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Insights into anti-pathogenic activities of mannose lectins
Carbohydrate-binding proteins, also known as lectins, are valuable tools for biotechnology, including pharmacological uses. Mannose lectins obtained from plant and animal sources are applied to protection and characterization of autoimmune diseases as well as defense proteins against pathogens. The...
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Published in: | International journal of biological macromolecules 2019-11, Vol.140, p.234-244 |
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Main Authors: | , , , , |
Format: | Article |
Language: | English |
Subjects: | |
Citations: | Items that this one cites Items that cite this one |
Online Access: | Get full text |
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Summary: | Carbohydrate-binding proteins, also known as lectins, are valuable tools for biotechnology, including pharmacological uses. Mannose lectins obtained from plant and animal sources are applied to protection and characterization of autoimmune diseases as well as defense proteins against pathogens. The presence of mannose-binding lectins in plants that also recognize glucose could be entitled Man/Glc lectins; such specificity has allowed employing these vegetal lectins for several applications. Animal mannose-binding lectins are synthesized in the liver and secreted into the blood stream where both concentration and activity are greatly affected due to gene polymorphisms; these serum proteins play important roles in the immune system by recognizing mannose-like carbohydrate ligands found exclusively on pathogenic microorganisms. Mannose lectins already showed strong binding to relevant bacteria, viruses, protozoa and helminth species, initiating potent host defense mechanisms by inducing growth inhibition or death of such organisms; the ability to prevent the formation or destruction of microbial biofilms has also been reported. Mannose-binding lectins have attracted considerable attention against carcinogenesis and atherogenesis. The aim of this review article is to approach biotechnology characteristics of these lectins from different sources and microorganism/cell surface interactions with mannose; in addition, aspects of mechanisms associated to lectin antipathogenic activities are described. |
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ISSN: | 0141-8130 1879-0003 |
DOI: | 10.1016/j.ijbiomac.2019.08.059 |