Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: infection due to Acinetobacter baumannii [ICD11:
XN8LS 
]
NCBI PubMed ID: 37975684Publication DOI: 10.1128/spectrum.03025-23Journal NLM ID: 101634614Publisher: Washington, DC: ASM Press
Correspondence: J.J. Kenyon <j.kenyon
griffith.edu.au>
Institutions: N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, Obolensk, Moscow Region, Russia, M. M. Shemyakin and Y. A. Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, Moscow, Russia, Centre for Immunology and Infection Control, School of Biomedical Sciences, Faculty of Health, Queensland University of Technology, Brisbane, Australia, School of Life and Environmental Sciences, Faculty of Science, University of Sydney, Sydney, Australia, Saw Swee Hock School of Public Health, National University of Singapore, Queenstown, Singapore, Yong Loo Lin School of Medicine, National University of Singapore, Queenstown, Singapore
Bacteriophage show promise for the treatment of Acinetobacter baumannii infections that resist all therapeutically suitable antibiotics. Many tail-spike depolymerases encoded by phage that are able to degrade A. baumannii capsular polysaccharide (CPS) exhibit specificity for the linkage present between K-units that make up CPS polymers. This linkage is formed by a specific Wzy polymerase, and the ability to predict this linkage using sequence-based methods that identify the Wzy at the K locus could assist with the selection of phage for therapy. However, little is known about the specificity of Wzy polymerase enzymes. Here, we describe a Wzy polymerase that can accommodate two different but similar sugars as one of the residues it links and phage depolymerases that can cleave both types of bond that Wzy forms.
Acinetobacter baumannii, capsular polysaccharide, Wzy polymerase, phage depolymerase, K70
Structure type: polymer chemical repeating unit
Location inside paper: table 1, K42 LUH5550
The structure in this paper was incorrect:
Trivial name: K125 CPS
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_137473,IEDB_1391961,IEDB_141584,IEDB_885822
Methods: 13C NMR, 1H NMR, NMR-2D, DNA sequencing, sugar analysis, DNA techniques, GLC, Smith degradation, HPLC, GPC, bioinformatic analysis, phage depolymerisation, HR-ESI-MS
Comments, role: KL type: KL125; erroroneous structure was corrected from ref [31] Arbatsky NP, et al., Int J Biol Macromol 2018, 117, 1195-1199. DOI: 10.1016/j.ijbiomac.2018.06.029
Related record ID(s): 20741, 20742, 20743, 20744, 20745, 20746, 20747, 20748, 20749, 20750, 20751, 20752, 20753, 20754, 22258
NCBI Taxonomy refs (TaxIDs): 470Reference(s) to other database(s): GTC:G70961ID
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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