Overexpression of β-1,3-Glucanase Gene in Response to Phytophthora palmivora Infection in Leaves of Hevea brasiliensis Clones

Anurag SUNPAPAO; Chaninun PORNSURIYA

Authors

Anurag SUNPAPAO Department of Pest Management, Faculty of Natural Resources, Prince of Songkla University, Songkhla 90110
Chaninun PORNSURIYA Department of Pest Management, Faculty of Natural Resources, Prince of Songkla University, Songkhla 90110

Keywords:

β-1, 3-glucanase, Hevea brasiliensis, leaf fall disease, Phytophthora palmivora, PR protein

Abstract

The b-1,3-glucanase (b-glu) gene belongs to pathogenesis-related protein family 2 (PR2), which is induced by pathogens. Leaf fall disease caused by Phytophthora palmivora is the most serious disease affecting Para rubber (Hevea brasiliensis Müll. Arg.) seedlings. In this study, we examined the development of necrotic lesions and the molecular responses shown by H. brasiliensis clones RRIT 251 and RRIM 600 from infection by P. palmivora. The expansion of necrotic lesions on Para rubber leaves was observed around points of inoculation. The expression of b-glu was analyzed by RT-PCR, and the accumulation of b-1,3-glucanase protein was determined by denatured SDS-PAGE. The inoculation tests suggested that RRIT 251 clones have a better resistance than RRIM 600 clones, with infection occurring in 33.34 and 100 % of inoculations, respectively. RNA analysis by RT-PCR demonstrated that both RRIT 251 and RRIM 600 clones expressed the b-glu gene during P. palmivora infection, and protein analysis by denatured SDS-PAGE displayed no obvious differences between the clones. Although expression of the b-glu gene occurred in both clones, the clones differed in phenotype. The better resistance of RRIT 251 relative to RRIM 600 against infection by inoculation may be associated with other defense mechanisms against Phytophthora infection.

doi:10.14456/WJST.2016.4

Downloads

Download data is not yet available.

Metrics

Metrics Loading ...

Author Biography

Anurag SUNPAPAO, Department of Pest Management, Faculty of Natural Resources, Prince of Songkla University, Songkhla 90110

Department of Pest Management

References

E Leiter, H Szappanos, C Oberparleiter, L Kaiserer, L Sernoch, T Pusztahelyi, T Emri, I Po’csi, W Salvenmoser and F Marx. Antifungal protein PAF severely affects the integrity of the plasma membrane of Aspergillus nidulans and induces and apoptosis-like phenotype. Antimicrob. Agents. Chemother. 2005; 49, 2445-53.

CS Adrienne and JH Barbara. Parallels in fungal pathogenesis on plant and animal host: Eukaryot. Cell 2006; 5, 1941-9.

JA Ryals, UH Neuenschwander, MG Willits, A Molina, HY Steiner and MD Hunt. Systemic acquired resistance. Plant Cells 1996; 8, 1809-19.

TP Delaney. Genetic dissection of acquired resistance to disease. Plant Physiol. 1997; 113, 5-12.

LC Van Loon and EAV Strien. The families of pathogenesis-related proteins, their activities, and comparative analysis of PR-1 type proteins. Physiol. Molec. Plant Pathol. 1999; 55, 85-97.

F Mauch and LA Staehelin. Functional implication of the subcellular localization of ethylene-induced chitinase and β-1,3-glucanase in bean leaves. Plant Cells 1989; 1, 447-57.

S Kauffmann, M Legrand, P Geoffroy and B Fritig. Biological function of pathogenesis-related proteins: four PR proteins of tobacco have β-1,3-glucanase activity. EMBO J. 1987; 6, 3209-12.

HJM Linthorst. Pathogenesis-related proteins of plants. Crit. Rev. Plant Sci. 1991; 10, 123-50.

MJ Cordero, D Raventos and B San Segundo. Differential expression and induction of chitinase and β-1,3-glucanase in response to fungal infection during germination of maize seeds. Mol. Plant Microbe Interact. 1994; 7, 23-31.

TY Hong and M Meng. Biochemical characterization and antifungal activity of an endo-1,3-glucanase of Paenibacillus sp. isolated from garden soil. Appl. Microbiol. Biotech. 2004; 61, 472-8.

R Saikia, BP Singh, R Kumar and DK Arora. Detection of pathogenesis-related proteins-chitinase and â-1,3-glucanase in induced chickpea. Curr. Sci. 2005; 89, 659-63.

I Thanseem and A Thulaseedharan. Optimization of RQRT-PCR protocols to measure beta-1,3-glucanase mRNA levels in infected tissues of rubber tree (Hevea brasiliensis). Indian J. Exp. Biol. 2006; 44, 492-8.

CR Simmons. The physiology and molecular biology of plant 1,3-â-D-glucanase and 1,3;14-β-D-glucanase. Crit. Rev. Plant Sci. 1994; 13, 325-87.

PB Hoj and GB Fincher. Molecular evolution of plant â-glucan endohydrolases. Plant J. 1995; 7, 367-9.

JGH Wessels and JH Sietsma. Fungal Cell Wall: A Survey. In: W Tanner and FA Loewus (eds.). Encyclopedia of Plant Physiology, New Series, Plant Carbohydrates II, Springer-Verlag, 1981, p. 352-94.

DJ Adam. Fungal cell wall chitinase and glucanase. Microbiol. 2004; 150, 2029-35.

T Boller. Antimicrobial Functions of the Plant Hydrolyasses Chitinase and β-1,3-glucanase. In: B Friting and MK Legrand (eds.). Developments in Plant Pathology, Academic Publishers, Dordecht, Netherlands, 1993, p. 391-400.

ML Chye and KY Cheung. β-1,3-glucanase is highly-expressed in laticifers of Hevea brasiliensis. Plant Mol. Biol. 1995; 29, 397-402.

T Subroto, GA van Koningsveld, HA Schreuder, UM Soedjanaatmadia and JJ Beintema. Chitinase and β-1,3-glucanase in the lutoid-body fraction of Hevea latex. Phytochem. 1996; 43, 29-37.

T Subroto, E de Vries, JJ Schuringa, UMS Soedjanaatmadja, J Hofsteenge, PA Jekel and JJ Beintema. Enzymatic and structural studies on processed proteins from the vacuolar (lutoid-body) fraction of latex of Hevea brasiliensis. Plant Physiol. Biochem. 2001; 39, 1047-55.

A Kobayashi, N Kiyosawa, Y Suauki, N Murofushi and I Yamaguchi. Pharbitis class-I knotted-like homeobox gene, Pkn3, share similar characteristics to those of class-2 knotted-like genes. Plant Cell Rep. 2000; 19, 911-20.

JAL Van Kan, MHAJ Joosten and CAM Wagemakers. Differential accumulation of mRNAs encoding extracellular and intercellular PR proteins in tomato induced by virulent and avirulent races of Cladosporium fulvum. Plant Mol. Biol. 1992; 20, 513-27.

S Philip, A Joseph, A Kumar, C Jacob and R Kothandaraman. Detection of β-1,3-glucanase isoforms against Corynespora leaf disease of rubber (Hevea brasiliensis). Indian J. Nat. Rubber Res. 2001; 14, 1-6.

C Bormann, D Baier, I Horr, C Raps, J Berger, G Jung and H Schwarz. Characterization of a novel, antifungal, chitin-binding protein from Streptomyces tendae Tu901 that interferes with growth polarity. J. Bacteriol. 1999; 181, 7421-9.

G Jach, B Gornhardt, J Mundy, J Logemann, E Pinsdorf, R Leah, J Schell and C Mass. Enhanced quantitative resistance against fungal disease by combinatorial expression of different barley antifungal proteins in transgenic tobacco. Plant J. 1995; 8, 97-109.

Q Zhu, EA Maher, S Masoud, RA Dixon and CJ Lamb. Enhanced protection against fungal attack by constitutive co-expression of chitinase and glucanase gene in transgenic tobacco. Nat. Biotechnol. 1994; 12, 807-12.

E Jongedijk, H Tigelaar, JSC Van Roekel, SA Bres-Vloemans, I Dekker, PJMV den Elzen, BJC Cornelissen and LS Melchers. Synergistic activity of chitinase and β-1,3-glucanase enhances fungal resistance in transgenic tomato plants. Euphytica 1995; 85, 173-80.

SMJ Ignatius and RK Chopra. Effect of fungal infection and wounding on the expression of chitinase and β-1,3-glucanase in near-isogenic lines of barley. Plant Physiol. 1994; 90, 584-92.

VV Lozovaya, A Waranyuwat and JM Widholm. β-1,3-glucanase and resistance to Aspergillus flavus infection in maize. Crop Sci. 1998; 38, 1255-60.

HW Jung and BK Hwang. Pepper gene encoding a basic β-1,3-glucanase is differentially expressed in pepper tissues upon pathogen infection and ethephon or methyl jasmonate treatment. Plant Sci. 2000; 159, 97-106.

WL Li, JD Faris, S Muthukrishanan, DJ Liu, PD Chen and BS Gill. Isolation and characterization of novel cDNA clones of acidic chitinase and β-1,3-glucanase from wheat spikes infected by Fusarium graminearum. Theor. Appl. Genet. 2001; 102, 353-62.

T Hanselle and W Barz. Purification and characterization of the extracellular PR-2b β-1,3-glucanase accumulating in different Ascochyta rabiei-infected chickpea (Cicer arietinum L.) cultivars. Plant Sci. 2001; 161, 773-81.

AB Zemanek, TS Ko, J Timmapuram, FA Hammerschlag and SS Korban. Changes in β-1,3-glucanase mRNA levels in peach in response to treatment with pathogen culture filtrates, wounding, and other elicitors. J. Plant Physiol. 2002; 159, 877-89.

T Niki, I Mitsuhara, S Seo, N Ohtsubo and Y Ohashi. Antagonistic effect of salicylic acid and jasmonic acid on the expression of pathogenesis-related (PR) protein genes in wounded mature tobacco leaves. Plant Cell Physiol. 1998; 39, 500-7.

ER Ward, SJ Uknes, SC Williams, SS Dincher, DL Wiederhold, DC Alexander, P Ahl-Goy, JP Metraux and JA Ryals. Coordinate gene activity in response to agents that induce systemic acquired resistance. Plant Cell 1991; 3, 1085-94.

E Rezzonico, N Flury, F Meins and R Beffa. Transcriptional down-regulation by abscisic acid of pathogenesis-related β-1,3-glucanase genes in tobacco cell cultures. Plant Physiol. 1998; 117, 585-92.

T Akiyama and MA Pillai. Molecular cloning, characterization and in vitro expression of a novel endo-1,3-glucanase up-regulated by ABA and drought stress in rice (Oryza sativus L.). Plant Sci. 2001; 161, 1089-98.

J Wu, AA Khan, CT Shih and DS Shih. Cloning and sequence determination of a gene encoding an osmotin-like protein from strawberry (Fragaria ananassa Ducth.). DNA Sequence 2001; 12, 447-53.