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History of Plant Lectin Research
2014Numerous plant species are known to express one or more lectins or proteins containing a lectin domain, enabling these proteins to select and bind specific carbohydrate structures. The group of plant lectins is quite heterogeneous since lectins differ in their molecular structure, specificity for certain carbohydrate structures, and biological ...
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Plant Lectins (Phytohemagglutinins)
1976It was already recognized at the end of the last century that proteins in extracts of certain plants are able to agglutinate red blood cells. For a long time this potency has been regarded as a curiosity only. Retrospectively however, it can be said that studies with the respective proteins were landmarks in the elucitation of the basic mechanisms of ...
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1981
The term lectin [Latin, legere — to pick out, choose] was coined by W. C. Boyd1 in order to call attention to a group of plant seed proteins which could distinguish among human blood groups. Boyd had discovered that extracts of the lima bean (Phaseolus lunatus) specifically agglutinated type A erythrocytes (Fig. 1).
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The term lectin [Latin, legere — to pick out, choose] was coined by W. C. Boyd1 in order to call attention to a group of plant seed proteins which could distinguish among human blood groups. Boyd had discovered that extracts of the lima bean (Phaseolus lunatus) specifically agglutinated type A erythrocytes (Fig. 1).
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Carbohydrate-Binding Sites of Plant Lectins
1988Lectins are a diverse group of proteins and glycoproteins that exhibit specific binding for certain carbohydrates. Proteins with this property have been described in a wide variety of taxa, ranging from bacteria (e.g. Neter 1956) to slime molds (Barondes and Haywood 1979) and lower vertebrates (Simpson et al.
G N, Reeke, J W, Becker
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Plant Lectin as defense proteins
Biotech Today : An International Journal of Biological Sciences, 2015Plant lectins are a very heterogeneous group of protein that all share one important biological property: they can recognize and bind reversibly to specific carbohydrate structures. They are one of the most important secondary metabolites in plants which are used as a defense tool against pathogens which attack plants.
Nitasha Thakur, Neelam Sharma
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Recombinant Plant Lectins and Their Mutants
2003Publisher Summary This chapter focuses on recombinant plant lectins, especially those that have been investigated by mutagenesis. Cloning and expression of plant lectins have developed into powerful tools in aiding investigations of the structure–function relationships in their lectins.
Hansjörg, Streicher, Nathan, Sharon
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Ribosome-inactivating lectins of plants
Molecular Biology, 2006A heterogeneous group of plant proteins are capable of enzymatically inactivating ribosomes by depurination of the invariant adenine in the 28S rRNA. Some of these proteins are heterodimers, containing a lectin subunit joined to an enzymatic subunit via a disulfide bond.
J. V. Kozlov +2 more
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Lectin Receptor Kinases in Plants
Critical Reviews in Plant Sciences, 2002Referee: Dr. Philip Becraft, Zoology and Genetics/Agronomy Depts., 2116 Molecular Building, lowa State University, Ames, IA 50011 Forty-two lectin receptor kinase (lecRK)-related sequences and nine related soluble legume lectin sequences were identified in the Arabidopsis thaliana genome.
Annick Barre +3 more
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Lectins and lectin-like molecules in lower plants — II. Freshwater algae
Developmental & Comparative Immunology, 1985Freshwater chlamydomonad algae possess flagella surface isoagglutinins of a glycoprotein nature which are involved in gamete recognition and consequent cell fusion. Alternatively, such molecules may have a receptor role in certain Chlamydomonas species. In some freshwater volvocaines, lectin-like substances act as inducers of sexuality.
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1993
Lectins are carbohydrate-binding proteins of nonimmune origin which occur throughout the biosphere (Goldstein and Poretz 1986). Their most obvious property, hemagglutination, has been known for more than a century (Franz 1988), whereas the art of purifying lectins is much younger.
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Lectins are carbohydrate-binding proteins of nonimmune origin which occur throughout the biosphere (Goldstein and Poretz 1986). Their most obvious property, hemagglutination, has been known for more than a century (Franz 1988), whereas the art of purifying lectins is much younger.
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