This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Erdenlig, S.
Right arrow Articles by Austin, F. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Erdenlig, S.
Right arrow Articles by Austin, F. W.
Agricola
Right arrow Articles by Erdenlig, S.
Right arrow Articles by Austin, F. W.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, July 1999, p. 2827-2832, Vol. 65, No. 7
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

Production of Monoclonal Antibodies to Listeria monocytogenes and Their Application To Determine the Virulence of Isolates from Channel Catfishdagger

Sevil Erdenlig, A. Jerald Ainsworth,* and Frank W. Austin

Veterinary Medical Research Program, College of Veterinary Medicine, Mississippi State University, Mississippi State, Mississippi 39762

Received 22 December 1998/Accepted 14 April 1999

We produced monoclonal antibodies (MAbs) to the extracellular proteins of Listeria monocytogenes EGD grown in Chelex-treated improved minimal medium. Ten of the positive hybridomas generated were chosen for further characterization. Seven of the MAbs reacted with a protein having a molecular mass of 60 kDa. These MAbs inhibited listeriolysin (LLO)-mediated hemolysis, and two of them were specific for LLO and none of the other thiol-activated toxins tested. In an enzyme-linked immunosorbent assay and Western blot analysis, five of the anti-LLO MAbs reacted with ivanolysin from Listeria ivanovii. Three of the 10 MAbs reacted with a 29-kDa protein on Western blots and neutralized the phosphatidylcholine-specific phospholipase C (PC-PLC) activity of L. monocytogenes. These three anti-PC-PLC MAbs did not react with phospholipases from five different gram-positive bacteria. However, the anti-PC-PLC MAbs recognized a 27-kDa extracellular protein from L. ivanovii and neutralized sphingomyelinase activity in a hemolysis test that demonstrates the antigenic relatedness of listerial phospholipases. These data indicate that listerial thiol-activated toxins possess species-specific epitopes and share group-specific epitopes. This is the first description of MAbs that neutralize listerial PC-PLC, and the data suggest that there is antigenic similarity between L. monocytogenes PC-PLC and L. ivanovii sphingomyelinase. The reactions of the MAbs with catfish isolates of L. monocytogenes suggested that some of the isolates examined lack the LLO and/or PC-PLC required for pathogenicity. The MAbs described here differentiated some catfish isolates from previously described type strain-pathogenic isolates and could be useful for detecting and determining the virulence of L. monocytogenes in food and clinical samples and for detecting L. ivanovii in veterinary clinical samples.

* Corresponding author. Mailing address: College of Veterinary Medicine, Box 9825, Mississippi State, MS 39762. Phone: (601) 325-1205. Fax: (601) 325-1031. E-mail: Ainsworth{at}cvm.msstate.edu.

dagger This paper is MAFES publication number J-9433.

Applied and Environmental Microbiology, July 1999, p. 2827-2832, Vol. 65, No. 7
0099-2240/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Autret, N., Raynaud, C., Dubail, I., Berche, P., Charbit, A. (2003). Identification of the agr Locus of Listeria monocytogenes: Role in Bacterial Virulence. Infect. Immun. 71: 4463-4471 [Abstract] [Full Text]  
  • Lety, M.-A., Frehel, C., Beretti, J.-l., Berche, P., Charbit, A. (2003). Modification of the signal sequence cleavage site of listeriolysin O does not affect protein secretion but impairs the virulence of Listeria monocytogenes. Microbiology 149: 1249-1255 [Abstract] [Full Text]  
  • Dubail, I., Autret, N., Beretti, J.-L., Kayal, S., Berche, P., Charbit, A. (2001). Functional assembly of two membrane-binding domains in listeriolysin O, the cytolysin of Listeria monocytogenes. Microbiology 147: 2679-2688 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»