Surface-expressed enolases of Plasmodium and other pathogens
Mem. Inst. Oswaldo Cruz
; 106(supl.1): 85-90, Aug. 2011. ilus, tab
Article
em En
| LILACS
| ID: lil-597248
Biblioteca responsável:
BR1.1
ABSTRACT
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.
Palavras-chave
Texto completo:
1
Coleções:
01-internacional
Base de dados:
LILACS
Assunto principal:
Fosfopiruvato Hidratase
/
Plasmodium
/
Membrana Celular
Limite:
Animals
Idioma:
En
Revista:
Mem. Inst. Oswaldo Cruz
Assunto da revista:
MEDICINA TROPICAL
/
PARASITOLOGIA
Ano de publicação:
2011
Tipo de documento:
Article
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Project document
País de afiliação:
Estados Unidos
País de publicação:
Brasil