Abstract

In plants, polygalacturonase inhibitor proteins (PGIPs) are very important to inactivate polygalacturonases secreted by pathogens. Vitis thunbergii Sieb. et Zucc. polygalacturonase inhibitor proteins (VtPGIP) was first isolated from the wild grape Vitis thunbergii Sieb. et Zucc., which exhibits high resistance to disease. VtPGIP is sublocated in the plant cell wall, and this location is consistent with the function of PGIPs in the first line of host defense. The promoter of VtPGIP contains salicylic acid (SA), abscisic acid (ABA), and fungus infection response elements. Results from real-time quantitative reverse transcriptase (RT)-PCR analysis showed that VtPGIP expression was induced by SA, ABA, and fungi. The results indicated that VtPGIP may have important functions in defense-related responses of V. thunbergii against pathogenic fungi.

Highlights

  • Epiphytes cause significant losses as destructive pathogens of many fruits and vegetables worldwide; such organisms affect the post-harvest industry

  • We found that the species of the same genus were classified into the same group except Eucalyptus grandis, Pyrus communis, and Malus pumila because the polygalacturonase inhibitor protein (PGIP) of these plants may have different evolutionary scenarios

  • For the amino acid sequence, the species of the same genus were classified into the same group, but E. grandis, P. communis, and M. pumila may indicate that PGIPs have various evolutionary histories

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Summary

Introduction

Epiphytes cause significant losses as destructive pathogens of many fruits and vegetables worldwide; such organisms affect the post-harvest industry. A very important aspect is to determine potential molecules that exhibit defense functions in plants, that is, the natural defense system, and the molecules that respond to induction. Fungal disease is caused by the secretion of hydrolytic enzymes to pectin substrates (Fish, 2005). Pathogens can release several types of enzymes, such as exopolygalacturonases and endopolygalacturonases (endoPGs), to breach this barrier and function with pectin methyl and acetyl esterases (Prade et al, 1999) to degrade pectin. Fungal endo-PGs, the first enzymes secreted by fungal plant pathogens, have important functions during the early stages of plant pathogenesis (English et al, 1971) to separate and macerate host tissues, thereby facilitating pathogen penetration and colonization of plant tissues. The products of this degradation process are used as a nutrient source for fungal growth (Karr et al, 1970)

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