Taxonomic group: bacteria / Proteobacteria
(Phylum: Proteobacteria)
Associated disease: nosocomial infections [ICD11:
XB25 
];
infection due to Acinetobacter baumannii [ICD11:
XN8LS ]
NCBI PubMed ID: 37240444Publication DOI: 10.3390/ijms24109100Journal NLM ID: 101092791Publisher: Basel, Switzerland: MDPI
Correspondence: A.V. Popova <popova_nastya86
mail.ru>
Institutions: Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997 Moscow, Russia, State Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, Russia, N. D. Zelinsky Institute of Organic Chemistry, Russian Academy of Sciences, 119991 Moscow, Russia, Bach Institute of Biochemistry, Research Centre of Biotechnology of the Russian Academy of Sciences, 119071 Moscow, Russia, Center for Photonics and 2D Materials, Moscow Institute of Physics and Technology, 141700 Dolgoprudny, Russia, Complex of NBICS Technologies, National Research Center 'Kurchatov Institute', 123182 Moscow, Russia, Central Scientific Research Institute of Epidemiology, 111123 Moscow, Russia
Acinetobacter baumannii is a critical priority nosocomial pathogen that produces a variety of capsular polysaccharides (CPSs), the primary receptors for specific depolymerase-carrying phages. In this study, the tailspike depolymerases (TSDs) encoded in genomes of six novel Friunaviruses, APK09, APK14, APK16, APK86, APK127v, APK128, and one previously described Friunavirus phage, APK37.1, were characterized. For all TSDs, the mechanism of specific cleavage of corresponding A. baumannii capsular polysaccharides (CPSs) was established. The structures of oligosaccharide fragments derived from K9, K14, K16, K37/K3-v1, K86, K127, and K128 CPSs degradation by the recombinant depolymerases have been determined. The crystal structures of three of the studied TSDs were obtained. A significant reduction in mortality of Galleria mellonella larvae infected with A. baumannii of K9 capsular type was shown in the example of recombinant TSD APK09_gp48. The data obtained will provide a better understanding of the interaction of phage-bacterial host systems and will contribute to the formation of principles of rational usage of lytic phages and phage-derived enzymes as antibacterial agents.
Acinetobacter baumannii, capsular polysaccharide, crystal structure, bacteriophage, glycosidase, capsular type, tailspike depolymerase
Structure type: polymer chemical repeating unit
Location inside paper: table 2, Fig. 10, CPS KZ-1093
The structure in this paper was incorrect:
Compound class: CPS
Contained glycoepitopes: IEDB_130648,IEDB_134624,IEDB_134627,IEDB_136044,IEDB_136906,IEDB_137472,IEDB_137473,IEDB_141794,IEDB_142488,IEDB_146664,IEDB_147450,IEDB_151528,IEDB_190606,IEDB_742248,IEDB_983931,SB_163,SB_165,SB_166,SB_187,SB_192,SB_195,SB_23,SB_24,SB_25,SB_7,SB_8,SB_88
Methods: 13C NMR, 1H NMR, NMR-2D, PCR, X-ray, DNA techniques, GPC, enzymatic depolymerization, crystallization, HR-ESI-MS, phage isolation, phage genome analysis, phage propagation, phage sequencing
Comments, role: erroroneous structure CPS was corrected from ref [20] Arbatsky NP at al., Carbohydr Res. 2019, 485, 107814. DOI: 10.1016/j.carres.2019.107814.
Related record ID(s): 22328, 24860, 24861, 24862, 24863, 24864, 24865, 24866, 24867, 24868, 24869, 24870, 27040, 27041, 27042, 27043, 27044, 27045, 27046, 27047, 27048, 27050
NCBI Taxonomy refs (TaxIDs): 470Reference(s) to other database(s): GTC:G41835WJ
Show glycosyltransferases
There is only one chemically distinct structure:
Found 
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