Enhanced Tolerance against a Fungal Pathogen and Insect Resistance in Transgenic Tobacco Plants Overexpressing an Endochitinase Gene from Serratia marcescens.

Samantha Sarai Navarro-González,Paul Gaytán,Guadalupe Peña-Chora,Gerardo Corzo,Abigail Roldán-Salgado,Laura Patricia Lina-García,José Augusto Ramírez-Trujillo,Ramón Suárez-Rodríguez,Víctor Manuel Hernández-Velázquez

doi:10.3390/ijms20143482

Abstract

In this study we cloned a chitinase gene (SmchiC), from Serratia marcescens isolated from the corpse of a Diatraea magnifactella lepidopteran, which is an important sugarcane pest. The chitinase gene SmchiC amplified from the S. marcescens genome was cloned into the transformation vector p2X35SChiC and used to transform tobacco (Nicotiana tabacum L. cv Petit Havana SR1). The resistance of these transgenic plants to the necrotrophic fungus Botrytis cinerea and to the pest Spodoptera frugiperda was evaluated: both the activity of chitinase as well as the resistance against B. cinerea and S. frugiperda was significantly higher in transgenic plants compared to the wild-type.

Highlights

Productivity of crops grown for human consumption is at risk due to the incidence of pathogens and pests
Due to the importance of the chitinolytic enzymes in the growth and development of insects, nematodes and fungi, they are of note with respect to their development as biopesticides or defense proteins in transgenic plants and pest control agents
The result of the phylogenetic analysis suggested that all chitinases evolved from the same ancestor, and that SmchiC shared a common evolutionary origin with chitinases from other bacteria (Figure 1b)

Summary

Introduction

Productivity of crops grown for human consumption is at risk due to the incidence of pathogens and pests. Due to the importance of the chitinolytic enzymes in the growth and development of insects, nematodes and fungi, they are of note with respect to their development as biopesticides or defense proteins in transgenic plants and pest control agents. In this context, glycosyl hydrolase enzymes have the ability to hydrolyze the unbranched polymer of chitin comprised of β-1,4-N-acetylglucosamine (GlcNAc), the second most abundant polymer in nature, after cellulose [4], GlcNAc is widely distributed in nature in the outer skeleton of insects and in internal structures, as well as in fungi, yeasts, algae, crabs, shrimps, and plants [5]

Methods

Results

Discussion

Conclusion