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1. (Article ID: 6077)
 
Kasimova AA, Arbatsky NP, Tickner J, Kenyon JJ, Hall RM, Shneider MM, Dzhaparova AA, Shashkov AS, Chizhov AO, Popova AV, Knirel YA
Acinetobacter baumannii K106 and K112: Two Structurally and Genetically Related 6-Deoxy-l-talose-Containing Capsular Polysaccharides
International Journal of Molecular Sciences 22(11) (2021) 5641
 

Whole genome sequences of two Acinetobacter baumannii clinical isolates, 48-1789 and MAR24, revealed that they carry the KL106 and KL112 capsular polysaccharide (CPS) biosynthesis gene clusters, respectively, at the chromosomal K locus. The KL106 and KL112 gene clusters are related to the previously described KL11 and KL83 gene clusters, sharing genes for the synthesis of l-rhamnose (l-Rhap) and 6-deoxy-l-talose (l-6dTalp). CPS material isolated from 48-1789 and MAR24 was studied by sugar analysis and Smith degradation along with one- and two-dimensional 1H and 13C NMR spectroscopy. The structures of K106 and K112 oligosaccharide repeats (K units) l-6dTalp-(1→3)-D-GlcpNAc tetrasaccharide fragment share the responsible genes in the respective gene clusters. The K106 and K83 CPSs also have the same linkage between K units. The KL112 cluster includes an additional glycosyltransferase gene, Gtr183, and the K112 unit includes α l-Rhap side chain that is not found in the K106 structure. K112 further differs in the linkage between K units formed by the Wzy polymerase, and a different wzy gene is found in KL112. However, though both KL106 and KL112 share the atr8 acetyltransferase gene with KL83, only K83 is acetylated.

Acinetobacter baumannii, capsular polysaccharide, 6-deoxy-L-talose, K locus, K106, K112

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2. (Article ID: 6079)
 
Kasimova AA, Arbatsky NP, Timoshina OY, Shneider MM, Shashkov AS, Chizhov AO, Popova AV, Hall RM, Kenyon JJ, Knirel YA
The K26 capsular polysaccharide from Acinetobacter baumannii KZ-1098: Structure and cleavage by a specific phage depolymerase
International Journal of Biological Macromolecules 191 (2021) 182-191
 

The KL26 gene cluster responsible for the synthesis of the K26 capsular polysaccharide (CPS) of Acinetobacter baumannii includes rmlBDAC genes for l-rhamnose (l-Rhap) synthesis, tle to generate 6-deoxy-l-talose (l-6dTalp) from l-Rhap, and a manC gene for D-mannose (D-Manp) that is rare in Acinetobacter CPS. K26 CPS material was isolated from A. baumannii isolate KZ-1098, and studied by sugar analysis, Smith degradation, and one and two-dimensional 1H and 13C NMR spectroscopy before and after O-deacetylation with aqueous ammonia. The following structure of the branched hexasaccharide repeating unit of the CPS was established: →2)-β-D-Manp-1→4-β-D-Glcp-1→3-α-L-6dTalp-1→3-β-D-GlcpNAc-(1→3↑14│Acα-L-Rhap-2←1-α-D-Glcp The structural depolymerase of phage vB_AbaP_APK26 cleaved selectively the β-GlcpNAc-(1→2)-α-Manp linkage in the K26 CPS formed by WzyK26 to give monomer, dimer, and trimer of the CPS repeating unit, which were characterized by high-resolution electrospray ionization mass spectrometry as well as 1H and 13C NMR spectroscopy. The wzyK26 gene responsible for this linkage and the manC gene were only found in six A. baumannii genomes carrying KL26 and one carrying the novel KL148 gene cluster, indicating the rare occurrence of β-GlcpNAc-(1→2)-α-Manp in A. baumannii CPS structures. However, K26 shares a β-d-Glcp-(1→3)-α-l-6dTalp-(1→3)-β-d-GlcpNAc trisaccharide fragment with a group of related A. baumannii CPSs that have varying patterns of acetylation of l-6dTalp.

Acinetobacter baumannii, capsular polysaccharide structure, 6-deoxy-L-talose, depolymerization, A.baumannii, phage depolymerase

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3. (Article ID: 6167)
 
Yakovleva L, Fulleborn JA, Walvoort MTC
Opportunities and Challenges of Bacterial Glycosylation for the Development of Novel Antibacterial Strategies
Frontiers in Microbiology 12 (2021) 745702
 

Glycosylation is a ubiquitous process that is universally conserved in nature. The various products of glycosylation, such as polysaccharides, glycoproteins, and glycolipids, perform a myriad of intra- and extracellular functions. The multitude of roles performed by these molecules is reflected in the significant diversity of glycan structures and linkages found in eukaryotes and prokaryotes. Importantly, glycosylation is highly relevant for the virulence of many bacterial pathogens. Various surface-associated glycoconjugates have been identified in bacteria that promote infectious behavior and survival in the host through motility, adhesion, molecular mimicry, and immune system manipulation. Interestingly, bacterial glycosylation systems that produce these virulence factors frequently feature rare monosaccharides and unusual glycosylation mechanisms. Owing to their marked difference from human glycosylation, bacterial glycosylation systems constitute promising antibacterial targets. With the rise of antibiotic resistance and depletion of the antibiotic pipeline, novel drug targets are urgently needed. Bacteria-specific glycosylation systems are especially promising for antivirulence therapies that do not eliminate a bacterial population, but rather alleviate its pathogenesis. In this review, we describe a selection of unique glycosylation systems in bacterial pathogens and their role in bacterial homeostasis and infection, with a focus on virulence factors. In addition, recent advances to inhibit the enzymes involved in these glycosylation systems and target the bacterial glycan structures directly will be highlighted. Together, this review provides an overview of the current status and promise for the future of using bacterial glycosylation to develop novel antibacterial strategies.

glycosylation, pathogenic bacteria, metabolic oligosaccharide engineering, antibacterial strategies, antivirulence

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