IAI FigSearch
Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Other Versions of this Article:
IAI.01643-06v1
75/4/1785    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by McClain, M. S.
Right arrow Articles by Cover, T. L.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by McClain, M. S.
Right arrow Articles by Cover, T. L.

 Previous Article  |  Next Article 

Infection and Immunity, April 2007, p. 1785-1793, Vol. 75, No. 4
0019-9567/07/$08.00+0     doi:10.1128/IAI.01643-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Functional Analysis of Neutralizing Antibodies against Clostridium perfringens Epsilon-Toxin{triangledown}

Mark S. McClain1* and Timothy L. Cover1,2,3

Departments of Medicine,1 Microbiology and Immunology, Vanderbilt University School of Medicine, Nashville, Tennessee 37232,2 Veterans Affairs Tennessee Valley Healthcare System, Nashville, Tennessee3

Received 11 October 2006/ Returned for modification 13 November 2006/ Accepted 15 January 2007

The Clostridium perfringens epsilon-toxin causes a severe, often fatal illness (enterotoxemia) characterized by cardiac, pulmonary, kidney, and brain edema. In this study, we examined the activities of two neutralizing monoclonal antibodies against the C. perfringens epsilon-toxin. Both antibodies inhibited epsilon-toxin cytotoxicity towards cultured MDCK cells and inhibited the ability of the toxin to form pores in the plasma membranes of cells, as shown by staining cells with the membrane-impermeant dye 7-aminoactinomycin D. Using an antibody competition enzyme-linked immunosorbent assay (ELISA), a peptide array, and analysis of mutant toxins, we mapped the epitope recognized by one of the neutralizing monoclonal antibodies to amino acids 134 to 145. The antibody competition ELISA and analysis of mutant toxins suggest that the second neutralizing monoclonal antibody also recognizes an epitope in close proximity to this region. The region comprised of amino acids 134 to 145 overlaps an amphipathic loop corresponding to the putative membrane insertion domain of the toxin. Identifying the epitopes recognized by these neutralizing antibodies constitutes an important first step in the development of therapeutic agents that could be used to counter the effects of the epsilon-toxin.

* Corresponding author. Mailing address: Division of Infectious Diseases, A2200 Medical Center North, Vanderbilt University School of Medicine, Nashville, TN 37232. Phone: (615) 322-2035. Fax: (615) 343-6160. E-mail: mark.mcclain{at}vanderbilt.edu.

{triangledown} Published ahead of print on 29 January 2007.

Editor: D. L. Burns

Infection and Immunity, April 2007, p. 1785-1793, Vol. 75, No. 4
0019-9567/07/$08.00+0     doi:10.1128/IAI.01643-06
Copyright © 2007, American Society for Microbiology. All Rights Reserved.





Home Help [Feedback] [For Subscribers] [Archive] [Search] [Contents]
J. Bacteriol. J. Virol. Eukaryot. Cell
Microbiol. Mol. Biol. Rev. Clin. Vaccine Immunol. All ASM Journals

Copyright © 2007 by the American Society for Microbiology. All rights reserved.