Induction of β-1,3-glucanase and chitinase in Vigna aconitifolia inoculated with Macrophomina phaseolina

References

• Abeles FB, Bosshart RP, Forrence LE, Habig WE. 1970. Preparation and purification of glucanase and chitinase from bean leaves. Plant Physiol. 47:129–134. doi:10.1104/pp.47.1.129
   Web of Science ®Google Scholar
• Anguelova-Merhar VS, Van der Westhuizen AJ, Pretorias ZA. 2001. β-1,3-Glucanase and chitinase activities and the resistance response of wheat to leaf rust. J Phytopathol. 149:381–384. doi:10.1046/j.1439-0434.2001.00638.x
   Web of Science ®Google Scholar
• Antoniw JF, Ritter CE, Pierpoint WS, Van Loon LC. 1980. Comparison of three pathogenesis-related proteins from plants of two cultivars of tobacco infected with TMV. J Gen Virol. 47:79–87. doi:10.1099/0022-1317-47-1-79
   Web of Science ®Google Scholar
• Berger LR, Reynolds DM. 1958. The chitinase system of a strain of Streptomyces griseus. Biochem Biophys Acta. 29:522–534. doi:10.1099/0022-1317-47-1-79
   PubMed Web of Science ®Google Scholar
• Castro MS, Fontes W. 2005. Plant defense and antimicrobial peptides. Protein Pept Lett. 12:13–18.
   PubMed Web of Science ®Google Scholar
• Datta K, Tu JM, Oliva N, Ona I, Velazhahan R, Mew TW, Muthukrishnan S, Datta SK. 2001. Enhanced resistance to sheath blight by constitutive expression of infection related rice chitinase in transgenic elite Indica rice cultivars. Plant Sci. 160:405–414. doi:10.1016/S0168-9452(00)00413-1
   PubMed Web of Science ®Google Scholar
• Funnell DL, Lawrence CB, Pedersen JF, Schardl CL. 2004. Expression of the tobacco β-1,3-glucanase, PR-2d, following induction of SAR with Peronospora tabacina. Physiol Mol Plant Pathol. 65:285–296. doi:10.1016/j.pmpp.2005.02.010
   Web of Science ®Google Scholar
• Gomez KA, Gomez AA. 1984. Statistical procedures for agricultural research. New York (NY): Wiley.
   Google Scholar
• Graham MY, Weidner J, Wheeler K, Pelow ML, Graham TL. 2003. Induced expression of pathogenesis-related protein genes in soybean by wounding and the Phytophthora sojae cell wall glucan elicitor. Physiol Mol Plant Pathol. 63:141–149. doi:10.1016/j.pmpp.2003.11.002
   Web of Science ®Google Scholar
• Grant M, Lamb C. 2006. Systemic immunity. Curr Opin Plant Biol. 9:414–420. doi:10.1016/j.pmpp.2003.11.002
   PubMed Web of Science ®Google Scholar
• Gupta P, Ravi I, Sharma V. 2012. Induction of β-1,3-glucanase and chitinase activity in the defense response of Eruca sativa plants against the fungal pathogen Alternaria brassicicola. J Plant Interact. 8:155–161. doi:10.1080/17429145.2012.679705
   Web of Science ®Google Scholar
• Ham KS, Kauffmann S, Albersheim P, Darvill AG. 1991. Host pathogen interactions. XXXIX. A soybean pathogenesis related protein with β-1,3-glucanase activity releases phytoalexin elicitor-active heat-stable fragments from fungal walls. Mol Plant Microbe Interact. 4:545–552.
   Web of Science ®Google Scholar
• Kasprzewska A. 2003. Plant chitinases – regulation and function. Cell Mol Biol Lett. 8:809–824.
   PubMed Web of Science ®Google Scholar
• Kim YJ, Hwang BK. 1997. Isolation of a basic 34 kiloDalton β-1,3-glucanase with inhibitory against Phytophthora capsici from pepper stems. Physiol Mol Plant Pathol. 50:103–115. doi:10.1006/pmpp.1996.0073
   Web of Science ®Google Scholar
• Kirubakaran SI, Sakthivel N. 2007. Cloning and over expression of antifungal barley chitinase gene in Escherichia coli. Protein Exp Purif. 52:1159–1166. doi:10.1016/j.pep.2006.08.012
   Web of Science ®Google Scholar
• Kumar D. 2002. New concept of moth bean improvement. In: Kumar D, Singh NB, editors. Moth bean in India. Jodhpur: Scientific Publishers; p. 31–47.
   Google Scholar
• Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680–685. doi:10.1038/227680a0
   PubMed Web of Science ®Google Scholar
• Lowry OH, Roserbrough NJ, Farr AL, Randell RJ. 1951. Protein measurement with the Folin-phenol reagent. J Biol Chem. 193:265–275.
   PubMed Web of Science ®Google Scholar
• McDowell JM, Dangl JL. 2000. Signal transduction in the plant immune response. Trends Biochem Sci. 25:79–82. doi:10.1016/S0968-0004(99)01532-7
   PubMed Web of Science ®Google Scholar
• Mihail JD, Taylor SJ. 1995. Interpreting variability among isolates for Macrophomina phaseolina in pathogenicity, pycnidium production and chlorate utilization. Can J Bot. 10:1596–1603. doi:10.1139/b95-172
   Google Scholar
• Nazeem PA, Achuthan CR, Babu TD, Parab GV, Girija D, Keshavachandran R, Samiyappan R. 2008. Expression of pathogenesis related proteins in black pepper (Piper nigrum L.) in relation to Phytophthora foot rot disease. J Trop Agr. 46:45–51.
   Google Scholar
• Nelson N. 1944. A photometric adaption of the Somogyi method for the determination of glucose. J Biol Chem. 153:375–380.
   Google Scholar
• Ramesh Sundar A, Velazhahan R, Nagarathinam S, Vidhyasekaran P. 2008. Induction of pathogenesis-related proteins in sugarcane leaves and cell-cultures by a glycoprotein elicitor isolated from Colletotrichum falcatum. Biol Plantarum. 52:321–328. doi:10.1007/s10535-008-0066-8
   Web of Science ®Google Scholar
• Reissig JL, Strominger JL, Leloir LF. 1955. A modified colorimetric method for the estimation of N-acetylamino sugars. J Biol Chem. 217:959–966. doi:10.1007/s10535-008-0066-8
   PubMed Web of Science ®Google Scholar
• Sharma I, Kumari N, Sharma V. 2013. Defense gene expression in Sorghum bicolor against Macrophomina phaseolina in leaves and roots of susceptible and resistant cultivars. J Plant Interact. doi:10.1080/17429145.2013.832425
   Web of Science ®Google Scholar
• Shrestha CL, Ona II, Muthukrishnan S, Mew TW. 2008. Chitinase levels in rice cultivars correlate with resistance to the sheath blight pathogen Rhizoctonia solani. Eur J Plant Pathol. 120:69–77. doi:10.1007/s10658-007-9199-4
   Web of Science ®Google Scholar
• Singh SK, Srivastava HP. 1988. Symptoms of Macrophomina phaseolina infections on moth bean seedling. Ann Arid Zone. 27:151–152.
   Google Scholar
• Somogyi M. 1952. Notes on sugar determination. J Biol Chem. 195:19–23.
   PubMed Web of Science ®Google Scholar
• Theis T, Stahl U. 2004. Antifungal protein: target, mechanism and prospective applications. Cell Mol Life Sci. 61:437–455. doi:10.1007/s00018-003-3231-4
   PubMed Web of Science ®Google Scholar
• Van Loon LC. 1999. Occurrence and properties of plant pathogenesis-related proteins. In: Datta SK, Muthukrishnan S, editors. Pathogenesis-related proteins in plants. Boca Raton (FL): CRC Press LLC, p. 1–19.
   Google Scholar
• Van't Slot KAE, Knogge W. 2002. A dual role for microbial pathogen-derived effector proteins in plant disease and resistance. Crit Rev Plant Sci. 21:229–271. doi:10.1080/0735-260291044223
   Web of Science ®Google Scholar
• Velazhahan R, Muthukrishnan S. 2004. Transgenic tobacco plants constitutively overexpressing a rice thaumatin-like protein (PR-5) show enhanced resistance to Alternaria alternata. Biol Plant. 47:347–354. doi:10.1080/0735-260291044223
   Web of Science ®Google Scholar
• Verdcourt B. 1970. Studies in leguminosae-papilionoideae for the flora of tropical east Africa IV. Kew. Bull. 24:235–307.
   Google Scholar