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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

Inhibition of the converting activity of the purified FCVC with 3-amino-1,2,4-trizole. The converting activity (A) and catalase activity (B) of the purified FCVC with and without the inhibitor 3-amino-1,2,4-trizole 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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fig03: Inhibition of the converting activity of the purified FCVC with 3-amino-1,2,4-trizole. The converting activity (A) and catalase activity (B) of the purified FCVC with and without the inhibitor 3-amino-1,2,4-trizole 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: In the experiment shown in Figure3, we examined the effect of a catalase inhibitor, 3-amino-1,2,4-triazole, on the VBNC-converting activity of the purified FCVC. The presence of 3-amino-1,2,4-triazole significantly decreased the VBNC-converting activity (Fig.3A) as well as the H2O2-degrading activity of FCVC (Fig.3B) of the purified FCVC.


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)

Inhibition of the converting activity of the purified FCVC with 3-amino-1,2,4-trizole. The converting activity (A) and catalase activity (B) of the purified FCVC with and without the inhibitor 3-amino-1,2,4-trizole 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

fig03: Inhibition of the converting activity of the purified FCVC with 3-amino-1,2,4-trizole. The converting activity (A) and catalase activity (B) of the purified FCVC with and without the inhibitor 3-amino-1,2,4-trizole 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: In the experiment shown in Figure3, we examined the effect of a catalase inhibitor, 3-amino-1,2,4-triazole, on the VBNC-converting activity of the purified FCVC. The presence of 3-amino-1,2,4-triazole significantly decreased the VBNC-converting activity (Fig.3A) as well as the H2O2-degrading activity of FCVC (Fig.3B) of the purified FCVC.

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