Elsevier

Advances in Botanical Research

Volume 26, 1997, Pages 135-170, A170, B170, C170, D170, 171-192
Advances in Botanical Research

Plant Proteins that Confer Resistance to Pests and Pathogens

https://doi.org/10.1016/S0065-2296(08)60120-2Get rights and content

Publisher Summary

Throughout their lives, from dormant seed to maturity, plants are exposed to attack by a wide variety of potentially pathogenic microorganisms, predatory insects and other invertebrate pests. Plant resistance is often divided into constitutive defense, expressed as a normal feature of plant development, or inducible defense, switched on following contact with the invading organism. A fundamental distinction is often drawn between pre–existing or constitutive features of the plant, and inducible systems switched on following challenge by a pest or pathogen. Lectins bind to chitin and other glycoconjugates containing N–acetylglycosamine or N–acetylneuraminic acid, and also cause the agglutination of mammalian red blood cells. The most widely studied graminaceous lectin is wheat germ agglutinin, an Mr 36000 protein consisting of two identical 171–residue chains. Thionins were first purified from wheat flour in the early 1940s and called purothionins. Lysozymes from egg white and bacteriophage are among the most widely studied proteins; they inhibit bacterial growth by hydrolysis of cell–wall peptidoglycans. In devising strategies for the manipulation of defense proteins in transgenic plants it is essential to consider the behavior of the target organism, as well as the construct to be used. The specificity of protective proteins for different groups of insects and other invertebrates provides an opportunity to develop resistances that are either highly specific or have wide spectra, based on individual proteins or combinations. A combination of protective proteins may also assist in preventing the development of resistance to individual components.

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      Such phytochemicals also include the plant proteinase inhibitors (PIs) that have evolved over the years, as adaptive responses to any biotic or abiotic stress, and are often accompanied by a spectrum of functional traits which manifests their regulatory role in diverse biochemical functions. For instance, role of PIs have been well documented as bioinsecticidal agents [2–6], in antifungal property [7], as anticarcinogenic agents [8], suppression of retroviruses replication [9], hemolytic activity [10], regulation of metabolism/proteolytic cascades [11] and inhibition of intraerythrocytic development of Plasmodium falciparum [12]. Overall, PIs have been categorized into 59 distinct families [13,14] which have been further sub-classified into serine, cysteine, aspartic or metallo proteinase inhibitors.

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