Identification of immunogenic proteins within distinct molecular mass fractions of Flavobacterium psychrophilum

Flavobacterium psychrophilum is the aetiological agent of bacterial coldwater disease (CWD), and this pathogen has large economic impacts on salmonid aquaculture worldwide. Previously, it was demonstrated that high levels of protection against F. psychrophilum challenge were conferred to rainbow tro...

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Bibliographic Details
Published inJournal of fish diseases Vol. 34; no. 11; pp. 823 - 830
Main Authors LaFrentz, B R, LaPatra, S E, Call, D R, Wiens, G D, Cain, K D
Format Journal Article
LanguageEnglish
Published Oxford, UK Blackwell Publishing Ltd 01.11.2011
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Summary:Flavobacterium psychrophilum is the aetiological agent of bacterial coldwater disease (CWD), and this pathogen has large economic impacts on salmonid aquaculture worldwide. Previously, it was demonstrated that high levels of protection against F. psychrophilum challenge were conferred to rainbow trout, Oncorhynchus mykiss (Walbaum), by immunization with distinct molecular mass fractions of the bacterium, and specific antibodies were correlated with protection. In this study, an immunoproteomic analysis of F. psychrophilum was performed using two‐dimensional polyacrylamide gel electrophoresis and Western blotting with serum from fish immunized with high‐ and mid‐molecular mass fractions of the bacterium. Mass spectrometry was used to determine the protein identity, and 15 immunogenic proteins were positively identified following Mascot searches of the F. psychrophilum genome. Based on known function and immunogenicity of homologous proteins in other bacterial pathogens, antibodies specific for several of the identified proteins may be important for protective immunity from CWD. These include outer membrane protein OmpA (P60), trigger factor, ClpB, elongation factor G, gliding motility protein GldN and a conserved hypothetical protein. This work increases the understanding of the protective humoral immune response of rainbow trout against these distinct molecular mass fractions of F. psychrophilum and provides new potential targets for recombinant protein vaccine development.
Bibliography:ArticleID:JFD1297
istex:5FCFCAB0B631C4B4D99820DDA0C3D50D0EFBF116
ark:/67375/WNG-1886M3G4-L
Present address: USDA‐ARS, Aquatic Animal Health Research Unit, 990 Wire Road, Auburn, AL 36832‐4352, USA.
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ISSN:0140-7775
1365-2761
DOI:10.1111/j.1365-2761.2011.01297.x