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

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.

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