title: Glycosylation of BclA Glycoprotein from Bacillus cereus and Bacillus anthracis Exosporium Is Domain-specific.
abstract: The spores of the Bacillus cereus group (B. cereus, Bacillus anthracis, and Bacillus thuringiensis) are surrounded by a paracrystalline flexible yet resistant layer called exosporium that plays a major role in spore adhesion and virulence. The major constituent of its hairlike surface, the trimerized glycoprotein BclA, is attached to the basal layer through an N-terminal domain. It is then followed by a repetitive collagen-like neck bearing a globular head (C-terminal domain) that promotes glycoprotein trimerization. The collagen-like region of B. anthracis is known to be densely substituted by unusual O-glycans that may be used for developing species-specific diagnostics of B. anthracis spores and thus targeted therapeutic interventions. In the present study, we have explored the species and domain specificity of BclA glycosylation within the B. cereus group. First, we have established that the collagen-like regions of both B. anthracis and B. cereus are similarly substituted by short O-glycans that bear the species-specific deoxyhexose residues anthrose and the newly observed cereose, respectively. Second we have discovered that the C-terminal globular domains of BclA from both species are substituted by polysaccharide-like O-linked glycans whose structures are also species-specific. The presence of large carbohydrate polymers covering the surface of Bacillus spores may have a profound impact on the way that spores regulate their interactions with biotic and abiotic surfaces and represents potential new diagnostic targets.
authors.affiliation: From the Université de Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France and.
authors.forename: Emmanuel
authors.initials: E
authors.lastname: Maes
authors.affiliation: From the Université de Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France and.
authors.forename: Frederic
authors.initials: F
authors.lastname: Krzewinski
authors.affiliation: From the Université de Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France and.
authors.forename: Estelle
authors.initials: E
authors.lastname: Garenaux
authors.affiliation: INRA, UMR8207, F-59650 Villeneuve d'Ascq, France.
authors.forename: Yannick
authors.initials: Y
authors.lastname: Lequette
authors.affiliation: From the Université de Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France and.
authors.forename: Bernadette
authors.initials: B
authors.lastname: Coddeville
authors.affiliation: From the Université de Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France and.
authors.forename: Xavier
authors.initials: X
authors.lastname: Trivelli
authors.affiliation: INRA, UMR8207, F-59650 Villeneuve d'Ascq, France.
authors.forename: Annette
authors.initials: A
authors.lastname: Ronse
authors.affiliation: INRA, UMR8207, F-59650 Villeneuve d'Ascq, France.
authors.forename: Christine
authors.initials: C
authors.lastname: Faille
authors.affiliation: From the Université de Lille, CNRS, UMR 8576-UGSF-Unité de Glycobiologie Structurale et Fonctionnelle, F-59000 Lille, France and yann.guerardel@univ-lille1.fr.
authors.forename: Yann
authors.initials: Y
authors.lastname: Guerardel
mesh_terms: D001408:Bacillus anthracis / Q000502:physiology*; D001409:Bacillus cereus / Q000502:physiology*; D006031:Glycosylation; D008562:Membrane Glycoproteins / Q000235:genetics / Q000378:metabolism*; D011135:Polysaccharides, Bacterial / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D013045:Species Specificity; D013171:Spores, Bacterial
chemical_list: C470593:BclA protein, Bacillus anthracis; D008562:Membrane Glycoproteins; D011135:Polysaccharides, Bacterial
keywords: Bacillus; carbohydrate structure; cell surface; exosporium; glycoprotein; polysaccharide; spore