Secondary cell wall polysaccharides of Bacillus anthracis are antigens that contain specific epitopes which cross-react with three pathogenic Bacillus cereus strains that caused severe disease, and other epitopes common to all the Bacillus cereus strains tested

Leoff, Christine; Saile, Elke; Rauvolfová, Jana; Quinn, Conrad P.; Hoffmaster, Alex R.; Zhong, Wanxie; Mehta, Alok Shaileshbhai; Boons, Geert‐Jan; Carlson, Russell W.; Kannenberg, Elmar L.

doi:10.1093/glycob/cwp036

Cited by 24 publications

(31 citation statements)

References 25 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…One mg of dried polysaccharide was dissolved in 90 l of 0.15 M HEPES buffer (pH 7.4). Subsequently, 90 l of 45 mg/ml of 1-cyano-4-dimethylaminopyridinium tetrafluoroborate (CDAP) in acetonitrile and 120 l of aqueous 0.3 M triethylamine as well as 4 mg bovine serum albumin (BSA) dissolved in 350 l 0.01 M PBS (pH 7.4) were added (26). The solution was stirred at 4°C for 18 h, and carbohydrate conjugation to BSA was quenched by adding 120 l of 0.5 M ethanolamine in 0.75 M HEPES buffer (pH 7.4).…”

Section: Purification Of Bacillus Anthracis Scwp B Anthracis Sternementioning

confidence: 99%

Bacillus cereus G9241 S-Layer Assembly Contributes to the Pathogenesis of Anthrax-Like Disease in Mice

Wang

Hendrickx

et al. 2012

Journal of Bacteriology

View full text Add to dashboard Cite

Bacillus cereus G9241, the causative agent of anthrax-like disease, harbors virulence plasmids encoding anthrax toxins as well as hyaluronic acid (HA) and B. cereus exopolysaccharide (BPS) capsules. B. cereus G9241 also harbors S-layer genes, including homologs of Bacillus anthracis surface array protein (Sap), extractable antigen 1 (EA1), and the S-layer-associated proteins (BSLs). In B. anthracis, S-layer proteins and BSLs attach via their S-layer homology domains (SLH) to the secondary cell wall polysaccharide (SCWP) in a manner requiring csaB, a predicted ketalpyruvate transferase. Here we used a genetic approach to analyze B. cereus G9241 S-layer assembly and function. Variants lacking the csaB gene synthesized SCWP but failed to retain Sap, EA1, and BSLs in the bacterial envelope. The B. cereus G9241 csaB mutant assembled capsular polysaccharides but displayed an increase in chain length relative to the wild-type strain. This phenotype is likely due to its inability to deposit BslO murein hydrolase at divisional septa. During growth under capsule-inducing conditions, B. cereus G9241 assembled BSLs (BslA and BslO) and the Sap S-layer protein, but not EA1, in the envelope. Finally, csaB-mediated assembly of S-layer proteins and BSLs in B. cereus G9241 contributes to the pathogenesis of anthrax-like disease in mice.

show abstract

Section: Purification Of Bacillus Anthracis Scwp B Anthracis Sternementioning

confidence: 99%

Bacillus cereus G9241 S-Layer Assembly Contributes to the Pathogenesis of Anthrax-Like Disease in Mice

Wang

Hendrickx

et al. 2012

Journal of Bacteriology

View full text Add to dashboard Cite

show abstract

“…Acetylation of SCWP appears to be a universal feature of B. anthracis and Bacillus cereus, and the sites of acetylation and pyruvylation on the polysaccharide appear similar between B. anthracis CDC 684 and B. anthracis Sterne (18,22,23). Nevertheless, the genetic basis for such modification is not yet known.…”

mentioning

confidence: 99%

Bacillus anthracis Acetyltransferases PatA1 and PatA2 Modify the Secondary Cell Wall Polysaccharide and Affect the Assembly of S-Layer Proteins

Lunderberg

Nguyen-Mau

Richter

et al. 2012

Journal of Bacteriology

View full text Add to dashboard Cite

The envelope of Bacillus anthracis encompasses a proteinaceous S-layer with two S-layer proteins (Sap and EA1). Protein assembly in the envelope of B. anthracis requires S-layer homology domains (SLH) within S-layer proteins and S-layer-associated proteins (BSLs), which associate with the secondary cell wall polysaccharide (SCWP), an acetylated carbohydrate that is tethered to peptidoglycan. Here, we investigated the contributions of two putative acetyltransferases, PatA1 and PatA2, on SCWP acetylation and S-layer assembly. We show that mutations in patA1 and patA2 affect the chain lengths of B. anthracis vegetative forms and perturb the deposition of the BslO murein hydrolase at cell division septa. The patA1 and patA2 mutants are defective for the assembly of EA1 in the envelope but retain the ability of S-layer formation with Sap. SCWP isolated from the patA1 patA2 mutant lacked acetyl moieties identified in wild-type polysaccharide and failed to associate with the SLH domains of EA1. A model is discussed whereby patA1-and patA2-mediated acetylation of SCWP enables the deposition of EA1 as well as BslO near the septal region of the B. anthracis envelope.

show abstract

“…The occurrence, structure, and glycosylation of LTAs were studied for different Bacillus species, including B. cereus strains containing LTAs (built up of polyglycerol phosphate chains and hydrophobic anchors) and D-alanine (11,50,51,62). Therefore, the presence of a dlt operon in the B. cereus 14579 genome suggests that the LTAs may be alanylated.…”

mentioning

confidence: 99%

ThedltOperon ofBacillus cereusIs Required for Resistance to Cationic Antimicrobial Peptides and for Virulence in Insects

et al. 2009

View full text Add to dashboard Cite

The dlt operon encodes proteins that alanylate teichoic acids, the major components of cell walls of gram-positive bacteria. This generates a net positive charge on bacterial cell walls, repulsing positively charged molecules and conferring resistance to animal and human cationic antimicrobial peptides (AMPs) in grampositive pathogenic bacteria. AMPs damage the bacterial membrane and are the most effective components of the humoral immune response against bacteria. We investigated the role of the dlt operon in insect virulence by inactivating this operon in Bacillus cereus, which is both an opportunistic human pathogen and an insect pathogen. The ⌬dlt Bc mutant displayed several morphological alterations but grew at a rate similar to that for the wild-type strain. This mutant was less resistant to protamine and several bacterial cationic AMPs, such as nisin, polymyxin B, and colistin, in vitro. It was also less resistant to molecules from the insect humoral immune system, lysozyme, and cationic AMP cecropin B from Spodoptera frugiperda. ⌬dlt Bc was as pathogenic as the wild-type strain in oral infections of Galleria mellonella but much less virulent when injected into the hemocoels of G. mellonella and Spodoptera littoralis. We detected the dlt operon in three gram-negative genera: Erwinia (Erwinia carotovora), Bordetella (Bordetella pertussis, Bordetella parapertussis, and Bordetella bronchiseptica), and Photorhabdus (the entomopathogenic bacterium Photorhabdus luminescens TT01, the dlt operon of which did not restore cationic AMP resistance in ⌬dlt Bc ). We suggest that the dlt operon protects B. cereus against insect humoral immune mediators, including hemolymph cationic AMPs, and may be critical for the establishment of lethal septicemia in insects and in nosocomial infections in humans.

show abstract

Secondary cell wall polysaccharides of Bacillus anthracis are antigens that contain specific epitopes which cross-react with three pathogenic Bacillus cereus strains that caused severe disease, and other epitopes common to all the Bacillus cereus strains tested

Cited by 24 publications

References 25 publications

Bacillus cereus G9241 S-Layer Assembly Contributes to the Pathogenesis of Anthrax-Like Disease in Mice

Bacillus cereus G9241 S-Layer Assembly Contributes to the Pathogenesis of Anthrax-Like Disease in Mice

Bacillus anthracis Acetyltransferases PatA1 and PatA2 Modify the Secondary Cell Wall Polysaccharide and Affect the Assembly of S-Layer Proteins

ThedltOperon ofBacillus cereusIs Required for Resistance to Cationic Antimicrobial Peptides and for Virulence in Insects

Contact Info

Product

Resources

About