Bacillus anthracis surface: capsule and S-layer

Fouet, Agnès; Mesnage, Stéphane; Tosi‐Couture, Evelyne; Gounon, Pierre; Mock, Michèle

doi:10.1046/j.1365-2672.1999.00882.x

Cited by 40 publications

(34 citation statements)

References 21 publications

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“…Putative adhesins include the Slayer proteins (EA1 and Sap), teichoic acids, the poly-ª-Dglutamic acid capsule and fibronectin-and collagen-binding proteins (Ariel et al, 2003;Ezzell & Welkos, 1999;Fouet et al, 1999). The carbohydrate specificities displayed in this study (Table 2) were not due to interactions with the capsule, because the strain used lacked the pXO2 plasmid that encodes this virulence factor.…”

Section: Oligosaccharide Specificity In Relation To Bacterial Adhesinsmentioning

confidence: 93%

Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens

Thomas

Brooks

2004

Journal of Medical Microbiology

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Intervention in bacterial adhesion to host cells is a novel method of overcoming current problems associated with antibiotic resistance. Antibiotic-resistant strains of bacteria that cause respiratory tract infections are a problem in hospitals and could be used in bioterrorist attacks. A range of bacterial species was demonstrated to attach to an alveolar epithelial (A549) cell line. In all cases, cell surface oligosaccharides were important in attachment, demonstrated by reduced adhesion when A549 cells were pre-treated with tunicamycin. Bacillus anthracis and Yersinia pestis displayed a restricted tropism for oligosaccharides compared to the environmental, opportunistic pathogens, Pseudomonas aeruginosa, Burkholderia cenocepacia, Burkholderia pseudomallei and Legionella pneumophila. The compound with the greatest anti-adhesion activity was p-nitrophenol. Other generic attachment inhibitors included the polymeric saccharides (dextran and heparin), GalNAcâ1-4Gal, GalNAcâ1-3Gal, Galâ1-4GlcNAc and Galâ1-3GlcNAc. Burkholderia pseudomallei attachment was particularly susceptible to oligosaccharide inhibition. Combinations of such compounds may serve as a novel generic therapeutics for respiratory tract infections. INTRODUCTIONThe development of antibiotic resistance amongst pathogenic bacteria is a frequent occurrence and of great concern for public health. This problem is associated with many bacteria that cause community-and hospital-acquired pneumonia such as Streptococcus pneumoniae, Haemophilus influenzae, Pseudomonas aeruginosa and Burkholderia cenocepacia (Lister, 2000;Lynch, 2001;Spencer, 1995;Tan, 2003). Problems with antibiotic resistance can also extend to those bacteria that could be used in bioterrorism. It is likely that such bacterial threat agents would be delivered by the aerosol route resulting in respiratory presentation of the disease (Cieslak & Eitzen, 2000;Leggiadro, 2000). Given the ease of natural acquisition of antibiotic resistance genes and genetic manipulation, it is prudent to research therapeutic alternatives to antibiotics.Attachment to cell surfaces is one of the key steps in bacterial pathogenesis, often involving oligosaccharides located on the host cell surface and bacterial adhesins (Karlsson et al., 1992;Ofek & Sharon, 1990). The terminal di-or trisaccharide units of these oligosaccharides may be used to inhibit these interactions, preventing attachment and hence disease (Zopf & Roth, 1996). The theory has been proven in vitro with a range of bacterial species. For example, lacto-N-neotetraose and asialoganglioside-GM1 (asialo-GM1) inhibit attachment of S. pneumoniae to alveolar epithelial cells (Tong et al., 1999). Similarly 3-sialyllactose inhibits Helicobacter pylori attachment to gastric epithelial cells . Asialoganglioside-GM1 and -GM2 are used as receptors by a number of respiratory pathogens, which specifically bind their terminal GalNAcâ1-3Gal and GalNAcâ1-4Gal moieties (Krivan et al., 1988a(Krivan et al., , b, 1991. The principle has also been proven to be valid in vivo...

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Section: Oligosaccharide Specificity In Relation To Bacterial Adhesinsmentioning

confidence: 93%

Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens

Thomas

Brooks

2004

Journal of Medical Microbiology

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“…The B. anthracis cell surface, in the vegetative nonencapsulated state as well as the capsulated state, is covered by a cell wall polymer, known as the surface layer (or S-layer [23,50,52,84]). Various functions have been assigned to the S-layer, ranging from shape maintenance to virulence, host recognition evasion, cell adhesion and resistance to phagocytosis (52,58,84).…”

Section: Resultsmentioning

confidence: 99%

Genome-Based Bioinformatic Selection of ChromosomalBacillus anthracisPutative Vaccine Candidates Coupled with Proteomic Identification of Surface-Associated Antigens

et al. 2003

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“…This was not the case with B. anthracis because treatment of encapsulated B. anthracis with DMSO had no apparent effect on either capsule size or the ability of MAbs to produce capsule reactions. The B. anthracis cell wall is surrounded by two abundant surface proteins, extractable antigen 1 and surface array protein, that comprise the B. anthracis S-layer (9). The capsule overlies the S-layer.…”

Section: Discussionmentioning

confidence: 99%

Protective and Immunochemical Activities of Monoclonal Antibodies Reactive with theBacillus anthracisPolypeptide Capsule

Kozel¹,

Thorkildson²,

Brandt³

et al. 2007

Infect Immun

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Bacillus anthracis is surrounded by a polypeptide capsule composed of poly-gamma-D-glutamic acid (␥DPGA). In a previous study, we reported that a monoclonal antibody (MAb F26G3) reactive with the capsular polypeptide is protective in a murine model of pulmonary anthrax. The present study examined a library of six MAbs generated from mice immunized with ␥DPGA. Evaluation of MAb binding to the capsule by a capsular "quellung" type reaction showed a striking diversity in capsular effects. Most MAbs produced a rim type reaction that was characterized by a sharp increase followed directly by a decrease in refractive index at the capsular edge. Some MAbs produced a second capsular reaction well beneath the capsular edge, suggesting complexity in capsular architecture. Binding of MAbs to soluble ␥DPGA was assessed by a fluorescence perturbation assay in which a change in the MAb intrinsic fluorescence produced by ligand binding was used as a reporter for antigen-antibody interaction. The MAbs differed considerably in the complexity of the binding curves. MAbs producing rim type capsule reactions typically produced the more complex binding isotherms. Finally, the protective activity of the MAbs was compared in a murine model of pulmonary anthrax. One MAb was markedly less protective than the remaining five MAbs. Characteristics of the more protective MAbs included a relatively high affinity, an immunoglobulin G3 isotype, and a complex binding isotherm in the fluorescence perturbation assay. Given the relatively monotonous structure of ␥DPGA, the results demonstrate a striking diversity in the antigen binding behavior of ␥DPGA antibodies.

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Bacillus anthracis surface: capsule and S-layer

Cited by 40 publications

References 21 publications

Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens

Common oligosaccharide moieties inhibit the adherence of typical and atypical respiratory pathogens

Genome-Based Bioinformatic Selection of ChromosomalBacillus anthracisPutative Vaccine Candidates Coupled with Proteomic Identification of Surface-Associated Antigens

Protective and Immunochemical Activities of Monoclonal Antibodies Reactive with theBacillus anthracisPolypeptide Capsule

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