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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 liquid chromatography (LC)-MS/MS analysis and the deduced sequence of Rhp-PSP.(a,b) Two peptides, AALGDLDKVVR and LGGFINSAPDFIDGPK, were identified with 95% confidence. (c) The nucleotide sequence of the PCR products of Rhp-PSP was identical to the sequence from the genome of R. palustris JSC-3b. The stop codon TGA is shown as an asterisk in the deduced amino acid sequence.
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f3: The liquid chromatography (LC)-MS/MS analysis and the deduced sequence of Rhp-PSP.(a,b) Two peptides, AALGDLDKVVR and LGGFINSAPDFIDGPK, were identified with 95% confidence. (c) The nucleotide sequence of the PCR products of Rhp-PSP was identical to the sequence from the genome of R. palustris JSC-3b. The stop codon TGA is shown as an asterisk in the deduced amino acid sequence.

Mentions: The protein sample was excised from the Tricine SDS-PAGE gel for liquid chromatography (LC)-MS/MS analysis of the in-gel-digested protein to determine the amino acid sequence of Rhp-PSP. The MS/MS data were analysed as described in the shotgun mass spectrometry analysis section of the materials and methods. Based on the ProteinPilot results, we obtained the best-matching protein, which was endoribonuclease L-PSP (UniProt No. Q07L61), from the R. palustris strain BisA53. The peptides coverage of the match was 76% with 39 different reliable peptides. Here, we present two of those peptides, i.e., AALGDLDKVVR (Fig. 3a) and LGGFINSAPDFIDGPK (Fig. 3b). Using the genomic sequence of JSC-3b, we found the endoribonuclease L-PSP gene, which had a full-length of 459 bp and encoded a protein of 152 amino acids (Fig. 3c). The gene was then cloned from the JSC-3b strain genomic DNA and verified by sequencing. The results revealed an 85.26% similarity with the gene from strain BisA53 based on alignment (DNAMAN, Version 8.0). Therefore we designated new protein isolated from R. palustris strain JSC-3b as Rhp-PSP.


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 liquid chromatography (LC)-MS/MS analysis and the deduced sequence of Rhp-PSP.(a,b) Two peptides, AALGDLDKVVR and LGGFINSAPDFIDGPK, were identified with 95% confidence. (c) The nucleotide sequence of the PCR products of Rhp-PSP was identical to the sequence from the genome of R. palustris JSC-3b. The stop codon TGA is shown as an asterisk in the deduced amino acid sequence.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f3: The liquid chromatography (LC)-MS/MS analysis and the deduced sequence of Rhp-PSP.(a,b) Two peptides, AALGDLDKVVR and LGGFINSAPDFIDGPK, were identified with 95% confidence. (c) The nucleotide sequence of the PCR products of Rhp-PSP was identical to the sequence from the genome of R. palustris JSC-3b. The stop codon TGA is shown as an asterisk in the deduced amino acid sequence.
Mentions: The protein sample was excised from the Tricine SDS-PAGE gel for liquid chromatography (LC)-MS/MS analysis of the in-gel-digested protein to determine the amino acid sequence of Rhp-PSP. The MS/MS data were analysed as described in the shotgun mass spectrometry analysis section of the materials and methods. Based on the ProteinPilot results, we obtained the best-matching protein, which was endoribonuclease L-PSP (UniProt No. Q07L61), from the R. palustris strain BisA53. The peptides coverage of the match was 76% with 39 different reliable peptides. Here, we present two of those peptides, i.e., AALGDLDKVVR (Fig. 3a) and LGGFINSAPDFIDGPK (Fig. 3b). Using the genomic sequence of JSC-3b, we found the endoribonuclease L-PSP gene, which had a full-length of 459 bp and encoded a protein of 152 amino acids (Fig. 3c). The gene was then cloned from the JSC-3b strain genomic DNA and verified by sequencing. The results revealed an 85.26% similarity with the gene from strain BisA53 based on alignment (DNAMAN, Version 8.0). Therefore we designated new protein isolated from R. palustris strain JSC-3b as Rhp-PSP.

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