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Applied and Environmental Microbiology, July 2006, p. 4845-4852, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.00279-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

A Protective Immune Response Is Generated in Rainbow Trout by an OmpH-Like Surface Antigen (P18) of Flavobacterium psychrophilum

Fabien Dumetz,1 Eric Duchaud,2 Scott E. LaPatra,3 Claire Le Marrec,4 Stéphane Claverol,5 Maria-C. Urdaci,1 and Michel Le Hénaff1*

Laboratoire de Microbiologie et de Biochimie Appliquées, Ecole Nationale d'Ingénieurs des Travaux Agricoles de Bordeaux, 1 Cours du Général de Gaulle, CS40201, F-33175 Gradignan, France,1 Unité de Virologie et Immunologie Moléculaires, INRA, Domaine de Vilvert, F-78352 Jouy-en-Josas, France,2 Clear Springs Foods, Inc., Research Division, Buhl, Idaho,3 Laboratoire de Biotechnologie et Microbiologie Appliquée, Université Victor Segalen Bordeaux 2 UMR INRA, Faculté d'Oenologie, 351 Cours de la Libération, F-33405 Talence, France,4 Plateforme Génomique Fonctionnelle, Université Victor Segalen Bordeaux 2, 146 Rue Léo Saignat, F-33076 Bordeaux, France5

Received 3 February 2006/ Accepted 29 April 2006

Investigations of the surface characteristics of Flavobacterium psychrophilum, an important pathogen of fish, assisted us in identifying a surface protein termed P18. In the current study, we developed a simple and efficient procedure for the purification of this protein by a two-step method. First, P18 was selectively released from flavobacteria by a heat-HEPES treatment of the cells and then subjected to anion-exchange high-performance liquid chromatography. De novo sequencing was used to generate a fragmented peptide spectrum from purified P18. Comparison of two obtained peptide sequences with a partial genome sequence of F. psychrophilum (INRA, Jouy-en-Josas, France) identified one gene encoding a 166-amino-acid OmpH-like protein that mostly likely undergoes N-terminal cleavage of the 23-residue signal peptide. The susceptibility of the OmpH-like protein to proteinase K treatment and the bacteriostatic/bactericidal activities of anti-OmpH-like protein antibodies indicated that this protein is actually exposed on the surface of F. psychrophilum. Vaccination trials showed that the OmpH-like protein can induce a high titer of anti-OmpH-like protein antibodies which are protective. Taken together, these results suggest that this surface protein produced by F. psychrophilum could be used in future vaccine development as a promising candidate antigen.

* Corresponding author. Mailing address: ENITAB, LMBA, 1 Cours du Général de Gaulle, CS40201, F-33175 Gradignan Cedex, France. Phone: 33 (0)557 350 738. Fax: 33 (0)557 350 739. E-mail: m-lehenaff{at}enitab.fr.

Applied and Environmental Microbiology, July 2006, p. 4845-4852, Vol. 72, No. 7
0099-2240/06/$08.00+0     doi:10.1128/AEM.00279-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Nicolas, P., Mondot, S., Achaz, G., Bouchenot, C., Bernardet, J.-F., Duchaud, E. (2008). Population Structure of the Fish-Pathogenic Bacterium Flavobacterium psychrophilum. Appl. Environ. Microbiol. 74: 3702-3709 [Abstract] [Full Text]  
  • Dumetz, F., Duchaud, E., Claverol, S., Orieux, N., Papillon, S., Lapaillerie, D., Le Henaff, M. (2008). Analysis of the Flavobacterium psychrophilum outer-membrane subproteome and identification of new antigenic targets for vaccine by immunomics. Microbiology 154: 1793-1801 [Abstract] [Full Text]  
  • Alvarez, B., Alvarez, J., Menendez, A., Guijarro, J. A. (2008). A mutant in one of two exbD loci of a TonB system in Flavobacterium psychrophilum shows attenuated virulence and confers protection against cold water disease. Microbiology 154: 1144-1151 [Abstract] [Full Text]  


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