Abstract
Enolase is a glycolytic and gluconeogenic enzyme also found on the surface of several eukaryotic and prokaryotic cells where it acts as plasminogen binding protein. Leishmania mexicana, one of the causative agents of Leishmaniasis, binds plasminogen and, in this parasite, enolase has been previously found associated with the external face of the plasma membrane. In this work, we show that the purified recombinant enolase has plasminogen binding activity indicating that, at the surface of the parasite, the protein may function as one of the plasminogen receptors. An internal motif 249AYDAERKMY257, similar to the nine amino-acid internal plasminogen-binding motif in Streptococcus pneumoniae enolase, is responsible for plasminogen interaction with the parasite enolase. Anti-enolase antibodies inhibited up to 60% of plasminogen binding on live parasites indicating that enolase act as a plasminogen receptor on the parasite. The fact that enolase acts as a possible plasminogen receptor in vivo makes this protein a promising target for therapy.
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Acknowledgments
This work was supported by CDCHT-ULA Grant C-1321-05-03B. We wish to thank Dr. Anne-Lise Haenni for critical reading of the manuscript.
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Vanegas, G., Quiñones, W., Carrasco-López, C. et al. Enolase as a plasminogen binding protein in Leishmania mexicana . Parasitol Res 101, 1511–1516 (2007). https://doi.org/10.1007/s00436-007-0668-7
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DOI: https://doi.org/10.1007/s00436-007-0668-7