 | 3.59 | 3.99 | 1.26 |
| 2 | Ac |
| 2.06 | |
| | bDGlcpN | 4.79 | 3.78 | 3.59 | 3.49 | 3.42 | 3.75
3.92 |
|
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
|---|
| 3 | aLRhap | 102.20 | 72.00 | 71.52 | 81.20 | 68.32 | 18.00 |
| 2 | Ac | 175.64 | 23.2 | |
| | bDGlcpN | 102.38 | 56.67 | 82.74 | 69.34 | 76.86 | 61.68 |
|
There is only one chemically distinct structure:
Found 
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