The SLH‐domain protein BslO is a determinant of <i>Bacillus anthracis</i> chain length

Anderson, Valerie J.; Kern, Justin W.; McCool, Justin W.; Schneewind, Olaf; Missiakas, Dominique

doi:10.1111/j.1365-2958.2011.07688.x

Cited by 31 publications

(75 citation statements)

References 43 publications

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“…Images were captured with a charge-coupled device (CCD) camera on an Olympus IX81 microscope using 40ϫ or 100ϫ objectives. For immunofluorescence microscopy, samples were incubated with dilute rabbit antiserum raised against purified recombinant Sap, BslO, or EA1 (15,16) and labeled with secondary antibody conjugated to a fluorophore (Molecular Probes). Cells were counterstained with boron-dipyrromethene (BODIPY)-vancomycin (Invitrogen).…”

Section: Methodsmentioning

confidence: 99%

“…The ⌬slaQ mutant mislocalizes Sap and BslO in the bacterial S-layer. BslO, an SLH domain-containing murein hydrolase, has been implicated in the separation of vegetative bacilli following cell division and in controlling chain length (15). Furthermore, the assembly of Sap on the surface directs proper localization of BslO to the site of activity at the septum (16).…”

Section: B Anthracis Slaq Is Required For S-layer Protein Secretionmentioning

confidence: 99%

“…Genetic approaches identified determinants of B. anthracis chain length (15,16). Insertional lesions in bslO, sap, and csaB, as well as patA1 and patA2, increase the chain lengths of B. anthracis vegetative forms without affecting the size of bacterial cells (15)(16)(17)(18).…”

mentioning

confidence: 99%

“…Insertional lesions in bslO, sap, and csaB, as well as patA1 and patA2, increase the chain lengths of B. anthracis vegetative forms without affecting the size of bacterial cells (15)(16)(17)(18). bslO encodes a secreted cell wall hydrolase with S-layer homology (SLH) domains that bind to pyruvylated secondary cell wall polysaccharide (SCWP) (15), comprised of the repeating unit [¡4)-␤-ManNAc-(1¡4)-␤-GlcNAc-(1¡6)-␣-GlcNAc-(1¡)] n (19,20). BslO functions as a murein hydrolase when deposited at the division septa of vegetative cells and promotes cell separation, thereby reducing chain length (15).…”

mentioning

confidence: 99%

“…bslO encodes a secreted cell wall hydrolase with S-layer homology (SLH) domains that bind to pyruvylated secondary cell wall polysaccharide (SCWP) (15), comprised of the repeating unit [¡4)-␤-ManNAc-(1¡4)-␤-GlcNAc-(1¡6)-␣-GlcNAc-(1¡)] n (19,20). BslO functions as a murein hydrolase when deposited at the division septa of vegetative cells and promotes cell separation, thereby reducing chain length (15). B. anthracis variants lacking the S-layer protein Sap cannot restrict BslO localization to septal rings; similar to bslO mutants, sap variants form elongated chains of vegetative bacilli (16).…”

mentioning

confidence: 99%

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Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

Nguyen-Mau

Schneewind

et al. 2015

J Bacteriol

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Bacillus anthracis vegetative forms assemble an S-layer comprised of two S-layer proteins, Sap and EA1. A hallmark of S-layer proteins are their C-terminal crystallization domains, which assemble into a crystalline lattice once these polypeptides are deposited on the bacterial surface via association between their N-terminal S-layer homology domains and the secondary cell wall polysaccharide. Here we show that slaQ, encoding a small cytoplasmic protein conserved among pathogenic bacilli elaborating S-layers, is required for the efficient secretion and assembly of Sap and EA1. S-layer protein precursors cosediment with SlaQ, and SlaQ appears to facilitate Sap assembly. Purified SlaQ polymerizes and when mixed with purified Sap promotes the in vitro formation of tubular S-layer structures. A model is discussed whereby SlaQ, in conjunction with S-layer secretion factors SecA2 and SlaP, promotes localized secretion and S-layer assembly in B. anthracis. IMPORTANCES-layer proteins are endowed with the propensity for self-assembly into crystalline arrays. Factors promoting S-layer protein assembly have heretofore not been reported. We identified Bacillus anthracis SlaQ, a small cytoplasmic protein that facilitates S-layer protein assembly in vivo and in vitro.

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Section: Methodsmentioning

confidence: 99%

Section: B Anthracis Slaq Is Required For S-layer Protein Secretionmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

Nguyen-Mau

Schneewind

et al. 2015

J Bacteriol

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Structure, Bioactivity, and Resistance Mechanism of Streptomonomicin, an Unusual Lasso Peptide from an Understudied Halophilic Actinomycete

Metelev¹,

Tietz²,

Melby³

et al. 2015

Chemistry & Biology

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Summary Natural products are the most historically significant source of compounds for drug development. However, unacceptably high rates of compound rediscovery associated with large-scale screening of common microbial producers have resulted in the abandonment of many natural product drug discovery efforts, despite the increasing prevalence of clinically-problematic antibiotic resistance. Screening of underexplored taxa represents one strategy to avoid rediscovery. Herein we report the discovery, isolation, and structural elucidation of streptomonomicin (STM), an antibiotic lasso peptide from Streptomonospora alba, and report the genome for its producing organism. STM-resistant clones of Bacillus anthracis harbor mutations to walR, the gene encoding a response regulator for the only known widely-distributed and essential two-component signal transduction system in Firmicutes. Streptomonospora had been hitherto biosynthetically and genetically uncharacterized, with STM being the first reported compound from the genus. Our results demonstrate that understudied microbes remain fruitful reservoirs for the rapid discovery of novel, bioactive natural products.

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4,6-O-Pyruvyl Ketal Modified N-Acetylmannosamine of the Secondary Cell Wall Polysaccharide of Bacillus anthracis Is the Anchoring Residue for Its Surface Layer Proteins

2018

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The secondary cell wall polysaccharide (SCWP) of Bacillus anthracis plays a key role in the organization of the cell envelope of vegetative cells and is intimately involved in host−guest interactions. Genetic studies have indicated that it anchors S-layer and S-layer-associated proteins, which are involved in multiple vital biological functions, to the cell surface of B. anthracis. Phenotypic observations indicate that specific functional groups of the terminal unit of SCWP, including 4,6-O-pyruvyl ketal and acetyl esters, are important for binding of these proteins. These observations are based on genetic manipulations and have not been corroborated by direct binding studies. To address this issue, a synthetic strategy was developed that could provide a range of pyruvylated oligosaccharides derived from B. anthracis SCWP bearing base-labile acetyl esters and free amino groups. The resulting oligosaccharides were used in binding studies with a panel of S-layer and S-layerassociated proteins, which identified structural features of SCWP important for binding. A single pyruvylated ManNAc monosaccharide exhibited strong binding to all proteins, making it a promising structure for S-layer protein manipulation. The acetyl esters and free amine of SCWP did not significantly impact binding, and this observation is contrary to a proposed model in which SCWP acetylation is a prerequisite for association of some but not all S-layer and S-layer-associated proteins.

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The SLH‐domain protein BslO is a determinant of Bacillus anthracis chain length

Cited by 31 publications

References 43 publications

Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

Structure, Bioactivity, and Resistance Mechanism of Streptomonomicin, an Unusual Lasso Peptide from an Understudied Halophilic Actinomycete

4,6-O-Pyruvyl Ketal Modified N-Acetylmannosamine of the Secondary Cell Wall Polysaccharide of Bacillus anthracis Is the Anchoring Residue for Its Surface Layer Proteins

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