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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

Multiple sequence alignment of the YER057c/YjgF/UK114 family.The last sequence shown in the picture is the deduced sequence of Rhp-PSP. The twelve invariant residues are highlighted in red, and the Arg129 of Rhp-PSP is indicated by the red triangle under the Rhp-PSP sequence. The sequences of the homologues and their crystal structures were obtained from UniProt and protein data bank RCSB PDB. This alignment and presentation was performed using ClustalX2 and ESPpript 3.0, and the secondary structure of Rhp-PSP was predicted in JPred 4.
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f5: Multiple sequence alignment of the YER057c/YjgF/UK114 family.The last sequence shown in the picture is the deduced sequence of Rhp-PSP. The twelve invariant residues are highlighted in red, and the Arg129 of Rhp-PSP is indicated by the red triangle under the Rhp-PSP sequence. The sequences of the homologues and their crystal structures were obtained from UniProt and protein data bank RCSB PDB. This alignment and presentation was performed using ClustalX2 and ESPpript 3.0, and the secondary structure of Rhp-PSP was predicted in JPred 4.

Mentions: In our present study, we initially isolated the putative endoribonuclease L-PSP from R. palustris and revealed its antiviral properties both in vivo and in vitro. However, due to the lack of direct evidence regarding the mechanism of the antiviral properties of this protein and the fact that most of its homologues are hypothetical proteins with unknown functions28, it seemed difficult to deduce the possible mechanism and support our results based on known resources related to this protein. However, its homologue RL-PSP has been reported to inhibit the protein translation of the tobacco mosaic virus mRNA in a rabbit reticulocyte lysate system, and it was subsequently proven the inhibition was driven by endoribonucleolytic activity, which cleaves the mRNA in a different manner than RNase A19. The multiple sequence alignment (Fig. 5) of the deduced sequence of Rhp-PSP with its homologues, i.e., PSPTO-PSP from P. syringe, YabJ from B. subtilis, TdcF from E. coli, Hp14.5 from humans, L-PSP from rats, UK114 from goats, and Hmf1 from S. serevisiae revealed that twelve residues of the YER057c/YjgF/UK114 family are invariantly conserved. Among these invariant residues, the conserved Arg103 of PSPTO-PSP and Arg107 of hp14.5 (which align with the Arg129 of Rhp-PSP) have been reported to be the crucial amino acids for different ligands and suitable binding sites for ribonucleotides32.


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)

Multiple sequence alignment of the YER057c/YjgF/UK114 family.The last sequence shown in the picture is the deduced sequence of Rhp-PSP. The twelve invariant residues are highlighted in red, and the Arg129 of Rhp-PSP is indicated by the red triangle under the Rhp-PSP sequence. The sequences of the homologues and their crystal structures were obtained from UniProt and protein data bank RCSB PDB. This alignment and presentation was performed using ClustalX2 and ESPpript 3.0, and the secondary structure of Rhp-PSP was predicted in JPred 4.
© Copyright Policy - open-access
Related In: Results  -  Collection

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

f5: Multiple sequence alignment of the YER057c/YjgF/UK114 family.The last sequence shown in the picture is the deduced sequence of Rhp-PSP. The twelve invariant residues are highlighted in red, and the Arg129 of Rhp-PSP is indicated by the red triangle under the Rhp-PSP sequence. The sequences of the homologues and their crystal structures were obtained from UniProt and protein data bank RCSB PDB. This alignment and presentation was performed using ClustalX2 and ESPpript 3.0, and the secondary structure of Rhp-PSP was predicted in JPred 4.
Mentions: In our present study, we initially isolated the putative endoribonuclease L-PSP from R. palustris and revealed its antiviral properties both in vivo and in vitro. However, due to the lack of direct evidence regarding the mechanism of the antiviral properties of this protein and the fact that most of its homologues are hypothetical proteins with unknown functions28, it seemed difficult to deduce the possible mechanism and support our results based on known resources related to this protein. However, its homologue RL-PSP has been reported to inhibit the protein translation of the tobacco mosaic virus mRNA in a rabbit reticulocyte lysate system, and it was subsequently proven the inhibition was driven by endoribonucleolytic activity, which cleaves the mRNA in a different manner than RNase A19. The multiple sequence alignment (Fig. 5) of the deduced sequence of Rhp-PSP with its homologues, i.e., PSPTO-PSP from P. syringe, YabJ from B. subtilis, TdcF from E. coli, Hp14.5 from humans, L-PSP from rats, UK114 from goats, and Hmf1 from S. serevisiae revealed that twelve residues of the YER057c/YjgF/UK114 family are invariantly conserved. Among these invariant residues, the conserved Arg103 of PSPTO-PSP and Arg107 of hp14.5 (which align with the Arg129 of Rhp-PSP) have been reported to be the crucial amino acids for different ligands and suitable binding sites for ribonucleotides32.

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