Proteomic analysis of Flavobacterium psychrophilum cultured in vivo and in iron-limited media

B R LaFrentz; S E LaPatra; D R Call; G D Wiens; K D Cain

doi:10.3354/dao02122

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Proteomic analysis of Flavobacterium psychrophilum cultured in vivo and in iron-limited media

Journal article

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Proteomic analysis of Flavobacterium psychrophilum cultured in vivo and in iron-limited media

B R LaFrentz, S E LaPatra, D R Call, G D Wiens and K D Cain

Diseases of aquatic organisms, Vol.87(3), pp.171-182

12/03/2009

DOI: https://doi.org/10.3354/dao02122

Handle:

https://hdl.handle.net/2376/110829

PMID: 20099411

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Abstract

Fish Diseases - microbiology

Iron - chemistry

Bacterial Proteins - genetics

Gene Expression Profiling

Flavobacterium - drug effects

Oncorhynchus mykiss

Flavobacteriaceae Infections - microbiology

Flavobacteriaceae Infections - veterinary

Gene Expression Regulation, Bacterial - drug effects

Animals

Flavobacterium - physiology

Bacterial Proteins - metabolism

Bacteriological Techniques

Culture Media - chemistry

Iron - pharmacology

Flavobacterium psychrophilum is the etiologic agent of bacterial coldwater disease, but the pathogenic mechanisms of this important fish pathogen are not fully understood. Identifying bacterial genes of F. psychrophilum differentially expressed in vivo may lead to a better understanding of pathogenesis and provide targets for vaccine development. Therefore, the present study used a proteomic approach to identify and quantify proteins of F. psychrophilum following growth in vivo and under iron-limited growth conditions. As determined by 2D polyacrylamide gel electrophoresis (2D-PAGE), numerous proteins exhibited different spot intensities following culture of the bacterium in vivo, and of these, 20 were selected and identified by liquid chromatography-mass spectrometry/mass spectrometry (LC-MS/MS) analysis and Mascot searches of the F. psychrophilum genome. Eighteen proteins exhibited increased spot intensities in vivo, and these included: several chaperone and stress proteins, gliding motility protein GldN, outer membrane protein OmpH, 2 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 spot intensities 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 protein spot intensity changes for 6 of the 20 proteins identified following growth in vivo. Results from the present study suggest a role of upregulated proteins in the pathogenesis of F. psychrophilum and these may represent potential vaccine candidate antigens.

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Title: Proteomic analysis of Flavobacterium psychrophilum cultured in vivo and in iron-limited media
Creators: B R LaFrentz - Department of Fish and Wildlife Resources and the Aquaculture Research Institute, University of Idaho, PO Box 441136, Moscow, Idaho 83844-1136, USA
S E LaPatra
D R Call
G D Wiens
K D Cain
Publication Details: Diseases of aquatic organisms, Vol.87(3), pp.171-182
Academic Unit: Center for Reproductive Biology; Paul G. Allen School for Global Animal Health
Publisher: Germany
Identifiers: 99900547006401842
Language: English
Resource Type: Journal article