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Isolation of Rhp-PSP, a member of YER057c/YjgF/UK114 protein family with antiviral properties, from the photosynthetic bacterium Rhodopseudomonas palustris strain JSC-3b.

Su P, Feng T, Zhou X, Zhang S, Zhang Y, Cheng J, Luo Y, Peng J, Zhang Z, Lu X, Zhang D, Liu Y - Sci Rep (2015)

Bottom Line: Herein, this protein is designated Rhp-PSP.Rhp-PSP exhibited significant inhibitory activities against tobacco mosaic virus (TMV) in vivo and in vitro.To our knowledge, this represents the first report on the antiviral activity of a protein of the YER057c/YjgF/UK114 family and also the first antiviral protein isolated from R. palustris.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory for the Integrated Management of Pest and Disease on Horticultural Crops in Hunan Province, Hunan Plant Protection Institute, Hunan Academy of Agricultural Sciences, Changsha 410125, China.

ABSTRACT
Rhodopseudomonas palustris strain JSC-3b isolated from a water canal adjacent to a vegetable field produces a protein that was purified by bioactivity-guided fractionation based on ammonium sulfate precipitation, ion-exchange absorption and size exclusion. The protein was further identified as an endoribonuclease L-PSP (Liver-Perchloric acid-soluble protein) by shotgun mass spectrometry analysis and gene identification, and it is member of YER057c/YjgF/UK114 protein family. Herein, this protein is designated Rhp-PSP. Rhp-PSP exhibited significant inhibitory activities against tobacco mosaic virus (TMV) in vivo and in vitro. To our knowledge, this represents the first report on the antiviral activity of a protein of the YER057c/YjgF/UK114 family and also the first antiviral protein isolated from R. palustris. Our research provides insight into the potential of photosynthetic bacterial resources in biological control of plant virus diseases and sustainable agriculture.

No MeSH data available.


Related in: MedlinePlus

The inactivation effect of Rhp-PSP on TMV.The purified Rhp-PSP was diluted to concentrations of 50, 12.5 and 7.5 μgmL−1 to test the inactivation effects on TMV. BSA at a concentration of 50 μgmL−1 was used as the negative control. The right hand sides of the leaves were treated with a mixture of protein diluents and TMV, and the left hand sides were treated with buffer control. Photographs were taken three days after treatment.
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f2: The inactivation effect of Rhp-PSP on TMV.The purified Rhp-PSP was diluted to concentrations of 50, 12.5 and 7.5 μgmL−1 to test the inactivation effects on TMV. BSA at a concentration of 50 μgmL−1 was used as the negative control. The right hand sides of the leaves were treated with a mixture of protein diluents and TMV, and the left hand sides were treated with buffer control. Photographs were taken three days after treatment.

Mentions: The purified protein was diluted to concentrations of 500, 250, 125, and 75 μgmL−1 as described in the bioactivity-guided fractionation section to test its inactivation effect on TMV. The observations from the half-leaf method revealed that the Nicotiana glutinosa leaves inoculated with the protein-treated TMV exhibited no apparent lesions. To observe the concentration-dependent inactivation effects of the protein, the protein was subsequently diluted to lower concentrations of 50, 12.5, and 7.5 μgmL−1 that were then used in the inactivation effect test. The inactivation effect still achieved a level of 82% even though the concentration was lowered to 7.5 μgmL−1, according to the results (Fig. 2).


Isolation of Rhp-PSP, a member of YER057c/YjgF/UK114 protein family with antiviral properties, from the photosynthetic bacterium Rhodopseudomonas palustris strain JSC-3b.

Su P, Feng T, Zhou X, Zhang S, Zhang Y, Cheng J, Luo Y, Peng J, Zhang Z, Lu X, Zhang D, Liu Y - Sci Rep (2015)

The inactivation effect of Rhp-PSP on TMV.The purified Rhp-PSP was diluted to concentrations of 50, 12.5 and 7.5 μgmL−1 to test the inactivation effects on TMV. BSA at a concentration of 50 μgmL−1 was used as the negative control. The right hand sides of the leaves were treated with a mixture of protein diluents and TMV, and the left hand sides were treated with buffer control. Photographs were taken three days after treatment.
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4632080&req=5

f2: The inactivation effect of Rhp-PSP on TMV.The purified Rhp-PSP was diluted to concentrations of 50, 12.5 and 7.5 μgmL−1 to test the inactivation effects on TMV. BSA at a concentration of 50 μgmL−1 was used as the negative control. The right hand sides of the leaves were treated with a mixture of protein diluents and TMV, and the left hand sides were treated with buffer control. Photographs were taken three days after treatment.
Mentions: The purified protein was diluted to concentrations of 500, 250, 125, and 75 μgmL−1 as described in the bioactivity-guided fractionation section to test its inactivation effect on TMV. The observations from the half-leaf method revealed that the Nicotiana glutinosa leaves inoculated with the protein-treated TMV exhibited no apparent lesions. To observe the concentration-dependent inactivation effects of the protein, the protein was subsequently diluted to lower concentrations of 50, 12.5, and 7.5 μgmL−1 that were then used in the inactivation effect test. The inactivation effect still achieved a level of 82% even though the concentration was lowered to 7.5 μgmL−1, according to the results (Fig. 2).

Bottom Line: Herein, this protein is designated Rhp-PSP.Rhp-PSP exhibited significant inhibitory activities against tobacco mosaic virus (TMV) in vivo and in vitro.To our knowledge, this represents the first report on the antiviral activity of a protein of the YER057c/YjgF/UK114 family and also the first antiviral protein isolated from R. palustris.

View Article: PubMed Central - PubMed

Affiliation: Key Laboratory for the Integrated Management of Pest and Disease on Horticultural Crops in Hunan Province, Hunan Plant Protection Institute, Hunan Academy of Agricultural Sciences, Changsha 410125, China.

ABSTRACT
Rhodopseudomonas palustris strain JSC-3b isolated from a water canal adjacent to a vegetable field produces a protein that was purified by bioactivity-guided fractionation based on ammonium sulfate precipitation, ion-exchange absorption and size exclusion. The protein was further identified as an endoribonuclease L-PSP (Liver-Perchloric acid-soluble protein) by shotgun mass spectrometry analysis and gene identification, and it is member of YER057c/YjgF/UK114 protein family. Herein, this protein is designated Rhp-PSP. Rhp-PSP exhibited significant inhibitory activities against tobacco mosaic virus (TMV) in vivo and in vitro. To our knowledge, this represents the first report on the antiviral activity of a protein of the YER057c/YjgF/UK114 family and also the first antiviral protein isolated from R. palustris. Our research provides insight into the potential of photosynthetic bacterial resources in biological control of plant virus diseases and sustainable agriculture.

No MeSH data available.


Related in: MedlinePlus