Structure of the K12 capsule containing 5,7-di-N-acetylacinetaminic acid from Acinetobacter baumannii isolate D36
| Autor: | Alberto M. Marzaioli, Ruth M. Hall, Johanna J. Kenyon, Cristina De Castro |
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| Přispěvatelé: | Johanna J., Kenyon, Marzaioli, ALBERTO MARIA, Ruth M., Hall, DE CASTRO, Cristina |
| Rok vydání: | 2015 |
| Předmět: |
Bacterial capsule
Acinetobacter baumannii Acetylgalactosamine Molecular Sequence Data Biology acinetaminic acid Biochemistry Fucose 060501 Bacteriology chemistry.chemical_compound Gene cluster Glycosyltransferase Transferase Polymerase Bacterial Capsules Repeat unit 060503 Microbial Genetics K locus Glycosyltransferases 060500 MICROBIOLOGY biology.organism_classification Microbial Biology capsular polysaccharide KL12 gene cluster chemistry Carbohydrate Sequence biology.protein Sialic Acids ORIGINAL ARTICLES |
| Zdroj: | Glycobiology |
| ISSN: | 1460-2423 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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