Found 2 publications. Displayed publications from 1 to 2
Expand all publications       Show all as text (SweetDB notation)
1. (Article ID: 6136)
 
Senchenkova SN, Shashkov AS, Shneider MM, Popova AV, Balaji V, Biswas I, Knirel YA, Kenyon JJ
A novel ItrA4 D-galactosyl 1-phosphate transferase is predicted to initiate synthesis of an amino sugar-lacking K92 capsular polysaccharide of Acinetobacter baumannii B8300
Research in Microbiology 172(3) (2021) 103815
 

The K92 capsular polysaccharide (CPS) from Acinetobacter baumannii B8300 was studied by sugar analysis, Smith degradation, and one- and two-dimensional 1H and 13C NMR spectroscopy. The elucidated CPS includes a branched pentasaccharide repeat unit containing one d-Galp and four l-Rhap residues; an atypical composition given that all A. baumannii CPS structures determined to date contain at least one amino sugar. Accordingly, biosynthesis of A. baumannii CPS types are initiated by initiating transferases (Itrs) that transfer 1-phosphate of either a 2-acetamido-2-deoxy-d-hexose, a 2-acetamido-2,6-dideoxy-d-hexose or a 2-acetamido-4-acylamino-2,4,6-trideoxy-d-hexose to an undecaprenyl phosphate (UndP) carrier. However, the KL92 capsule biosynthesis gene cluster in the B8300 genome sequence includes a gene for a novel Itr type, ItrA4, which is predicted to begin synthesis of the K92 CPS by transferring D-Galp 1-phosphate to the UndP lipid carrier. The itrA4 gene was found in a module transcribed in the opposite direction to the majority of the K locus. This module also includes an unknown open reading frame (orfKL92), a gtr166 glycosyltransferase gene, and a wzi gene predicted to be involved in the attachment of CPS to the cell surface. Investigation into the origins of orfKL92-gtr166-itrA4-wziKL92 revealed it might have originated from Acinetobacter junii.

Acinetobacter baumannii, capsular polysaccharide, capsule biosynthesis, galactosyl 1-phosphate transferase, initiating transferase, ItrA4

The publication contains the following compound(s):
 

Expand this publication
2. (Article ID: 6217)
 
Drobiazko AY, Kasimova AA, Evseev PV, Schneider MM, Klimuk EI, Shashkov AS, Dmitrenok AS, Chizhov AO, Slukin PV, Skryabin YP, Volozhantsev NV, Miroshnikov KA, Knirel YA, Popova AV
Capsule-Targeting Depolymerases Derived from Acinetobacter baumannii Prophage Regions
International Journal of Molecular Sciences 23(9) (2022) 4971
 

In this study, several different depolymerases encoded in the prophage regions of Acinetobacter baumannii genomes have been bioinformatically predicted and recombinantly produced. The identified depolymerases possessed multi-domain structures and were identical or closely homologous to various proteins encoded in other A. baumannii genomes. This means that prophage-derived depolymerases are widespread, and different bacterial genomes can be the source of proteins with polysaccharide-degrading activities. For two depolymerases, the specificity to capsular polysaccharides (CPSs) of A. baumannii belonging to K1 and K92 capsular types (K types) was determined. The data obtained showed that the prophage-derived depolymerases were glycosidases that cleaved the A. baumannii CPSs by the hydrolytic mechanism to yield monomers and oligomers of the K units. The recombinant proteins with established enzymatic activity significantly reduced the mortality of Galleria mellonella larvae infected with A. baumannii of K1 and K92 capsular types. Therefore, these enzymes can be considered as suitable candidates for the development of new antibacterials against corresponding A. baumannii K types.

Acinetobacter baumannii, capsular polysaccharide, glycosidase, capsular type, phage receptor-binding proteins, prophages, structural depolymerase

The publication contains the following compound(s):
 

Expand this publication

Resort publications by:

New query Export IDs Home Help

Execution: <1 sec