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

Yıl 2012, Cilt: 2 Sayı: 4, 52 - 58, 23.07.2016

Öz

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

Kaynakça

  • Ahn, S.C., Back, B.S., Oh, T., Song, C.S., and Chatterjee, B. (2000). Biotechniques, 29, 466-468.
  • Barbieri, L., Battelli, M.G., Stirpe, F., (1993). Ribosome inactivating proteins from plants. Biochemica and Biophysica Acta 1154, 237-282.
  • Barbieri, L., Valbonesi, P., Righi, F., Zuuccheri, G., Monti, F., Gorini, P., Samori, B., and Stirpe, F., (2000). Polynucleotide: Adenosine glycosidase is the sole activity of ribosome-inactivating proteins on DNA. J. Biochem. 128(5):883-9.
  • Barbieri,L., Valbonesi,P., Govoni,M., Pession, A., and Stirpe,F. (2000). Polynucleotide: adenosine glycosidase activity of saporine L1: effect on various forms of mammalian DNA. Biochem. Biophys. Acta 1480, 258-266.
  • Choudhary, NL., Yadav, OP., and Lodha, ML., (2008). Ribonuclease, deoxyribonuclease, and antiviral activity of Escherichia coli- expressed Bougainvillea xbuttiana antiviral protein 1. Biochemistry (Mosc), 73(3):273-7.
  • Corrado, G., Bovi, P., and Ciliento, R., (2005). Inducible Expression of a Phytolacca heterotepala Ribosome-Inactivating Protein Leads to Enhanced Resistance Against Major Fungal Pathogens in Tobacco. Phytopathology, Feb;95(2):206- 15.
  • Desmyter, S.(2002). Study of the antiviral activity of Iris RIP, a type 1 ribosome inactivating protein from Iris hallandica. PhD thesis, Katholieke Universiteit Leuven, Belgium.
  • Gholizadeh, A., Kumar, M., Balasubrahmanyam, A., Kumar, S., Narewal, s., Lodha, M.L., and Kapoor, H.C., (2004). Antioxidant activity of antiviral proteins from Celosia cristata. J. plant Biochem. Biotechnol. 13, 13-18.
  • Girbes, T., Ferreras, J.M., Arias, F.J., and Stripe, F.(2004). Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi, and bacteria. Mini Rev. Med Chem., 4, 461-476.
  • Gu, Y., Chen, W., Xia, Z.(2000) . Molecular modeling of the interactions of trichosanthin with four substrate analogs. J.Protein Chem. 19(4) :291-7.
  • Hao, Q., VanDamme, E.J.M., Hause, B., Barre, A., Chen, Y., Rouge, P. and Peumans, w.J. (2001). Iris bulbs express type 1 and type 2 ribosome-inactivating proteins with unusual properties plant physiol. 125, 866-876.
  • Hudak, K.A., Bauman, J.D., and Tumer, N.E., (2002). Pokeweed antiviral protein binds to the cap structure of eukaryotic mRNA and depurinates the mRNA downstream of the cap. RNA 8, 1148-1159.
  • Hudak, K.A., Wang, P., and Tumer, N.E., (2000). A novel mechanism for inhibition of translation by pokeweed antiviral protein; depurination of the capped RNA template. RNA 6, 369-380.
  • Iglesias, R., Perez, Y., Torre, C., Ferreras, JM., Antolin, P., Jimenez, P., Rojo, MA., Mendez, E., and Gribes, T., (2005). Molecular characterization and systemic induction of single-chain ribosome-inactivating proteins (RIPs) in sugar beet (Beta vulgaris) leaves. J.Exp.Bot. 56(416):1675-84.
  • Kataoka,J., Habuka,N., Miyano,M., Masuta,C., and Koiwai,A. (1992). Adenine depurination and inactivation of plant ribosomes by an antiviral protein of Mirabilis jalapa, Plant Molecular Biology, 20; 1111-1119.
  • Kim, J.K., Jang, I, C., Wu, R., Zuo, W.N., Boston, R.S., Lee, Y.H., Ahn, IP., and Nahm, B.H., (2003). Co-expression of a modified maize ribosome-inactivating protein and a rice basic chitinase gene in transgenic rice plants confers enhanced resistance to sheath blight. Transgenic Research 12, 475-484.
  • Kurinov, IV., Myers, DE., Irvin, JD., and Uckun, FM. (1999). X-ray crystallographic analysis of the structural basis for the interactions of pokeweed antiviral protein with its active site inhibitor and ribosomal Rna substrate analogs. Protein Sci, 8(9):1765-72.
  • Laemmli, U.K. (1970). Nature (London) 227,680-685. Lau, CK., Wong, RN., Lo, SC., Kwok, F. (1998). Refolding of denatured trichosanthin in the presence of GroEL. Biochem Biophys Res Commun, 245(1):149-45.
  • Lowry,O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951). Biol. Chem. 193, 223-234.
  • Moon, YH., Song, SK., Choi, KW., and Lee, JS., (1997). Expression of a cDNA encoding Phytolacca insularis antiviral protein confers virus resistance on transgenic potato plants. Mol Cells, 7(6):807-15
  • Nielsen, K. and Boston, R.S., (2001). Ribosome-inactivating proteins : a plant perspective. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 785-816.
  • Park, Vepachedu, R., Sharma, N., and Vivanco, J.M. (2004). Ribosome-inactivating proteins in plant biolog. Planta 219, 1903- 1906.
  • Peumans, W.J., Hao, Q. and Van Damme, E.J.M.(2001). Ribosome-inactivating protein from plants: more than RNA Nglycosidases? FASEB J. 15, 1493-1506.
  • Sawasaki, T., Nishihara, M., and Endo, Y. (2008). RIP and RALyase cleave the sarcin/ricin domain, a critical domain for ribosome function, during senescence of wheat coleoptiles. Biochem Biophys Res Commun, 370(4):561-5.
  • Sikriwal, D., Ghosh, P., and Batra, JK., (2008). Ribosome inactivating protein saporin induces apoptosis through mitochondrial cascade, independent of translation inhibition. Int J Biochem Cell Biol, 40(12):2880-8
  • Sribash, R., Sadhana, P., and Begum, M., (2006. )Purification, characterization and cloning of antiviral/ribosome inactivating protein from Amaranthus tricolor leaves
  • Stirpe, F., Gasperi,Campani, A., Barbieri, L., Falasca, A. I., Abbondanza, A., and Stevens, W.A. (1983). Ribosomeinactivating proteins from the seeds of Saponaria officinalis L. (soapwort), Agrostemma githago L. (corn cockle), Asparagus officinalis L. (asparagus) and from the latex of Hura crepitans L. (sandbox tree). Biochem. J., 216, 617.
  • Stirpe,F., Barbieri,I., Batelli,M.G., Soria,M., and Lappi,D.A. (1992). Ribosome inactivating proteins from plants: present status and future prospects, BioTechnology. 10:405-412.
  • Taylor,B.E., and Irvin,J.D. (1990). Depurination of plant ribosomes by pokeweed antiviral proteins. FEBS lett,273:144-146.
  • Taylor,S., Massiah,A., Lomonossof,G., Roberts,L.M., Lord,J.M., and Hartley,M. (1994). Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco mosaic virus infection.Plant J.5(6):827-835.
  • Tumer, N.E., Hwang, D.J., and Bonness, M., (1997). C-terminal deletion mutant of Pokeweed antiviral protein inhibits viral infection but does not depurinate host ribosomes. Proc. Natl. Acad. Sci. USA, 94, 3866-3871.
  • Van Damme, E.J.M., Hao, Q., Chen, Y., Barre, A., Vandenbussche, F., Desmyter, S., Rouge, P. and Peumans, W.J. (2001). Ribosome-inactivating proteins: a family of plant proteins do more than inactivate ribosomes. Crit. Rev. plant Sci. 20, 395-465.
  • Vandenbussche, F., Desmyter, s., Ciani, M., Proost, P., Peumans, W.J., and Van Damme, E.J.M., (2004). Analysis of the in planta antiviral activity of elderberry ribosome-inactivating proteins. Eur.J.Biochem.271, 1508-1515.
  • Vepachedu, R., Park, SW., Sharma, N., and Vivanco, JM., (2005). Bacterial expression and enzymatic activity analysis of ME1, a ribosome-inactivating protein from Mirabilis expansa. Protein Expr Purif, Mar; 40(1):142-51
  • Verma, H.N., Srivastava, S., Kumar, V., Kumar, D., (1996). Induction of systemic resistance in plants against viruses by a basic protein from Clerodendrum aculeatum leaves. Biochem. Cell Biol.86,485-491.
  • Watanabe,K., Kawasaki,T., Sako,N., and Funatsu,G. (1997). Actions of pokeweed antiviral protein on virus-infected protoplasts. Bioscience,-Biotechnology-and-Biochemistry, 61: 6, 994-997.
  • Zoubenko, O., Hudak, K. and Tumer, N.E., (2000). A non-toxic pokeweed antiviral protein mutant inhibits pathogen infection via a novel salicylic acid-independent pathway. Plant Mol.Biol.44, 219-229.
Yıl 2012, Cilt: 2 Sayı: 4, 52 - 58, 23.07.2016

Öz

Kaynakça

  • Ahn, S.C., Back, B.S., Oh, T., Song, C.S., and Chatterjee, B. (2000). Biotechniques, 29, 466-468.
  • Barbieri, L., Battelli, M.G., Stirpe, F., (1993). Ribosome inactivating proteins from plants. Biochemica and Biophysica Acta 1154, 237-282.
  • Barbieri, L., Valbonesi, P., Righi, F., Zuuccheri, G., Monti, F., Gorini, P., Samori, B., and Stirpe, F., (2000). Polynucleotide: Adenosine glycosidase is the sole activity of ribosome-inactivating proteins on DNA. J. Biochem. 128(5):883-9.
  • Barbieri,L., Valbonesi,P., Govoni,M., Pession, A., and Stirpe,F. (2000). Polynucleotide: adenosine glycosidase activity of saporine L1: effect on various forms of mammalian DNA. Biochem. Biophys. Acta 1480, 258-266.
  • Choudhary, NL., Yadav, OP., and Lodha, ML., (2008). Ribonuclease, deoxyribonuclease, and antiviral activity of Escherichia coli- expressed Bougainvillea xbuttiana antiviral protein 1. Biochemistry (Mosc), 73(3):273-7.
  • Corrado, G., Bovi, P., and Ciliento, R., (2005). Inducible Expression of a Phytolacca heterotepala Ribosome-Inactivating Protein Leads to Enhanced Resistance Against Major Fungal Pathogens in Tobacco. Phytopathology, Feb;95(2):206- 15.
  • Desmyter, S.(2002). Study of the antiviral activity of Iris RIP, a type 1 ribosome inactivating protein from Iris hallandica. PhD thesis, Katholieke Universiteit Leuven, Belgium.
  • Gholizadeh, A., Kumar, M., Balasubrahmanyam, A., Kumar, S., Narewal, s., Lodha, M.L., and Kapoor, H.C., (2004). Antioxidant activity of antiviral proteins from Celosia cristata. J. plant Biochem. Biotechnol. 13, 13-18.
  • Girbes, T., Ferreras, J.M., Arias, F.J., and Stripe, F.(2004). Description, distribution, activity and phylogenetic relationship of ribosome-inactivating proteins in plants, fungi, and bacteria. Mini Rev. Med Chem., 4, 461-476.
  • Gu, Y., Chen, W., Xia, Z.(2000) . Molecular modeling of the interactions of trichosanthin with four substrate analogs. J.Protein Chem. 19(4) :291-7.
  • Hao, Q., VanDamme, E.J.M., Hause, B., Barre, A., Chen, Y., Rouge, P. and Peumans, w.J. (2001). Iris bulbs express type 1 and type 2 ribosome-inactivating proteins with unusual properties plant physiol. 125, 866-876.
  • Hudak, K.A., Bauman, J.D., and Tumer, N.E., (2002). Pokeweed antiviral protein binds to the cap structure of eukaryotic mRNA and depurinates the mRNA downstream of the cap. RNA 8, 1148-1159.
  • Hudak, K.A., Wang, P., and Tumer, N.E., (2000). A novel mechanism for inhibition of translation by pokeweed antiviral protein; depurination of the capped RNA template. RNA 6, 369-380.
  • Iglesias, R., Perez, Y., Torre, C., Ferreras, JM., Antolin, P., Jimenez, P., Rojo, MA., Mendez, E., and Gribes, T., (2005). Molecular characterization and systemic induction of single-chain ribosome-inactivating proteins (RIPs) in sugar beet (Beta vulgaris) leaves. J.Exp.Bot. 56(416):1675-84.
  • Kataoka,J., Habuka,N., Miyano,M., Masuta,C., and Koiwai,A. (1992). Adenine depurination and inactivation of plant ribosomes by an antiviral protein of Mirabilis jalapa, Plant Molecular Biology, 20; 1111-1119.
  • Kim, J.K., Jang, I, C., Wu, R., Zuo, W.N., Boston, R.S., Lee, Y.H., Ahn, IP., and Nahm, B.H., (2003). Co-expression of a modified maize ribosome-inactivating protein and a rice basic chitinase gene in transgenic rice plants confers enhanced resistance to sheath blight. Transgenic Research 12, 475-484.
  • Kurinov, IV., Myers, DE., Irvin, JD., and Uckun, FM. (1999). X-ray crystallographic analysis of the structural basis for the interactions of pokeweed antiviral protein with its active site inhibitor and ribosomal Rna substrate analogs. Protein Sci, 8(9):1765-72.
  • Laemmli, U.K. (1970). Nature (London) 227,680-685. Lau, CK., Wong, RN., Lo, SC., Kwok, F. (1998). Refolding of denatured trichosanthin in the presence of GroEL. Biochem Biophys Res Commun, 245(1):149-45.
  • Lowry,O.H., Rosebrough, N.J., Farr, A.L., and Randall, R.J. (1951). Biol. Chem. 193, 223-234.
  • Moon, YH., Song, SK., Choi, KW., and Lee, JS., (1997). Expression of a cDNA encoding Phytolacca insularis antiviral protein confers virus resistance on transgenic potato plants. Mol Cells, 7(6):807-15
  • Nielsen, K. and Boston, R.S., (2001). Ribosome-inactivating proteins : a plant perspective. Annu. Rev. Plant Physiol. Plant Mol. Biol. 52, 785-816.
  • Park, Vepachedu, R., Sharma, N., and Vivanco, J.M. (2004). Ribosome-inactivating proteins in plant biolog. Planta 219, 1903- 1906.
  • Peumans, W.J., Hao, Q. and Van Damme, E.J.M.(2001). Ribosome-inactivating protein from plants: more than RNA Nglycosidases? FASEB J. 15, 1493-1506.
  • Sawasaki, T., Nishihara, M., and Endo, Y. (2008). RIP and RALyase cleave the sarcin/ricin domain, a critical domain for ribosome function, during senescence of wheat coleoptiles. Biochem Biophys Res Commun, 370(4):561-5.
  • Sikriwal, D., Ghosh, P., and Batra, JK., (2008). Ribosome inactivating protein saporin induces apoptosis through mitochondrial cascade, independent of translation inhibition. Int J Biochem Cell Biol, 40(12):2880-8
  • Sribash, R., Sadhana, P., and Begum, M., (2006. )Purification, characterization and cloning of antiviral/ribosome inactivating protein from Amaranthus tricolor leaves
  • Stirpe, F., Gasperi,Campani, A., Barbieri, L., Falasca, A. I., Abbondanza, A., and Stevens, W.A. (1983). Ribosomeinactivating proteins from the seeds of Saponaria officinalis L. (soapwort), Agrostemma githago L. (corn cockle), Asparagus officinalis L. (asparagus) and from the latex of Hura crepitans L. (sandbox tree). Biochem. J., 216, 617.
  • Stirpe,F., Barbieri,I., Batelli,M.G., Soria,M., and Lappi,D.A. (1992). Ribosome inactivating proteins from plants: present status and future prospects, BioTechnology. 10:405-412.
  • Taylor,B.E., and Irvin,J.D. (1990). Depurination of plant ribosomes by pokeweed antiviral proteins. FEBS lett,273:144-146.
  • Taylor,S., Massiah,A., Lomonossof,G., Roberts,L.M., Lord,J.M., and Hartley,M. (1994). Correlation between the activities of five ribosome-inactivating proteins in depurination of tobacco mosaic virus infection.Plant J.5(6):827-835.
  • Tumer, N.E., Hwang, D.J., and Bonness, M., (1997). C-terminal deletion mutant of Pokeweed antiviral protein inhibits viral infection but does not depurinate host ribosomes. Proc. Natl. Acad. Sci. USA, 94, 3866-3871.
  • Van Damme, E.J.M., Hao, Q., Chen, Y., Barre, A., Vandenbussche, F., Desmyter, S., Rouge, P. and Peumans, W.J. (2001). Ribosome-inactivating proteins: a family of plant proteins do more than inactivate ribosomes. Crit. Rev. plant Sci. 20, 395-465.
  • Vandenbussche, F., Desmyter, s., Ciani, M., Proost, P., Peumans, W.J., and Van Damme, E.J.M., (2004). Analysis of the in planta antiviral activity of elderberry ribosome-inactivating proteins. Eur.J.Biochem.271, 1508-1515.
  • Vepachedu, R., Park, SW., Sharma, N., and Vivanco, JM., (2005). Bacterial expression and enzymatic activity analysis of ME1, a ribosome-inactivating protein from Mirabilis expansa. Protein Expr Purif, Mar; 40(1):142-51
  • Verma, H.N., Srivastava, S., Kumar, V., Kumar, D., (1996). Induction of systemic resistance in plants against viruses by a basic protein from Clerodendrum aculeatum leaves. Biochem. Cell Biol.86,485-491.
  • Watanabe,K., Kawasaki,T., Sako,N., and Funatsu,G. (1997). Actions of pokeweed antiviral protein on virus-infected protoplasts. Bioscience,-Biotechnology-and-Biochemistry, 61: 6, 994-997.
  • Zoubenko, O., Hudak, K. and Tumer, N.E., (2000). A non-toxic pokeweed antiviral protein mutant inhibits pathogen infection via a novel salicylic acid-independent pathway. Plant Mol.Biol.44, 219-229.
Toplam 37 adet kaynakça vardır.

Ayrıntılar

Diğer ID JA56PY53ZE
Bölüm Makaleler
Yazarlar

Zenab Aly Torky Bu kişi benim

Yayımlanma Tarihi 23 Temmuz 2016
Yayımlandığı Sayı Yıl 2012 Cilt: 2 Sayı: 4

Kaynak Göster

APA Torky, Z. A. (2016). Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity. TOJSAT, 2(4), 52-58.
AMA Torky ZA. Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity. TOJSAT. Temmuz 2016;2(4):52-58.
Chicago Torky, Zenab Aly. “Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity”. TOJSAT 2, sy. 4 (Temmuz 2016): 52-58.
EndNote Torky ZA (01 Temmuz 2016) Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity. TOJSAT 2 4 52–58.
IEEE Z. A. Torky, “Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity”, TOJSAT, c. 2, sy. 4, ss. 52–58, 2016.
ISNAD Torky, Zenab Aly. “Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity”. TOJSAT 2/4 (Temmuz 2016), 52-58.
JAMA Torky ZA. Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity. TOJSAT. 2016;2:52–58.
MLA Torky, Zenab Aly. “Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity”. TOJSAT, c. 2, sy. 4, 2016, ss. 52-58.
Vancouver Torky ZA. Isolation and Characterization of Antiviral Protein From Salsola Longifolia Leaves Expressing Polynucleotide Adenosine Glycoside Activity. TOJSAT. 2016;2(4):52-8.