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ARS Home » Southeast Area » Auburn, Alabama » Aquatic Animal Health Research » Research » Publications at this Location » Publication #240484
Title: Proteomic analysis of Flavobacterium psychrophilum cultured in vivo and in iron-limited media

Author
item Lafrentz, Benjamin
item LAPATRA, SCOTT - Clear Springs Foods, Inc
item CALL, DOUGLAS - Washington State University
item WIENS, GREGORY - US Department Of Agriculture (USDA)
item CAIN, KENNETH - University Of Idaho

Submitted to: Meeting Abstract
Publication Type: Abstract Only
Publication Acceptance Date: 7/1/2009
Publication Date: 9/21/2009
Citation: Lafrentz, B.R., Lapatra, S.E., Call, D.R., Wiens, G.D., Cain, K.D. 2009. Proteomic analysis of Flavobacterium psychrophilum cultured in vivo and in iron-limited media. In: Flavobacterium 2009 Conference, September 21-23, 2009, Paris, France. p. 46.

Interpretive Summary:

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 differentially regulated proteins of F. psychrophilum during in vivo and iron-limited growth conditions. A total of 20 proteins were observed to be differentially regulated 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 regulation in vivo, and included chaperone and stress proteins, a gliding motility protein, outer membrane proteins, and several proteins with unknown function. Two proteins exhibited decreased regulation in vivo and were identified as ferritin and an outer membrane protein. 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.