Lectins: Carbohydrate-Specific Proteins That Mediate Cellular Recognition.

1. 1 ntrodllction . . 2. Activation of Defense Responses . . 3. Classes of Defense-Related Proteins ... . . . . ....... .. ... . . . . . . . . . . . . . .. . . ... .... . . . . . . .. . . . Core enzymes of phenylpropanoid metabolism ........ " .. . . . . . . "" . . . . . . . . . . . . . . . . . . . 4. Proteins that Change the Properties of the Extracellular Matrix , Extensins: hydroxyproline-rich glycoproteins . Glycine-rich proteins . Peroxidases . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . Cinnamyl alcohol dehydrogenase .... .. . . . .... .. . . ........ . ...... .. . . . .... . ....... . . . . . .. . Callose synthetase . 5. Proteins Associated with Deterrence and Antimicrobial Activif)l . . Endohydrolases ........ .. ......... ...... . "'" Thionins . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . ������a;!: li fn�r:;;���;��. : : : : : : : : : : : : : : : : : : : :: : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : : Late enzymes of phytoalexin biosynthesis . 6. Additional Defense-Related Proteins " . . . . . . . . . . Pathogenesis-related proteins ........ " . .. . . . . . . . . . . . . . . . . ..... . . . . . . . . . . . . . . . .. Proteins encoded by wun 1 and wun 2 . . Proteins encoded by win 1 and win 2 . ELl products . . . ... .... . . . . . .. . . . . . . . . . . . . . . . . ... . . . . . . . . . . . . . . . . . ... . . . . . . . . . . . . . . . .. . . . .. . . . . Elicitor-induced products . . . . . .. . . . . . . . . . . . . . . . . . . . .. . .. . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 7. Coordination of Defense Responses """""""" . . . . . . . . . . . . . . . . . .. . . . . . . . . . . . . . . . . . . . , 8. Concluding Remarks... .. . .. .. . . . ...... ".

Defense-related proteins in higher plants.

The occurrence in nature of erythrocyte-agglutinating proteins has been known since the turn of the 19th century. By the 1960s it became apparent that such proteins also agglutinate other types of cells, and that many of them are sugar-specific. These cell-agglutinating and sugar-specific proteins have been named lectins. Although shown to occur widely in plants and to some extent also in invertebrates, very few lectins had been isolated until the early 1970s, and they had attracted little attention. This attitude changed with the demonstration that lectins are extremely useful tools for the investigation of carbohydrates on cell surfaces, in particular of the changes that the latter undergo in malignancy, as well as for the isolation and characterization of glycoproteins. In subsequent years numerous lectins have been isolated from plants as well as from microorganisms and animals, and during the past two decades the structures of hundreds of them have been established. Concurrently, it was shown that lectins function as recognition molecules in cell-molecule and cell-cell interactions in a variety of biological systems. Here we present a brief account of 100-plus years of lectin research and show how these proteins have become the focus of intense interest for biologists and in particular for the glycobiologists among them.

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History of lectins: from hemagglutinins to biological recognition molecules

Multivalent ligands can function as inhibitors or effectors of biological processes. Potent inhibitory activity can arise from the high functional affinities of multivalent ligand-receptor interactions. Effector functions, however, are influenced not only by apparent affinities but also by alternate factors, including the ability of a ligand to cluster receptors. Little is known about the molecular features of a multivalent ligand that determine whether it will function as an inhibitor or effector. We envisioned that, by altering multivalent ligand architecture, ligands with preferences for different binding mechanisms would be generated. To this end, a series of 28 ligands possessing structural diversity was synthesized. This series provides the means to explore the effects of ligand architecture on the inhibition and clustering of a model protein, the lectin concanavalin A (Con A). The structural parameters that were varied include scaffold shape, size, valency, and density of binding elements. We found that ligands with certain architectures are effective inhibitors, but others mediate receptor clustering. Specifically, high molecular weight, polydisperse polyvalent ligands are effective inhibitors of Con A binding, whereas linear oligomeric ligands generated by the ring-opening metathesis polymerization have structural properties that favor clustering. The shape of a multivalent ligand also influences specific aspects of receptor clustering. These include the rate at which the receptor is clustered, the number of receptors in the clusters, and the average interreceptor distance. Our results indicate that the architecture of a multivalent ligand is a key parameter in determining its activity as an inhibitor or effector. Diversity-oriented syntheses of multivalent ligands coupled with effective assays that can be used to compare the contributions of different binding parameters may afford ligands that function by specific mechanisms.

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Influencing Receptor−Ligand Binding Mechanisms with Multivalent Ligand Architecture

Grain legume proteins and nutraceutical properties

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Irvin E. Liener

Papers

The Lectins: Properties, Functions and Applications in Biology and Medicine