Surface-expressed enolases of Plasmodium and other pathogens
Enolase is the eighth enzyme in the glycolytic pathway, a reaction that generates ATP from phosphoenol pyruvate in cytosolic compartments. Enolase is essential, especially for organisms devoid of the Krebs cycle that depend solely on glycolysis for energy. Interestingly, enolase appears to serve a separate function in some organisms, in that it is also exported to the cell surface via a poorly understood mechanism. In these organisms, surface enolase assists in the invasion of their host cells by binding plasminogen, an abundant plasma protease precursor. Binding is mediated by the interaction between a lysine motif of enolase with Kringle domains of plasminogen. The bound plasminogen is then cleaved by specific proteases to generate active plasmin. Plasmin is a potent serine protease that is thought to function in the degradation of the extracellular matrix surrounding the targeted host cell, thereby facilitating pathogen invasion. Recent work revealed that the malaria parasite Plasmodium also expresses surface enolase, and that this feature may be essential for completion of its life cycle. The therapeutic potential of targeting surface enolases of pathogens is discussed.
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Instituto Oswaldo Cruz, Ministério da Saúde
2011
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oai:scielo:S0074-027620110009000112011-08-26Surface-expressed enolases of Plasmodium and other pathogensGhosh,Anil KumarJacobs-Lorena,Marcelo Plasmodium cell surface enolase pathogenicity Enolase is the eighth enzyme in the glycolytic pathway, a reaction that generates ATP from phosphoenol pyruvate in cytosolic compartments. Enolase is essential, especially for organisms devoid of the Krebs cycle that depend solely on glycolysis for energy. Interestingly, enolase appears to serve a separate function in some organisms, in that it is also exported to the cell surface via a poorly understood mechanism. In these organisms, surface enolase assists in the invasion of their host cells by binding plasminogen, an abundant plasma protease precursor. Binding is mediated by the interaction between a lysine motif of enolase with Kringle domains of plasminogen. The bound plasminogen is then cleaved by specific proteases to generate active plasmin. Plasmin is a potent serine protease that is thought to function in the degradation of the extracellular matrix surrounding the targeted host cell, thereby facilitating pathogen invasion. Recent work revealed that the malaria parasite Plasmodium also expresses surface enolase, and that this feature may be essential for completion of its life cycle. The therapeutic potential of targeting surface enolases of pathogens is discussed.info:eu-repo/semantics/openAccessInstituto Oswaldo Cruz, Ministério da SaúdeMemórias do Instituto Oswaldo Cruz v.106 suppl.1 20112011-08-01info:eu-repo/semantics/articletext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762011000900011en10.1590/S0074-02762011000900011 |
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Ghosh,Anil Kumar Jacobs-Lorena,Marcelo |
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Ghosh,Anil Kumar Jacobs-Lorena,Marcelo Surface-expressed enolases of Plasmodium and other pathogens |
author_facet |
Ghosh,Anil Kumar Jacobs-Lorena,Marcelo |
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Ghosh,Anil Kumar |
title |
Surface-expressed enolases of Plasmodium and other pathogens |
title_short |
Surface-expressed enolases of Plasmodium and other pathogens |
title_full |
Surface-expressed enolases of Plasmodium and other pathogens |
title_fullStr |
Surface-expressed enolases of Plasmodium and other pathogens |
title_full_unstemmed |
Surface-expressed enolases of Plasmodium and other pathogens |
title_sort |
surface-expressed enolases of plasmodium and other pathogens |
description |
Enolase is the eighth enzyme in the glycolytic pathway, a reaction that generates ATP from phosphoenol pyruvate in cytosolic compartments. Enolase is essential, especially for organisms devoid of the Krebs cycle that depend solely on glycolysis for energy. Interestingly, enolase appears to serve a separate function in some organisms, in that it is also exported to the cell surface via a poorly understood mechanism. In these organisms, surface enolase assists in the invasion of their host cells by binding plasminogen, an abundant plasma protease precursor. Binding is mediated by the interaction between a lysine motif of enolase with Kringle domains of plasminogen. The bound plasminogen is then cleaved by specific proteases to generate active plasmin. Plasmin is a potent serine protease that is thought to function in the degradation of the extracellular matrix surrounding the targeted host cell, thereby facilitating pathogen invasion. Recent work revealed that the malaria parasite Plasmodium also expresses surface enolase, and that this feature may be essential for completion of its life cycle. The therapeutic potential of targeting surface enolases of pathogens is discussed. |
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Instituto Oswaldo Cruz, Ministério da Saúde |
publishDate |
2011 |
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http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0074-02762011000900011 |
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AT ghoshanilkumar surfaceexpressedenolasesofplasmodiumandotherpathogens AT jacobslorenamarcelo surfaceexpressedenolasesofplasmodiumandotherpathogens |
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1756383708136341504 |