SBTX, a new toxic protein distinct from soyatoxin and other toxic soybean [Glycine max] proteins, and its inhibitory effect on Cercospora sojina growth

Toxicon

Volumn 51, Issue 6, 2008, Pages 952-963

  Vasconcelos, I M ^a   Morais, J K S ^a   Siebra, E A ^a   Carlini, C R ^b   Sousa, D O B ^a   Beltramini, L M ^c   Melo, V M M ^a   Oliveira, J T A ^a  

^a FEDERAL UNIVERSITY OF CEARÁ   (Brazil)

^b FEDERAL UNIVERSITY OF RIO GRANDE DO SUL   (Brazil)

^c UNIVERSITY OF SÃO PAULO   (Brazil)

Author keywords

Antifungal protein; Glycine max; Plant toxin; Soybean; Toxicity

Indexed keywords

AGGLUTININ; CANATOXIN; PROTEIN SBTX; SOYATOXIN; TOXIN; TRYPSIN INHIBITOR;

ANTIFUNGAL ACTIVITY; ARTICLE; ASCOMYCETES; CERCOSPORA SOJINA; CONTROLLED STUDY; FAST PROTEIN LIQUID CHROMATOGRAPHY; FUNGUS GROWTH; LD 50; MOUSE; NONHUMAN; NUCLEOTIDE SEQUENCE; PHYSICAL CHEMISTRY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PURIFICATION; SOYBEAN;

AMINO ACID SEQUENCE; ANIMALS; ANTIFUNGAL AGENTS; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, LIQUID; ELECTROPHORESIS, POLYACRYLAMIDE GEL; GLYCOPROTEINS; HEMAGGLUTINATION; MICE; MITOSPORIC FUNGI; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PLANT PROTEINS; PROTEIN STRUCTURE, SECONDARY; SOYBEAN PROTEINS; SOYBEANS; SPECTRUM ANALYSIS; TOXINS, BIOLOGICAL;

CERCOSPORA SOJINA; FUNGI; GLYCINE MAX; MUS;

EID: 42649138877     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2007.10.005     Document Type: Article

References (42)

1. Altschul S.F., Gish W., Miller W., Myers E.W., and Lipman D.J. Basic local alignment search tool. J. Mol. Biol. 215 (1990) 403-410
2. Barja-Fidalgo C., Guimarães J.A., and Carlini C.R. Lipoxygenase-mediated secretory effect of canatoxin the toxic protein from Canavalia ensiformis seeds. Toxicon 29 (1991) 453-459
3. Blum H., Beier H., and Grossa H.J. Improved silver staining of plant proteins, RNA and DNA in polyacrylamide gels. Electrophoresis 8 (1987) 93-99
4. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of proteins utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
5. Broekaert W.F., Terras F.R.G., Cammue B.P., and Vanderleyden J. An automated quantitative assay for fungal growth inhibition. FEMS Microbiol. Lett. 69 (1990) 61-66
6. Burstein E.A., Vedenkina N.S., and Ivkova M.N. Fluorescence and location of tryptophan residues in protein molecules. Photochem. Photobiol. 18 (1973) 263-279
7. Carlini C.R., and Guimarães J.A. Isolation and characterization of a toxic protein from Canavalia ensiformis (jack bean) seeds, distinct from concanavalin A. Toxicon 54 (1981) 667-676
8. Carlini C.R., Barcellos G.B.S., Baeta-Neves A.D.V., and Guimarães J.A. Immunoreactivity for canatoxin and concanavalin A among proteins from leguminous seeds. Phytochemistry 27 (1988) 25-30
9. Chu K.T., Xia L., and Ng T.B. Pleurostrin, an antifungal peptide from the oyster mushroom. Peptides 26 (2006) 2098-2103
10. Dhaubhadel S., Kuflu K., Romero M.C., and Gijzen M. A soybean seed protein with carboxylate-binding activity. J. Exp. Bot. 56 (2005) 2335-2344
11. Dubois M., Gilles K.A., Hamilton J.K., Rebers P.A., and Smith F. Colorimetric method for determination of sugars and related substances. Anal. Chem. 28 (1956) 350-354
12. Eftink M.R. Fluorescence techniques for studying protein structure. In: Suelter C.H. (Ed). Methods of Biochemical Analysis: Protein Structure Determination vol. 35 (1991), Wiley, London 128-205
13. Follmer C., Barcellos G.B.S., Zingali R.B., Machado O.L.T., Alves E.W., Barja-Fidalgo T.C., Guimarães J.A., and Carlini C.R. Canatoxin, a toxic protein of jack beans (Canavalia ensiformis), is a variant form of urease (EC 3.5.1.5). Biological effects of urease independent of its ureolytic activity. Biochem. J. 360 (2001) 217-224
14. Goodwin T.W., and Morton R.A. The spectrophotometric determination of tyrosine and tryptophan in proteins. Biochem. J. 40 (1946) 628-632
15. Görg A., Obermaier O., Boguth G., Harder A., Scheibe B., Wildgruber R., and Weiss W. The current state of two-dimensional electrophoresis with immobilized pH gradients. Electrophoresis 21 (2000) 1037-1053
16. Gravina G.A., Sediyama C.S., Martins Filho S., Moreira M.A., Barros E.G., and Cruz C.D. Multivariate analysis of combining ability for soybean resistance to Cercospora sojina Hara. Genet. Mol. Biol. 27 (2004) 395-399
17. 1[W]. Plant Physiol. 137 (2005) 1397-1419
18. Hamerstrand G.E., Black L.T., and Glover J.D. Trypsin inhibitors in soy products: modification of standard analytical procedure. Cer. Chem. 58 (1981) 42-45
19. Harboe N., and Inglid A. Immunization, isolation of immunoglobulins, estimation of antibody titre. In: Axelsen N.H. (Ed). A Manual Quantitative Immunoelectrophoresis (1973), Blackwell Scientific Publications, London 161-164
20. Herman E.M., Helm R.M., Jung R., and Kinney A.J. Genetic modification removes an immunodominant allergen from soybean. Plant Physiol. 132 (2003) 36-43
21. Johnston J. Further topics in the k-variable linear model. In: Johnston J. (Ed). Economics Methods (1987), McGraw-Hill, Singapore 204-259
22. Kan Y.-C., Liu S.-W., Guo Z.-J., and Li D.-B. Characterization of a cyclophilin cDNA from soybean cells. Acta Bot. Sin. 44 (2002) 173-176
23. Kaplan A. The determination of urea, ammonia and urease. In: Glick D. (Ed). Methods of Biochemical Analysis (1969), Wiley, New York 311-314
24. Laemmli U.K. Cleavage of structural proteins during the assembly of bacteriophage T4. Nature 227 (1970) 685-689
25. Lee S.P., Hwang Y.S., Kim Y.J., Kwon K., Kim H.J., Kim K., and Chae H.Z. Cyclophilin A binds to peroxiredoxins and activates its peroxidase activity. J. Biol. Chem. 276 (2001) 29826-29832
26. Liener I.E. The intraperitoneal toxicity of concentrates of the soybean trypsin inhibitor. J. Biol. Chem. 193 (1951) 183-188
27. Liener I.E., and Pallansch M.J. Purification of a toxic substance from defatted soy bean flour. J. Biol. Chem. 197 (1952) 29-36
28. Melo V.M.M., Vasconcelos I.M., Gomes V.M., Da Cunha M., Soares A.A., and Oliveira J.T.A. A cotyledonary agglutinin from Luetzelburgia auriculata inhibits the fungal growth of Colletotrichum lindemuthianum, Fusarium solani and Aspergillus niger and impairs glucose-stimulated acidification of the incubation medium by Saccharomyces cerevisiae cells. Plant Sci. 169 (2005) 629-639
29. Mooney B.P., and Thelen J.J. High-throughput peptide mass fingerprinting of soybean seed proteins: automated workflow and utility of UniGene expressed sequence tag databases for protein identification. Phytochemistry 65 (2004) 1733-1744
30. Pallansch M.J., and Liener I.E. Soyin. II. Physical characterization. Biophysics 45 (1953) 366-374
31. Rabilloud T., and Chevallet M. Solubilization of proteins in 2-D electrophoresis. In: Rabilloud T. (Ed). Proteome Research: Two-Dimensional Gel Electrophoresis and Identification Methods (Principle and Practices) (2000), Springer, Germany 9-30
32. Reisfeld R.A., Lewis U.L., and Williams D.E. Disc electrophoresis of basic proteins and peptides on polyacrylamide gels. Nature 195 (1962) 281-284
33. Rios F.J.B., Cavada B.S., Medeiros D.A., Moreira R.A., Vasconcelos I.M., and Oliveira J.T.A. Digestibility of plant lectins from Canavalia, Cratylia, Dioclea and Artocarpus genera. In: Van Driessche E., Rougé P., Beeckmans S., and Bog-Hansen T.C. (Eds). Lectins: Biology, Biochemistry, Clinical Biochemistry Vol. 11 (1996), Textop, Denmark 277-284
34. Rowhani, A., Falk, B.W., 1995. Enzyme-linked immunosorbent assay (ELISA). In: Gamborg, O.L., Phillips, G.C., (Eds.), Methods to Certify Pathogen (Virus)-Free Plants. Plant Cell, Tissue and Organ Culture, pp. 266-280.
35. Sambeth W., Nesheim M.C., and Serafin J.A. Separation of soyabean whey into fractions with different biological activities for chicks and rats. J. Nutr. 92 (1967) 472-490
36. Schwab M.E., Suda K., and Thoenen H. Selective retrograde transsypnatic transfer of a protein, tetanus toxin, subsequent to its retrograde axonal transport. J. Cell Biol. 82 (1979) 798-810
37. Sreerama N., and Woody R.W. A self-consistent method for the analysis of protein secondary structure from circular-dichroism. Anal. Biochem. 209 (1993) 32-44
38. Van Parijs J., Joosen H.M., Peumans W.J., Geuns J.M., and Van Laere A.J. Effect of the Urtica dioica agglutinin on germination and cell wall formation of Phycomyces blakesleeanus Burgeff. Arch. Microbiol. 158 (1992) 19-25
39. Vasconcelos I.M., Trentin A., Guimarães J.A., and Carlini C.R. Purification and physicochemical characterization of soyatoxin, a novel toxic protein isolated from soybeans (Glycine max). Arch. Biochem. Biophys. 312 (1994) 357-366
40. Vasconcelos I.M., Siebra E.A., Maia A.A.B., Moreira R.A., Neto A.F., Campelo G.J.A., and Oliveira J.T.A. Composition, toxic and antinutritional factors of newly developed cultivars of Brazilian soybean (Glycine max). J. Sci. Food Agric. 75 (1997) 419-426
41. Vasconcelos I.M., Maia A.A.B., Siebra E.A., Oliveira J.T.A., Carvalho A.F.F.U., Melo V.M.M., Carlini C.R., and Castelar L.I.M. Nutritional study of two Brazilian soybean (Glycine max) cultivars differing in the contents of antinutritional and toxic proteins. J. Nutr. Biochem. 12 (2001) 1-8
42. Ye X.Y., and Ng T.B. Isolation of a new cyclophilin-like protein from chickpeas with mitogenic, antifungal and anti-HIV-1 reverse transcriptase activities. Life Sci. 70 (2002) 1129-1138