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A factor converting viable but nonculturable Vibrio cholerae to a culturable state in eukaryotic cells is a human catalase.

Senoh M, Hamabata T, Takeda Y - Microbiologyopen (2015)

Bottom Line: Homogeneity of the purified FCVC was demonstrated by SDS-PAGE.Nano-LC MS/MS analysis showed that the purified FCVC was a human catalase.An experiment of RNAi knockdown of catalase mRNA from HT-29 cells and treatment of the purified FCVC with a catalase inhibitor, 3-amino-1,2,4-triazole confirmed that the FCVC was a catalase.

View Article: PubMed Central - PubMed

Affiliation: Collaborative Research Center of Okayama University for Infectious Diseases in India, Okayama University, Kolkata, India.

No MeSH data available.


Related in: MedlinePlus

Activity of cell extracts from catalase siRNA-transfected HT-29 cells. Cell extracts of catalase siRNA-transfected HT-29 cells were prepared, and measured for their converting activity (A) and catalase activity (B) were measured as described in the text. The culturability of VBNC Vibrio cholerae by incubation at 37°C for 16 h in APW without FCVC was not detected. Bars represent means ± SD of four determinations.
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fig02: Activity of cell extracts from catalase siRNA-transfected HT-29 cells. Cell extracts of catalase siRNA-transfected HT-29 cells were prepared, and measured for their converting activity (A) and catalase activity (B) were measured as described in the text. The culturability of VBNC Vibrio cholerae by incubation at 37°C for 16 h in APW without FCVC was not detected. Bars represent means ± SD of four determinations.

Mentions: To obtain further evidence, we employed an siRNA to knockdown the catalase expression in HT-29 cells and examine the effect on the VBNC-converting activity of the purified FCVC. As shown in Figure2A, siRNA-induced reduction of catalase expression resulted in a significant decrease in the FCVC activity. The rate of decrease in the FCVC activity shown in Figure2A was almost the same as the decrease in the H2O2-degrading activity (catalase activity) shown in Figure2B.


A factor converting viable but nonculturable Vibrio cholerae to a culturable state in eukaryotic cells is a human catalase.

Senoh M, Hamabata T, Takeda Y - Microbiologyopen (2015)

Activity of cell extracts from catalase siRNA-transfected HT-29 cells. Cell extracts of catalase siRNA-transfected HT-29 cells were prepared, and measured for their converting activity (A) and catalase activity (B) were measured as described in the text. The culturability of VBNC Vibrio cholerae by incubation at 37°C for 16 h in APW without FCVC was not detected. Bars represent means ± SD of four determinations.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4554454&req=5

fig02: Activity of cell extracts from catalase siRNA-transfected HT-29 cells. Cell extracts of catalase siRNA-transfected HT-29 cells were prepared, and measured for their converting activity (A) and catalase activity (B) were measured as described in the text. The culturability of VBNC Vibrio cholerae by incubation at 37°C for 16 h in APW without FCVC was not detected. Bars represent means ± SD of four determinations.
Mentions: To obtain further evidence, we employed an siRNA to knockdown the catalase expression in HT-29 cells and examine the effect on the VBNC-converting activity of the purified FCVC. As shown in Figure2A, siRNA-induced reduction of catalase expression resulted in a significant decrease in the FCVC activity. The rate of decrease in the FCVC activity shown in Figure2A was almost the same as the decrease in the H2O2-degrading activity (catalase activity) shown in Figure2B.

Bottom Line: Homogeneity of the purified FCVC was demonstrated by SDS-PAGE.Nano-LC MS/MS analysis showed that the purified FCVC was a human catalase.An experiment of RNAi knockdown of catalase mRNA from HT-29 cells and treatment of the purified FCVC with a catalase inhibitor, 3-amino-1,2,4-triazole confirmed that the FCVC was a catalase.

View Article: PubMed Central - PubMed

Affiliation: Collaborative Research Center of Okayama University for Infectious Diseases in India, Okayama University, Kolkata, India.

No MeSH data available.


Related in: MedlinePlus