Access the full text.
Sign up today, get DeepDyve free for 14 days.
U. Laemmli (1970)
Cleavage of structural proteins duringNature
(1997)
Generation of a membrane bound pre-pore complex is necessary for poreformation by C. perfringens alpha-toxin
A. Habeeb, Ching‐li Lee, M. Atassi (1973)
Conformational studies on modified proteins and peptides. VII. Conformation of ε-prototoxin and ε-toxin from Clostridium perfringens. Conformational changes associated with toxicityBiochimica et Biophysica Acta, 322
Valgerdur Steinthorsdottir, Haraldur Halldórsson, OÂlafur Andrésson (2000)
Clostridium perfringens beta-toxin forms multimeric transmembrane pores in human endothelial cells.Microbial pathogenesis, 28 1
L. Petit, E. Maier, M. Gibert, M. Popoff, R. Benz (2001)
Clostridium perfringens Epsilon Toxin Induces a Rapid Change of Cell Membrane Permeability to Ions and Forms Channels in Artificial Lipid Bilayers*The Journal of Biological Chemistry, 276
E. Tamai, T. Ishida, S. Miyata, O. Matsushita, H. Suda, Shoji Kobayashi, H. Sonobe, A. Okabe (2003)
Accumulation of Clostridium perfringens Epsilon-Toxin in the Mouse Kidney and Its Possible Biological SignificanceInfection and Immunity, 71
M. Perkins, R. Theiler, S. Lunte, M. Jeschke (2000)
Determination of the Origin of Charge Heterogeneity in a Murine Monoclonal AntibodyPharmaceutical Research, 17
B. Sellman, R. Tweten (1997)
The propeptide of Clostridium septicum alpha toxin functions as an intramolecular chaperone and is a potent inhibitor of alpha toxin‐dependent cytolysisMolecular Microbiology, 25
D. Liu (1993)
Deamidation: A Source of Microheterogeneity in Pharmaceutical ProteinsChemInform, 24
S. Ohri, D. Sharma, A. Dixit (2004)
Interaction of an approximately 40 kDa protein from regenerating rat liver with the -148 to -124 region of c-jun complexed with RLjunRP coincides with enhanced c-jun expression in proliferating rat liver.European journal of biochemistry, 271 23-24
M. Parker, S. Feil (2005)
Pore-forming protein toxins: from structure to function.Progress in biophysics and molecular biology, 88 1
S. Ohri, D. Sharma, A. Dixit (2004)
Interaction of an ≈ 40 kDa protein from regenerating rat liver with the −148 to −124 region of c-jun complexed with RLjunRP coincides with enhanced c-jun expression in proliferating rat liverFEBS Journal, 271
R. Titball (2009)
Clostridium perfringens vaccines.Vaccine, 27 Suppl 4
O. Knapp, E. Maier, R. Benz, B. Geny, M. Popoff (2009)
Identification of the channel-forming domain of Clostridium perfringens Epsilon-toxin (ETX).Biochimica et biophysica acta, 1788 12
D. Payne, E. Williamson, H. Havard, N. Modi, J. Brown (1994)
Evaluation of a new cytotoxicity assay for Clostridium perfringens type D epsilon toxin.FEMS microbiology letters, 116 2
R. WORTHINGTONt, M. Mulders
Physical Changes in the Epsilon Prototoxin Molecule of Clostridium perfringens During Enzymatic Activation
J. Sakùrai, M. Nagahama (1987)
Carboxyl groups in Clostridium perfringens epsilon toxin.Microbial pathogenesis, 3 6
M. Atassi, E. Nakhleh (1975)
Conformational studies on modified proteins and peptides. IX. Conformation and immunochemistry of hemoglobin reduced at some carboxyl groups by diborane.Biochimica et biophysica acta, 379 1
D. Gardner (1973)
Pathology of Clostridium welchii type D enterotoxaemia. II. Structural and ultrastructural alterations in the tissues of lambs and mice.Journal of comparative pathology, 83 4
L. Petit, M. Gibert, Daniel Gillet, Christine Laurent-Winter, Patrice Boquet, M. Popoff (1997)
Clostridium perfringens epsilon-toxin acts on MDCK cells by forming a large membrane complexJournal of Bacteriology, 179
B. McClane, G. Chakrabarti (2004)
New insights into the cytotoxic mechanisms of Clostridium perfringens enterotoxin.Anaerobe, 10 2
B. Promdonkoy, D. Ellar (2003)
Investigation of the pore-forming mechanism of a cytolytic delta-endotoxin from Bacillus thuringiensis.The Biochemical journal, 374 Pt 1
R. Thomson (1962)
Crystalline ɛ-Prototoxin from Clostridium welchiiNature, 193
M. Atassi, M. Perlstein, A.F.S.A. Habeeb (2003)
Conformational Studies on Modified Proteins and Peptides BY
A. Cole, M. Gibert, M. Popoff, D. Moss, R. Titball, A. Basak (2004)
Clostridium perfringens epsilon-toxin shows structural similarity to the pore-forming toxin aerolysin.Nature structural & molecular biology, 11 8
UK Laemmli (1970)
Cleavage of structural proteins using the assembly of the head of bacteriophage T4Nature, 227
Alex Soler-Jover, J. Dorca, M. Popoff, M. Gibert, J. Saura, J. Tusell, J. Serratosa, J. Blasi, M. Martín-Satué (2007)
Distribution of Clostridium perfringens epsilon toxin in the brains of acutely intoxicated mice and its effect upon glial cells.Toxicon : official journal of the International Society on Toxinology, 50 4
B. Sellman, B. Kagan, R. Tweten (1997)
Generation of a membrane‐bound, oligomerized pre‐pore complex is necessary for pore formation by Clostridium septicum alpha toxinMolecular Microbiology, 23
C. Zhu, M. Ghabriel, P. Blumbergs, Peter Reilly, J. Manavis, J. Youssef, S. Hatami, John Finnie (2001)
Clostridium perfringens Prototoxin-Induced Alteration of Endothelial Barrier Antigen (EBA) Immunoreactivity at the Blood–Brain Barrier (BBB)Experimental Neurology, 169
(2009)
Clostridium perfringens vaccines. Vaccine 27 (suppl 4):D44–D47
M. Nagahama, J. Sakùrai (1992)
High-affinity binding of Clostridium perfringens epsilon-toxin to rat brainInfection and Immunity, 60
R. Thomson (1962)
Crystalline epsilon-prototoxin from Clostridium welchii.Nature, 193
S. Hunter, I. Clarke, D. Kelly, R. Titball (1992)
Cloning and nucleotide sequencing of the Clostridium perfringens epsilon-toxin gene and its expression in Escherichia coliInfection and Immunity, 60
P. Goswami, P. Rupa, N. Prihar, L. Garg (1996)
Molecular cloning of Clostridium perfringens epsilon-toxin gene and its high level expression in E. coli.Biochemical and biophysical research communications, 226 3
D. Gardner (1973)
Pathology of Clostridium welchii type D enterotoxaemia. I. Biochemical and haematological alterations in lambs.Journal of comparative pathology, 83 4
M. Nakano, Y. Kawano, Mika Kawagishi, T. Hasegawa, Y. Iinuma, M. Ohta (2002)
Two‐Dimensional Analysis of Exoproteins of Methicillin‐Resistant Staphylococcus aureus (MRSA) for Possible Epidemiological ApplicationsMicrobiology and Immunology, 46
Axel Hildebrandlg, Margit Pohl, Sucharit Bhakdill (1991)
Staphylococcus aureus alpha-toxin. Dual mechanism of binding to target cells.The Journal of biological chemistry, 266 26
Clostridium perfringens types B and D are responsible for enterotoxaemia, one of the major causes of cattle mortality and is therefore of great economic concern. The epsilon toxin produced by the organism is the major antigenic determinant and has been directly implicated for the disease causation. In the present paper, we evaluated the biological activity of the recombinant epsilon toxin (rEtx) produced as soluble protein in Escherichia coli. The rEtx was purified to near homogeneity by a one-step anion-exchange chromatography. The immunological identity of purified rEtx was confirmed by Western blotting using a monoclonal antibody against the native toxin. The rEtx formed heptamer in the Madin–Darby canine kidney (MDCK) cells and synaptosomal membrane of mouse brain and was cytotoxic to the MDCK cells with a CT50 of 30 ng/ml. The rEtx was highly stable and its thermostability profile related well with its biological activity. The rEtx was purified in large amounts and exhibited all the properties of native toxin and therefore can be used for the development of vaccine against the pathogen.
Applied Microbiology and Biotechnology – Springer Journals
Published: Jul 31, 2010
Read and print from thousands of top scholarly journals.
Already have an account? Log in
Bookmark this article. You can see your Bookmarks on your DeepDyve Library.
To save an article, log in first, or sign up for a DeepDyve account if you don’t already have one.
Copy and paste the desired citation format or use the link below to download a file formatted for EndNote
Access the full text.
Sign up today, get DeepDyve free for 14 days.
All DeepDyve websites use cookies to improve your online experience. They were placed on your computer when you launched this website. You can change your cookie settings through your browser.