Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Host organism: Homo sapiens
Associated disease: nosocomial infections [ICD11:
XB25 
];
infection due to Acinetobacter baumannii [ICD11:
XN8LS 
]
The structure was elucidated in this paperNCBI PubMed ID: 25926563Publication DOI: 10.1093/glycob/cwv028Journal NLM ID: 9104124Publisher: IRL Press at Oxford University Press
Correspondence: ruth.hall

sydney.edu.au
Institutions: School of Molecular Bioscience, The University of Sydney, Sydney, NSW, 2006, Australia, Department of Chemical Sciences, University of Napoli, Napoli, Italy
The repeat unit of the K12 capsular polysaccharide isolated from the Acinetobacter baumannii global clone 1 clinical isolate, D36, was elucidated by means of chemical and spectroscopical methods. The structure was shown to contain N-acetyl-D-galactosamine (D-GalpNAc), N-acetyl-D-fucosamine and N-acetyl-L-fucosamine linked together in the main chain, with the novel sugar, 5,7-diacetamido-3,5,7,9-tetradeoxy-L-glycero-L-altro-non-2-ulosonic acid (5,7-di-N-acetylacinetaminic acid or Aci5Ac7Ac), attached to D-GalpNAc as a side branch. This matched the sugar composition of the K12 capsule and the genetic content of the KL12 capsule gene cluster reported previously. D-FucpNAc was predicted to be the substrate for the initiating transferase, ItrB3, with the Wzy polymerase making a α-D-FucpNAc-(1 → 3)-D-GalpNAc linkage between the repeat units. The three glycosyltransferases encoded by KL12 are all retaining glycosyltransferases and were predicted to form specific linkages between the sugars in the K12 repeat unit.
Acinetobacter baumannii, capsular polysaccharide, K locus, KL12 gene cluster, acinetaminic acid
Structure type: polymer chemical repeating unit
Location inside paper: p.883, fig.3, table 1, dCPS
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_885822
Methods: 13C NMR, 1H NMR, methylation, NMR-2D, GC-MS, sugar analysis, mild acid hydrolysis, NMR-1D, acetylation, bioinformatic analysis, SEC
Biosynthesis and genetic data: genetic data
Comments, role: CPS after mild acid hydrolysis.
Related record ID(s): 30739
NCBI Taxonomy refs (TaxIDs): 470Reference(s) to other database(s): GTC:G50469GQ
Show glycosyltransferases
NMR conditions: in D2O at 308 K
[as TSV]
13C NMR data:
Linkage Residue C1 C2 C3 C4 C5 C6
3,3,2 Ac
3,3 aDGalpN 99.6 49.8 73.5 65.6 72.5 62.6
3,2 Ac
3 aLFucpN 99.8 49.3 74.3 72.1 68.2 16.5
2 Ac
aDFucpN 94.7 49.3 74.3 72.2 68.5 16.5
1H NMR data:
Linkage Residue H1 H2 H3 H4 H5 H6
3,3,2 Ac
3,3 aDGalpN 5.08 4.37 3.40 4.12 3.93 3.76-3.76
3,2 Ac
3 aLFucpN 4.95 4.34 4.09 3.96 4.10 1.21
2 Ac
aDFucpN 4.95 4.35 3.81 3.82 3.94 1.25
1H/13C HSQC data:
Linkage Residue C1/H1 C2/H2 C3/H3 C4/H4 C5/H5 C6/H6
3,3,2 Ac
3,3 aDGalpN 99.6/5.08 49.8/4.37 73.5/3.40 65.6/4.12 72.5/3.93 62.6/3.76-3.76
3,2 Ac
3 aLFucpN 99.8/4.95 49.3/4.34 74.3/4.09 72.1/3.96 68.2/4.10 16.5/1.21
2 Ac
aDFucpN 94.7/4.95 49.3/4.35 74.3/3.81 72.2/3.82 68.5/3.94 16.5/1.25
1H NMR data:
| Linkage | Residue | H1 | H2 | H3 | H4 | H5 | H6 |
| 3,3,2 | Ac | |
| 3,3 | aDGalpN | 5.08 | 4.37 | 3.40 | 4.12 | 3.93 | 3.76 3.76 |
| 3,2 | Ac | |
| 3 | aLFucpN | 4.95 | 4.34 | 4.09 | 3.96 | 4.10 | 1.21 |
| 2 | Ac | |
| | aDFucpN | 4.95 | 4.35 | 3.81 | 3.82 | 3.94 | 1.25 |
|
13C NMR data:
| Linkage | Residue | C1 | C2 | C3 | C4 | C5 | C6 |
| 3,3,2 | Ac | |
| 3,3 | aDGalpN | 99.6 | 49.8 | 73.5 | 65.6 | 72.5 | 62.6 |
| 3,2 | Ac | |
| 3 | aLFucpN | 99.8 | 49.3 | 74.3 | 72.1 | 68.2 | 16.5 |
| 2 | Ac | |
| | aDFucpN | 94.7 | 49.3 | 74.3 | 72.2 | 68.5 | 16.5 |
|
There is only one chemically distinct structure: