Structure of the exosporium and sublayers of spores of the Bacillus cereus family revealed by electron crystallography
| Autor: | Patricia Sylvestre, Robert Taylor, Anne Moir, Evelyne Couture-Tosi, David A. Ball, Per A. Bullough, Sarah J. Todd, Caroline Redmond |
|---|---|
| Přispěvatelé: | Department of Molecular Biology and Biotechnology, University of Sheffield [Sheffield], Defence Science and Technology Laboratory (Dstl), Ministry of Defence (UK) (MOD), Toxines et Pathogénie Bactérienne, Institut Pasteur [Paris] (IP)-Centre National de la Recherche Scientifique (CNRS), Centre National de la Recherche Scientifique (CNRS)-Institut Pasteur [Paris] |
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Bacillus cereus
MESH: Microscopy Electron Microbiology Endospore law.invention 03 medical and health sciences Bacterial Proteins MESH: Spores Bacterial law Molecular Biology MESH: Bacterial Proteins 030304 developmental biology Alanine Spores Bacterial 0303 health sciences Bacillaceae Crystallography biology 030306 microbiology Electron crystallography MESH: Crystallography fungi Exosporium biology.organism_classification GroEL [SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/Bacteriology Microscopy Electron Biochemistry MESH: Bacillus cereus Biophysics Electron microscope |
| Zdroj: | Molecular Microbiology Molecular Microbiology, 2008, 68 (4), pp.947-58. ⟨10.1111/j.1365-2958.2008.06206.x⟩ Molecular Microbiology, Wiley, 2008, 68 (4), pp.947-58. ⟨10.1111/j.1365-2958.2008.06206.x⟩ |
| ISSN: | 0950-382X 1365-2958 |
| DOI: | 10.1111/j.1365-2958.2008.06206.x⟩ |
| Popis: | International audience; We report on the first step in mapping out the spatial location of structural proteins within the exosporium, namely a description of its three-dimensional architecture. Using electron microscopy and image analysis, we have characterized crystalline fragments from the exosporium of Bacillus cereus, B. thuringiensis and B. anthracis strains and identified up to three distinct crystal types. Type I and type II crystals were examined in three dimensions and shown to form arrays of interlinked crown-like structures each enclosing a cavity approximately 26-34 A deep with threefold symmetry. The arrays appear to be permeated by tunnels allowing access from one surface to the other, possibly indicating that the exosporium forms a semi-permeable barrier. The pore size of approximately 23-34 A would allow passage of the endospore germinants, alanine or inosine but not degradative enzymes or antibodies. Thus the structures appear compatible with a protective role for the exosporium. Furthermore the outermost crystalline layer must act as a scaffold for binding the BclA protein that contributes to the 'hairy nap' layer. The array of crowns may also act as a matrix for the binding or adsorption of other proteins that have been identified in the exosporium such as GroEL, immune inhibitor A and arginase. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Plný text