Extracellular functions of glycolytic enzymes of parasites: Unpredicted use of ancient proteins |
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Authors: | Amaranta Gó mez-Arreaza,Hector Acosta,Wilfredo Quiñ ones,Juan Luis Concepció n,Paul A.M. Michels,Luisana Avilá n |
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Affiliation: | 1. Laboratorio de Fisiología Animal, Departamento de Biología, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela;2. Laboratorio de Enzimología de Parásitos, Departamento de Biología, Facultad de Ciencias, Universidad de Los Andes, Mérida 5101, Venezuela;3. Institute of Structural and Molecular Biology, School of Biological Sciences, University of Edinburgh, King''s Buildings, Edinburgh EH9 3JU, Scotland, UK |
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Abstract: | In addition of their usual intracellular localization where they are involved in catalyzing reactions of carbohydrate and energy metabolism by glycolysis, multiple studies have shown that glycolytic enzymes of many organisms, but notably pathogens, can also be present extracellularly. In the case of parasitic protists and helminths, they can be found either secreted or attached to the surface of the parasites. At these extracellular localizations, these enzymes have been shown to perform additional, very different so-called “moonlighting” functions, such as acting as ligands for a variety of components of the host. Due to this recognition, different extracellular glycolytic enzymes participate in various important parasite–host interactions such as adherence and invasion of parasites, modulation of the host's immune and haemostatic systems, promotion of angiogenesis, and acquisition of specific nutrients by the parasites. Accordingly, extracellular glycolytic enzymes are important for the invasion of the parasites and their establishment in the host, and in determining their virulence. |
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Keywords: | ALD, aldolase ENO, enolase GAPDH, glyceraldehyde-3-phosphate dehydrogenase HK, hexokinase PFK, phosphofructokinase PGAM, phosphoglycerate mutase PGI, glucose-6-phosphate isomerase PYK, pyruvate kinase TIM, triosephosphate isomerase |
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