BslA, a pXO1‐encoded adhesin of Bacillus anthracis

Kern, Justin W.; Schneewind, Olaf

doi:10.1111/j.1365-2958.2008.06169.x

Cited by 87 publications

(126 citation statements)

References 57 publications

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“…Host cell viability and immune response to B. anthracis infection are complex processes that are dependent on multiple biological variables, including susceptibility to B. anthracis toxins and expression of cell surface receptors. For example, B. anthracis cells express the BslA adhesin that is required for attachment to host cells (Kern and Schneewind, 2008). Compared with the virulent Ames strain, bslA mutants exhibited a marked increase in LD50 and reduced bacterial load in an anthrax guinea pig model, indicating that BslA functions as a surface adhesin for B. anthracis (Kern and Schneewind, 2010).…”

Section: Discussionmentioning

confidence: 99%

Effects of Bacillus anthracis hydrophobicity and induction of host cell death on sample collection from environmental surfaces

Taylor-McCabe

Shou

Hong-Geller

2012

J. Gen. Appl. Microbiol.

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Section: Discussionmentioning

confidence: 99%

Effects of Bacillus anthracis hydrophobicity and induction of host cell death on sample collection from environmental surfaces

Taylor-McCabe

Shou

Hong-Geller

2012

J. Gen. Appl. Microbiol.

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“…HF-PS). Recently, it was shown that another SLH-containing surface protein that is encoded on the pathogenicity island of pXO1, BslA, is involved in the attachment of B. anthracis to host cells (22). Thus, it is possible that the HF-PS is involved in localizing important virulence proteins to the bacterial cell surface.…”

mentioning

confidence: 99%

Structural Elucidation of the Nonclassical Secondary Cell Wall Polysaccharide from Bacillus cereus ATCC 10987

Leoff

Choudhury

Saile

et al. 2008

Journal of Biological Chemistry

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Nonclassical secondary cell wall polysaccharides constitute a major cell wall structure in the Bacillus cereus group of bacteria. The structure of the secondary cell wall polysaccharide from Bacillus cereus ATCC 10987, a strain that is closely related to Bacillus anthracis, was determined. This polysaccharide was released from the cell wall with aqueous hydrogen fluoride (HF) and purified by gel filtration chromatography. The purified polysaccharide, HF-PS, was characterized by glycosyl composition and linkage analyses, mass spectrometry, and one-and twodimensional NMR analysis. The results showed that the B. cereus ATCC 10987 HF-PS has a repeating oligosaccharide consisting of a 36)-␣-GalNAc- (134) The Bacillus cereus is a group of Gram-positive bacteria that includes Bacillus anthracis, B. cereus, and Bacillus thuringiensis strains. Members of this group are very closely related. In fact, on the basis of detailed phylogenetic analysis, it has been suggested that they all may belong to a single species (1). Despite the very close relatedness of B. cereus group members, there is considerable pathogenic variability. Some members of this group are not pathogenic, whereas others are opportunistic pathogens causing a range of conditions on a variety of hosts. Bacillus thuringiensis is an insect pathogen, and B. cereus is normally a soil-dwelling bacterium, which in rare cases, causes, in humans, usually nonfatal cases of food poisoning, sepsis, endophthalmitis, and occasionally severe or fatal pneumonia. One member, B. anthracis, causes anthrax in animals and humans and is considered a high threat bioterrorism agent.This variability in pathogenicity and host range is largely attributed to the plasmid content of the B. cereus group members, which can vary in size and number (2). For example, the crystal toxin genes of B. thuringiensis are carried on a plasmid (3), and plasmids pXO1 and pXO2 contain the genes required for the production of the B. anthracis toxin proteins and ␥-polyglutamate capsule, respectively (4, 5). Further, recent B. cereus isolates from cases of severe and fatal pneumonia were found to have the pXO1 plasmid (6, 7), and another report showed that B. cereus or B. thuringiensis isolates from cases of "anthrax-like" disease in gorillas contain both pXO1 and pXO2 (8, 9).For numerous bacterial pathogens, both Gram-positive and Gram-negative, cell wall polysaccharides are known virulence factors. However, little work has been done on the cell wall polysaccharides from members of the B. cereus group. We recently showed that the polysaccharides released from the cell walls from members of the B. cereus group using aqueous hydrogen fluoride (HF) 3 have carbohydrate compositions that vary qualitatively in a manner that is correlated, at least in part, to phylogenetic relatedness as determined by multilocus

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“…Mutants were screened for growth on BHI agar and no growth on BHI-kanamycin agar. All complementation plasmids were derived from pJK4, and the expression of its P spac promoter was induced with 0.1 mM isopropyl-␤-D-thiogalactopyranoside (IPTG) (32). The primers for the amplification and construction of genes and plasmids are listed in Table 2.…”

Section: Methodsmentioning

confidence: 99%

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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BslA, a pXO1‐encoded adhesin of Bacillus anthracis

Cited by 87 publications

References 57 publications

Effects of <i>Bacillus anthracis</i> hydrophobicity and induction of host cell death on sample collection from environmental surfaces

Effects of <i>Bacillus anthracis</i> hydrophobicity and induction of host cell death on sample collection from environmental surfaces

Structural Elucidation of the Nonclassical Secondary Cell Wall Polysaccharide from Bacillus cereus ATCC 10987

Bacillus anthracis SlaQ Promotes S-Layer Protein Assembly

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