title: Antimicrobial activity of different proteins and their fragments from Bacillus thuringiensis parasporal crystals against clostridia and archaea.
abstract: Proteins of parasporal crystals (Cry proteins) from entomopathogenic bacterium Bacillus thuringiensis (subspecies kurstaki, galleriae, tenebrionis) as well as some fragments of these proteins, obtained by limited proteolysis, are capable of antimicrobial action against anaerobic bacteria and archaea-Clostridium butyricum, Clostridium acetobutylicum and Methanosarcina barkeri. The MICs are 45-150 microg/mL. Electron microscopy showed that lysis of M. barkeri cells in the presence of 49kDa fragment of Cry3Aa toxin is generally similar to the bacterial cell lysis, which has been previously detected in the presence of Cry11A, Cry1Ab and other Cry proteins. The Cry1D-like toxin from crystals of B. thuringiensis subsp. galleriae has been put forward as an example of the supposition that cell wall and some of its components like teichoic acid and N-acetylgalactosamine have possible influence on Cry toxins, enhancing their antimicrobial activity. The possible ecological role of the antimicrobial activity of Cry proteins is also discussed.
authors.affiliation: Department of Microbiology, Biological Faculty, M.V. Lomonosov Moscow State University, Leninskie Gory 1/12, 119992 Moscow, Russian Federation.
authors.forename: Tatyana G
authors.initials: TG
authors.lastname: Yudina
authors.forename: Andrei L
authors.initials: AL
authors.lastname: Brioukhanov
authors.forename: Igor A
authors.initials: IA
authors.lastname: Zalunin
authors.forename: Ludmila P
authors.initials: LP
authors.lastname: Revina
authors.forename: Andrei I
authors.initials: AI
authors.lastname: Shestakov
authors.forename: Nina E
authors.initials: NE
authors.lastname: Voyushina
authors.forename: Galina G
authors.initials: GG
authors.lastname: Chestukhina
authors.forename: Alexander I
authors.initials: AI
authors.lastname: Netrusov
mesh_terms: D001105:Archaea / Q000187:drug effects*; D001413:Bacillus thuringiensis / Q000737:chemistry* / Q000378:metabolism; D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D001427:Bacterial Toxins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D003013:Clostridium / Q000187:drug effects*; D004591:Electrophoresis, Polyacrylamide Gel / Q000379:methods; D004731:Endotoxins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D006460:Hemolysin Proteins / Q000737:chemistry / Q000302:isolation & purification / Q000494:pharmacology*; D008826:Microbial Sensitivity Tests; D010446:Peptide Fragments / Q000737:chemistry / Q000494:pharmacology*
chemical_list: D000083722:Bacillus thuringiensis Toxins; D001426:Bacterial Proteins; D001427:Bacterial Toxins; D004731:Endotoxins; D006460:Hemolysin Proteins; D010446:Peptide Fragments; C030956:insecticidal crystal protein, Bacillus Thuringiensis