Location: Cool and Cold Water Aquaculture ResearchTitle: Global proteomic profiling of Yersinia ruckeri strains Author
|Kumar, Gokhlesh - University Of Veterinary Medicine|
|Hummel, Karin - University Of Veterinary Medicine|
|Welch, Timothy - Tim|
|Razzazi-fazeli, Ebrahim - University Of Veterinary Medicine|
|El-matbouli, Mansour - University Of Veterinary Medicine|
Submitted to: Veterinary Research
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 9/6/2017
Publication Date: 9/20/2017
Citation: Kumar, G., Hummel, K., Welch, T.J., Razzazi-Fazeli, E., El-Matbouli, M. 2017. Global proteomic profiling of Yersinia ruckeri strains [online serial]. Veterinary Research. 48:55. https://doi.org/10.1186/s13567-017-0460-3.
DOI: https://doi.org/10.1186/s13567-017-0460-3 Interpretive Summary: Yersinia ruckeri causes enteric red mouth disease (ERM), an invasive septicemia that affects farmed salmonid fish species worldwide. Despite the importance of this disease, very little is known regarding the protein expression patterns of Y. ruckeri. In this paper, we present the identification and quantification of the whole-cell proteins of Y. ruckeri strains using a shotgun proteomic approach. This descriptive study revealed a total of 1395 proteins expressed by Y. ruckeri under laboratory growth conditions. Proteins identified included proteases, chaperones, cell division proteins, outer membrane proteins, lipoproteins, receptors, ion binding proteins, transporters and catalytic proteins. In addition, potential virulence and antimicrobial resistance proteins were identified which could be used for the development of vaccine targets for the treatment of ERM in fish. This work represents one of the first global proteomic reference profiles of Y. ruckeri and will aid in the elucidation of virulence and antimicrobial resistance mechanisms in this important pathogen.
Technical Abstract: Yersinia ruckeri is the causative agent of enteric red mouth disease (ERM) of salmonids. There is little information regarding the proteomics of Y. ruckeri. Herein, we perform whole protein identification and quantification of biotype 1 and biotype 2 strains of Y. ruckeri grown under standard culture conditions using a shotgun proteomic approach. Proteins were extracted, digested and peptides were separated by a nano liquid chromatography system and analyzed with a high-resolution hybrid triple quadrupole time of flight mass spectrometer coupled via a nano ESI interface. SWATH-MS technology and sophisticated statistical analyses were used to identify proteome differences among virulent and avirulent strains. GO annotation, subcellular localization, virulence proteins and antibiotic resistance ontology were predicted using bioinformatic tools. A total of 1395 proteins were identified in the whole cell of Y. ruckeri. These included proteases, chaperones, cell division proteins, outer membrane proteins, lipoproteins, receptors, ion binding proteins, transporters and catalytic proteins. In virulent strains, a total of 16 proteins were upregulated including anti-sigma regulatory factor, arginine deiminase, phosphate-binding protein PstS and superoxide dismutase Cu-Zu. Additionally, several virulence proteins were predicted such as Clp and Lon pro TolB, PPIases, PstS, PhoP and LuxR family transcriptional regulators. These putative virulence proteins might be used for development of novel targets for treatment of ERM in fish. Our study represents one of the first global proteomic reference profiles of Y. ruckeri and this data can be accessed via ProteomeXchange with identifier PXD005439. These proteomic profiles elucidate proteomic mechanisms, pathogenicity, host-interactions, antibiotic resistance and localization of Y. ruckeri proteins.