Stable isotope labelling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Edwardsiella tarda ATCC 15947 under prolonged cold stress. (December 2018)
- Record Type:
- Journal Article
- Title:
- Stable isotope labelling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Edwardsiella tarda ATCC 15947 under prolonged cold stress. (December 2018)
- Main Title:
- Stable isotope labelling by amino acids in cell culture (SILAC) applied to quantitative proteomics of Edwardsiella tarda ATCC 15947 under prolonged cold stress
- Authors:
- Ma, Weixing
Jia, Juntao
Huang, Xiaohua
Xie, Wancui
Zhang, Xiaoliang
Tang, Jing
Lin, Chao
Zhao, Liqing
Fang, Peipei - Abstract:
- Abstract: Edwardsiella tarda poses a threat to human health and has resulted in enormous economic losses in aquaculture. Low temperatures are usually applied to contain the growth of this microorganism. In this study, stable isotope labelling by amino acids in cell culture (SILAC) was used to conduct comparative proteomic quantitation of E. tarda ATCC 15947 under cold stress for two weeks. We identified 1391 proteins, of which 898 were quantifiable. Of these, 72 proteins were upregulated and 164 were downregulated in response to cold stress. Even though E. tarda ATCC 15947 is not a psychrophile, several key proteins related to DNA synthesis and transcription were significantly upregulated. Additionally, proteins related to haemolytic activities and gluconeogenesis were upregulated, even though E. tarda ATCC 15497 is considered non-virulent in aquaculture. This study therefore delineated the specific proteomic response of this E. tarda ATCC 15947 to prolonged cold stress. Highlights: Edwardsiella tarda is not a psychrophile, however some key proteins related to DNA synthesis and transcription are significantly upregulated after incubation at 4 °C for 2 weeks. Some proteins related to hemolytic activities in Edwardsiella tarda ATCC 15947 (non-virulent to aquaculture) are significantly upregulated after incubation at 4 °C for 2 weeks. Fructose 1, 6-bisphosphatase (the critical enzyme to control gluconeogenesis reaction rates), DNA starvation/stationary phase protection proteinAbstract: Edwardsiella tarda poses a threat to human health and has resulted in enormous economic losses in aquaculture. Low temperatures are usually applied to contain the growth of this microorganism. In this study, stable isotope labelling by amino acids in cell culture (SILAC) was used to conduct comparative proteomic quantitation of E. tarda ATCC 15947 under cold stress for two weeks. We identified 1391 proteins, of which 898 were quantifiable. Of these, 72 proteins were upregulated and 164 were downregulated in response to cold stress. Even though E. tarda ATCC 15947 is not a psychrophile, several key proteins related to DNA synthesis and transcription were significantly upregulated. Additionally, proteins related to haemolytic activities and gluconeogenesis were upregulated, even though E. tarda ATCC 15497 is considered non-virulent in aquaculture. This study therefore delineated the specific proteomic response of this E. tarda ATCC 15947 to prolonged cold stress. Highlights: Edwardsiella tarda is not a psychrophile, however some key proteins related to DNA synthesis and transcription are significantly upregulated after incubation at 4 °C for 2 weeks. Some proteins related to hemolytic activities in Edwardsiella tarda ATCC 15947 (non-virulent to aquaculture) are significantly upregulated after incubation at 4 °C for 2 weeks. Fructose 1, 6-bisphosphatase (the critical enzyme to control gluconeogenesis reaction rates), DNA starvation/stationary phase protection protein and universal stress proteins (related to stress resistance) were significantly upregulated after incubation at 4 °C for 2 weeks. … (more)
- Is Part Of:
- Microbial pathogenesis. Volume 125(2018)
- Journal:
- Microbial pathogenesis
- Issue:
- Volume 125(2018)
- Issue Display:
- Volume 125, Issue 2018 (2018)
- Year:
- 2018
- Volume:
- 125
- Issue:
- 2018
- Issue Sort Value:
- 2018-0125-2018-0000
- Page Start:
- 12
- Page End:
- 19
- Publication Date:
- 2018-12
- Subjects:
- SILAC -- Proteomics -- Edwardsiella tarda ATCC 15947 -- Cold stress -- Aquaculture -- Virulence
SILAC stable isotope labelling by amino acids in cell culture -- RP-HPLC reverse-phase high-performance liquid chromatography -- ESI electrospray ionisation -- iTRAQ isobaric tags for relative and absolute quantitation -- FDR false discovery rate -- GAPDH glyceraldehyde-3-phosphate dehydrogenase -- FBAA-II fructose-bisphosphate aldolase class II -- Omps outer membrane proteins -- OmpA outer membrane protein A -- MutS DNA mismatch repair protein -- FBP fructose 1, 6-bisphosphatase -- G/HRA glyoxylate/hydroxypyruvate reductase A -- Dps DNA starvation/stationary phase protection protein -- USPs universal stress proteins -- GO gene ontology -- PANTHER protein analysis through evolutionary relationships -- KEGG Kyoto Encyclopedia of Gene and Genomes -- T3SS type III secretion system -- T6SS type VI secretion system -- TCE time course expression -- PSMs peptide-spectrum matches
Pathogenic microorganisms -- Periodicals
Pathology, Molecular -- Periodicals
Communicable Diseases -- microbiology -- Periodicals
Communicable Diseases -- parasitology -- Periodicals
Micro-organismes pathogènes -- Périodiques
Pathologie moléculaire -- Périodiques
Electronic journals
616.9041 - Journal URLs:
- http://www.sciencedirect.com/science/journal/08824010 ↗
http://firstsearch.oclc.org ↗
http://firstsearch.oclc.org/journal=0882-4010;screen=info;ECOIP ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.micpath.2018.09.006 ↗
- Languages:
- English
- ISSNs:
- 0882-4010
- Deposit Type:
- Legaldeposit
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