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Insights into anti-pathogenic activities of mannose lectins.

Authors :
Dos Santos Silva PM
de Oliveira WF
Albuquerque PBS
Dos Santos Correia MT
Coelho LCBB
Source :
International journal of biological macromolecules [Int J Biol Macromol] 2019 Nov 01; Vol. 140, pp. 234-244. Date of Electronic Publication: 2019 Aug 07.
Publication Year :
2019

Abstract

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.<br /> (Copyright © 2019 Elsevier B.V. All rights reserved.)

Details

Language :
English
ISSN :
1879-0003
Volume :
140
Database :
MEDLINE
Journal :
International journal of biological macromolecules
Publication Type :
Academic Journal
Accession number :
31400430
Full Text :
https://doi.org/10.1016/j.ijbiomac.2019.08.059