Purification of a Ribosome-inactivating Protein with Antioxidation and Root Developer Potencies from

Overview

Journal Physiol Mol Biol Plants

Specialty Biology

Date 2019 Feb 27

PMID 30804646

Citations 1

Authors

Ashraf Gholizadeh

Affiliations

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Abstract

Considering as a potent antiviral plant, the attempt was made to determine, purify and characterize its proteinaceous antiviral elements against tobacco mosaic virus hypersensitive response on . By using 60% ammonium sulphate-precipitation, FPLC-based anion and cation-exchange chromatography in 10 and 50 mM NaCl, size-exclusion chromatography in 50 mM NaCl and SDS-PAGE 10%, a 25 kD antiviral protein with ribosome-inactivating/28S rRNase ability was purified from the leaves of . at vegetative growth stage. The purified protein showed FRAP-based antioxidant activity in vitro and caused 1.7-fold and 1.4-fold increases in the growth rate of root system upon carborundum-based application on the root growth medium of . . The present work reports an antiviral protein with ribosome-inactivating, antioxidation and root developer potencies in as an edible or ornamental plant that may be useful in health and agricultural biotechnology in the future.

Citing Articles

Antiviral Activity of Ribosome-Inactivating Proteins.

Citores L, Iglesias R, Ferreras J Toxins (Basel). 2021; 13(2).

PMID: 33499086 PMC: 7912582. DOI: 10.3390/toxins13020080.

References

Hong Y, Saunders K, Hartley M, Stanley J . Resistance to geminivirus infection by virus-induced expression of dianthin in transgenic plants. Virology. 1996; 220(1):119-27. DOI: 10.1006/viro.1996.0292. View

Stoscheck C . Quantitation of protein. Methods Enzymol. 1990; 182:50-68. DOI: 10.1016/0076-6879(90)82008-p. View

Shu S, Xie G, Guo X, Wang M . Purification and characterization of a novel ribosome-inactivating protein from seeds of Trichosanthes kirilowii Maxim. Protein Expr Purif. 2009; 67(2):120-5. DOI: 10.1016/j.pep.2009.03.004. View

Balasubrahmanyam , Baranwal , Lodha , Varma , Kapoor . Purification and properties of growth stage-dependent antiviral proteins from the leaves of Celosia cristata. Plant Sci. 2000; 154(1):13-21. DOI: 10.1016/s0168-9452(99)00192-2. View

Yeung H, Li W, Feng Z, Barbieri L, Stirpe F . Trichosanthin, alpha-momorcharin and beta-momorcharin: identity of abortifacient and ribosome-inactivating proteins. Int J Pept Protein Res. 1988; 31(3):265-8. DOI: 10.1111/j.1399-3011.1988.tb00033.x. View

Knight B . Ricin--a potent homicidal poison. Br Med J. 1979; 1(6159):350-1. PMC: 1597717. View

Gholizadeh A, Kohnehrouz B, Santha I, Lodha M, Kapoor H . Cloning and expression of small cDNA fragment encoding strong antiviral peptide from Celosia cristata in Escherichia coli. Biochemistry (Mosc). 2005; 70(9):1005-10. DOI: 10.1007/s10541-005-0216-y. View

Stirpe F, Williams D, Onyon L, Legg R, Stevens W . Dianthins, ribosome-damaging proteins with anti-viral properties from Dianthus caryophyllus L. (carnation). Biochem J. 1981; 195(2):399-405. PMC: 1162903. DOI: 10.1042/bj1950399. View

Iglesias R, Perez Y, de Torre C, Ferreras J, Antolin P, Jimenez P . Molecular characterization and systemic induction of single-chain ribosome-inactivating proteins (RIPs) in sugar beet (Beta vulgaris) leaves. J Exp Bot. 2005; 56(416):1675-84. DOI: 10.1093/jxb/eri164. View

10.

Stirpe F, Battelli M . Ribosome-inactivating proteins: progress and problems. Cell Mol Life Sci. 2006; 63(16):1850-66. PMC: 11136412. DOI: 10.1007/s00018-006-6078-7. View

11.

Girbes T, Ferreras J, Javier Arias F, Stirpe F . Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi and bacteria. Mini Rev Med Chem. 2004; 4(5):461-76. DOI: 10.2174/1389557043403891. View

12.

Laemmli U . Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 1970; 227(5259):680-5. DOI: 10.1038/227680a0. View

13.

Peumans W, Hao Q, Van Damme E . Ribosome-inactivating proteins from plants: more than RNA N-glycosidases?. FASEB J. 2001; 15(9):1493-506. DOI: 10.1096/fj.00-0751rev. View

14.

Benzie I, Strain J . The ferric reducing ability of plasma (FRAP) as a measure of "antioxidant power": the FRAP assay. Anal Biochem. 1996; 239(1):70-6. DOI: 10.1006/abio.1996.0292. View

15.

Battelli M, Polito L, Bolognesi A, Lafleur L, Fradet Y, Stirpe F . Toxicity of ribosome-inactivating proteins-containing immunotoxins to a human bladder carcinoma cell line. Int J Cancer. 1996; 65(4):485-90. DOI: 10.1002/(SICI)1097-0215(19960208)65:4<485::AID-IJC16>3.0.CO;2-9. View

16.

Kennedy M, Cortes F, Pinero J, Castanys S, Lopez-Arencibia A, Gamarro F . Leishmanicidal and reversal multidrug resistance constituents from Aeonium lindleyi. Planta Med. 2010; 77(1):77-80. DOI: 10.1055/s-0030-1250144. View

17.

Puri M, Kaur I, Kanwar R, Gupta R, Chauhan A, Kanwar J . Ribosome inactivating proteins (RIPs) from Momordica charantia for anti viral therapy. Curr Mol Med. 2009; 9(9):1080-94. DOI: 10.2174/156652409789839071. View

18.

He Y, Guo C, Pan Y, Peng C, Weng Z . Inhibition of hepatitis B virus replication by pokeweed antiviral protein in vitro. World J Gastroenterol. 2008; 14(10):1592-7. PMC: 2693758. DOI: 10.3748/wjg.14.1592. View

19.

Uckun F, Rajamohan F, Pendergrass S, Ozer Z, Waurzyniak B, Mao C . Structure-based design and engineering of a nontoxic recombinant pokeweed antiviral protein with potent anti-human immunodeficiency virus activity. Antimicrob Agents Chemother. 2003; 47(3):1052-61. PMC: 149289. DOI: 10.1128/AAC.47.3.1052-1061.2003. View

20.

Parikh B, Tumer N . Antiviral activity of ribosome inactivating proteins in medicine. Mini Rev Med Chem. 2004; 4(5):523-43. DOI: 10.2174/1389557043403800. View