Surface-expressed enolases of Plasmodium and other pathogens

Anil Kumar Ghosh, Marcelo Jacobs-Lorena

Research output: Contribution to journalArticle

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.

Original languageEnglish (US)
Pages (from-to)85-90
Number of pages6
JournalMemorias do Instituto Oswaldo Cruz
Volume106
Issue numberSUPPL. 1
DOIs
StatePublished - Aug 2011

Fingerprint

Plasmodium
Phosphopyruvate Hydratase
Plasminogen
Fibrinolysin
Peptide Hydrolases
Plasmodium malariae
Kringles
Citric Acid Cycle
Serine Proteases
Glycolysis
Life Cycle Stages
Pyruvic Acid
Lysine
Extracellular Matrix
Parasites
Adenosine Triphosphate
Enzymes

Keywords

  • Cell surface enolase
  • Pathogenicity
  • Plasmodium

ASJC Scopus subject areas

  • Microbiology (medical)

Cite this

Surface-expressed enolases of Plasmodium and other pathogens. / Ghosh, Anil Kumar; Jacobs-Lorena, Marcelo.

In: Memorias do Instituto Oswaldo Cruz, Vol. 106, No. SUPPL. 1, 08.2011, p. 85-90.

Research output: Contribution to journalArticle

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