130 years of Plant Lectin Research
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REVIEW ARTICLE
130 years of Plant Lectin Research Mariya Tsaneva 1 & Els J. M. Van Damme 1 Received: 19 April 2020 / Revised: 12 July 2020 / Accepted: 21 August 2020 # Springer Science+Business Media, LLC, part of Springer Nature 2020
Abstract Lectins are proteins with diverse molecular structures that share the ability to recognize and bind specifically and reversibly to carbohydrate structures without changing the carbohydrate moiety. The history of lectins started with the discovery of ricin about 130 years ago but since then our understanding of lectins has dramatically changed. Over the years the research focus was shifted from ‘the characterization of carbohydrate-binding proteins’ to ‘understanding the biological function of lectins’. Nowadays plant lectins attract a lot of attention especially because of their potential for crop improvement and biomedical research, as well as their application as tools in glycobiology. The present review aims to give an overview of plant lectins and their applications, and how the field evolved in the last decades. Keywords Lectin . Plant protection . Biomedical application . Protein-carbohydrate interaction . Glycobiology
Historical overview Plant lectin research started more than 130 years ago. Since then many biochemists and molecular biologists have been intrigued by this particular group of carbohydrate-binding proteins. In 1888 Stillmark reported a highly toxic protein from the seeds of castor bean (Ricinus communis L.). The protein, referred to as ‘ricin’ revealed hemagglutination activity and later turned out to be the first lectin [1]. Consequently 1888 is accepted as the start of lectinology, although Dixson already hypothesized the presence of protein-like toxins one year earlier [2]. Since the discovery of ricin our knowledge and ideas related to lectins and their biological activities have constantly evolved in accordance with new discoveries and new technologies that became available. The most important hallmarks in the history of the plant lectinology are highlighted in Fig. 1. Ten years after the first report on ricin Elfstrand introduced the term ‘agglutinin’ to describe all proteins that cause hemagglutination or agglutination of red blood cells [3]. In the same year Ehrlich discovered some of the fundamental principles in immunology using sublethal doses of ricin and abrin * Els J. M. Van Damme [email protected] 1
Laboratory of Biochemistry and Glycobiology, Department of Biotechnology, Faculty of Bioscience Engineering, Ghent University, Coupure Links 653, 9000 Ghent, Belgium
in mice models namely the specificity of the immune response, the existence of an immunological memory against distinct antigens and the ability of the mother to transfer antibodies during pregnancy and through the milk [4]. Landsteiner and Raubitschek [5] discovered that not all agglutinating proteins isolated from legume seeds (e.g. Phaseolus vulgaris (bean), Pisum sativum (pea), Lens culinaris (lentil), and Vicia sativa (vetch)) are toxic. In 1919 Sumner reported the p
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