Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity

Abstract

Disease control of economically important crops using non-costly and environmentally nonharmful methods is a necessity. Due to their wide antimicrobial activities in general and their antiviral activities in particular, ribosome-inactivating proteins (RIPs) have a very strong potential in plant defense. A new type -1 single chain RIP named SLP was purified from the leaves of Salsola longifolia by ammonium sulphate fractionation, anion exchange on DE-cellulose chromatography and cation exchange chromatography on CM-cellulose. This new RIP’s molecular mass was 32 KDa with homology to singlechain ribosome inactivating protein. Reverse transcribtase polymerase chain reaction detected the ribonuclease activity of SLP from the examined species showing SLP to be a broad spectrum RIP that depurinates not only its own ribosomes but also other heterologus plant ribosomes (Phaseolus vulgaris). SLP also showed deoxyribonuclease activity against pBlue Script SK+ plasmid DNA at moderate SLP concentration which led to nick super coiled DNA and then to nicked circular form. By increasing RIP concentration, it transformed the nicked DNA into a linear form. SLP also showed to possess a powerful antiviral activity

Keywords

• Isolation, Antiviral protection, Salsola longifolla leave

References

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