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Taxonomic group: bacteria / Firmicutes (Phylum: Firmicutes)
Associated disease: infection due to Bacillus anthracis [ICD11: XN94F

]

NCBI PubMed ID: 35997505
Publication DOI: 10.1128/jb.00253-22
Journal NLM ID: 2985120R
Publisher: American Society for Microbiology
Correspondence: D. Missiakas <dmissiak

bsd.uchicago.edu>
Institutions: Department of Microbiology, Howard Taylor Ricketts Laboratory, The University of Chicago, Lemont, Illinois, USA

Bacillus anthracis elaborates a secondary cell wall polysaccharide (SCWP) made of 6 to 12 trisaccharide units. Pyruvyl and acetyl substitutions of the distal unit are prerequisites for the noncovalent retention of 22 secreted Bacillus S-layer (Bsl)-associated proteins bearing an S-layer homology (SLH) domain. Surface display of Bsl proteins contributes to cell separation as well as virulence. Earlier work suggested that TagO initiates the synthesis of SCWP while GneY and GneZ, two UDP-GlcNAc 2-epimerases, synthesize ManNAc that is later incorporated in the repeat unit (→4)-ManNAc-(β1→4)-GlcNAc-(β1→6)-GlcNAc-(α1→). In organisms that synthesize wall teichoic acid, TagA catalysts have been shown to form the glycosidic bond ManNAc-(β1→4)-GlcNAc. Here, we show that genes bas2675 and bas5272, predicted to encode glycosyltransferases of the WecB/TagA/CpsF family (PFAM03808; CAZy GT26), are required for B. anthracis SCWP synthesis and S-layer assembly. Similar to tagO or gneY gneZ mutants, B. anthracis strains depleted of tagA1 (bas5272) cannot maintain cell shape, support vegetative growth, or synthesize SCWP. Expression of tagA2 (bas2675), or Staphylococcus aureus tagA on a plasmid, rescues the nonviable tagA1 mutant. We propose that TagA1 and TagA2 fulfill overlapping and key glycosyltransferase functions for the synthesis of repeat units of the SCWP of B. anthracis. IMPORTANCE Glycosyltransferases (GTs) catalyze the transfer of sugar moieties from activated donor molecules to acceptor molecules to form glycosidic bonds using a retaining or inverting mechanism. Based on the structural relatedness of their catalytic and carbohydrate-binding modules, GTs have been grouped into 115 families in the Carbohydrate-Active EnZyme (CAZy) database. For complex products, the functional assignment of GTs remains highly challenging without the knowledge of the chemical structure of the assembled polymer. Here, we propose that two uncharacterized GTs of B. anthracis belonging to the WecB/TagA/CpsF family incorporate ManNAc in repeat units of the secondary cell wall polymer of bacilli species.

glycosyltransferase, Bacillus anthracis, secondary cell wall polysaccharide, envelope biogenesis, S-layer homology domain, TagA, UDP-N-acetyl-mannosamine, undecaprenol-phosphate

Structure type: structural motif or average structure
Location inside paper: abstract, Fig.1A, p. e0025322-2
Compound class: secondary cell wall polysaccharide
Contained glycoepitopes: IEDB_135813,IEDB_136044,IEDB_136906,IEDB_137340,IEDB_137472,IEDB_140108,IEDB_141794,IEDB_141807,IEDB_151528,IEDB_151531,IEDB_190606,IEDB_885813,SB_165,SB_166,SB_187,SB_195,SB_30,SB_7,SB_88

Methods: Western blotting, genetic methods, immunofluorescence microscopy, SEC-HPLC, lectin binding
Enzymes that release or process the structure: TagA, GtsE

NCBI Taxonomy refs (TaxIDs): 1392
Show glycosyltransferases

There is only one chemically distinct structure:

CC(=O)N[C@@H]1[C@H](O[C@@H]2[C@@H](CO)O[C@@H](OC[C@H]3O[C@H](O[C@@H]4[C@@H](CO)O[C@@H](O[C@@H]5[C@@H](CO)O[C@@H](OC[C@H]6O[C@H](O[C@@H]7[C@@H](CO)O[C@@H](O[C@@H]8[C@@H](CO)O[C@@H](OC[C@H]9O[C@H](O[C@@H]%10[C@@H](CO)O[C@@H](O[C@@H]%11[C@@H](CO)O[C@@H](OC[C@H]%12O[C@H](O[C@@H]%13[C@@H](CO)O[C@@H](O[C@@H]%14[C@@H](CO)O[C@@H](OC[C@H]%15O[C@H](O)[C@H](NC(C)=O)[C@@H](O[C@H]%16O[C@H](CO)[C@H](O)[C@H](O)[C@H]%16O)[C@@H]%15O[C@@H]%15O[C@H](CO)[C@H](O)[C@H](O)[C@H]%15O)[C@H](NC(C)=O)[C@H]%14O[C@H]%14O[C@H](CO)[C@H](O)[C@H](O)[C@H]%14O)[C@@H](NC(C)=O)[C@H]%13O)[C@H](NC(C)=O)[C@@H](O[C@H]%13O[C@H](CO)[C@H](O)[C@H](O)[C@H]%13O)[C@@H]%12O[C@@H]%12O[C@H](CO)[C@H](O)[C@H](O)[C@H]%12O)[C@H](NC(C)=O)[C@H]%11O[C@H]%11O[C@H](CO)[C@H](O)[C@H](O)[C@H]%11O)[C@@H](NC(C)=O)[C@H]%10O)[C@H](NC(C)=O)[C@@H](O[C@H]%10O[C@H](CO)[C@H](O)[C@H](O)[C@H]%10O)[C@@H]9O[C@@H]9O[C@H](CO)[C@H](O)[C@H](O)[C@H]9O)[C@H](NC(C)=O)[C@H]8O[C@H]8O[C@H](CO)[C@H](O)[C@H](O)[C@H]8O)[C@@H](NC(C)=O)[C@H]7O)[C@H](NC(C)=O)[C@@H](O[C@H]7O[C@H](CO)[C@H](O)[C@H](O)[C@H]7O)[C@@H]6O[C@@H]6O[C@H](CO)[C@H](O)[C@H](O)[C@H]6O)[C@H](NC(C)=O)[C@H]5O[C@H]5O[C@H](CO)[C@H](O)[C@H](O)[C@H]5O)[C@@H](NC(C)=O)[C@H]4O)[C@H](NC(C)=O)[C@@H](O[C@H]4O[C@H](CO)[C@H](O)[C@H](O)[C@H]4O)[C@@H]3O[C@@H]3O[C@H](CO)[C@H](O)[C@H](O)[C@H]3O)[C@H](NC(C)=O)[C@H]2O[C@H]2O[C@H](CO)[C@H](O)[C@H](O)[C@H]2O)O[C@H](CO)[C@@H](O[C@H]2O[C@H](CO[C@@H]3O[C@H](CO)[C@@H](O[C@@H]4O[C@@H]5CO[C@@](C)(C(=O)O)O[C@H]5[C@H](O)[C@@H]4NC(C)=O)[C@H](OC(C)=O)[C@H]3NC(C)=O)[C@@H](O)[C@H](O)[C@H]2N)[C@@H]1O

SVG MW SMILES 3D mol Ionize

Warning = sub-repeat ending at aDGlcpN: variable unit count (4-10) was assumed to be 4