ARS | Publication request: Proteomic Analysis of Flavobacterium psychrophilum cultured In Vivo and In Iron-Limited Media

Submitted to: American Fisheries Society Annual Meeting
Publication Type: Abstract Only
Publication Acceptance Date: June 30, 2008
Publication Date: July 13, 2008
Citation: Lafrentz, B.R., Lapatra, S., Call, D., Wiens, G., Cain, K. 2008. Proteomic Analysis of Flavobacterium psychrophilum cultured In Vivo and In Iron-Limited Media. In: Proceedings of the American Fisheries Society Fish Health Section, July 14 - 12, 2008, Charlottetown, Prince Edward Island, Canada, p.140.

Technical Abstract: Flavobacterium psychrophilum is the etiologic agent of bacterial coldwater disease and the pathogenic mechanisms of this important fish pathogen are not fully understood. Identifying bacterial components expressed in vivo may lead to a better understanding of pathogenesis and provide targets for vaccine development. Therefore, this study used a proteomic approach to identify proteins of F. psychrophilum expressed during in vivo and iron-limited growth conditions. A total of 20 proteins were observed to be differentially expressed following culture of the bacterium in vivo and these were positively identified by LC-MS/MS analysis and Mascot searches of the F. psychrophilum genome. A number of proteins exhibited increased expression in vivo, and these included: several chaperone and heat shock proteins, the gliding motility protein GldN, outer membrane protein OmpH, two probable outer membrane proteins (OmpA family), probable aminopeptidase precursor, probable lipoprotein precursor, 3-oxoacyl-[acyl-carrier-protein]-reductase, and several proteins with unknown function. Two proteins exhibited decreased expression in vivo and were identified as ferritin FtnA and outer membrane protein OmpA (P60). Culture of F. psychrophilum in iron-limited media resulted in similar expression for some of the identified proteins. The results suggest that some of these proteins may be involved in the pathogenesis of F. psychrophilum and may serve as vaccine candidate antigens.