Extracellular matrix degradation via Enolase/Plasminogen interaction: Evidence for a mechanism conserved in Metazoa

Autor: Gerarda, Grossi, Annalisa, Grimaldi, Rosa A, Cardone, Magnus, Monné, Stephan J, Reshkin, Rossana, Girardello, Maria R, Greco, Elena, Coviello, Simona, Laurino, Patrizia, Falabella
Jazyk: angličtina
Rok vydání: 2016
Předmět:
Popis: While enolase is a ubiquitous metalloenzyme involved in the glycolytic pathway, it is also known as a multifunctional protein, since enolases anchored on the outer surface of the plasma membrane are involved in tissue invasion.We have identified an extracellular enolase (Ae-ENO) produced by the teratocytes, embryonic cells of the insect parasitoid Aphidius ervi. We demonstrate that Ae-ENO, although lacking a signal peptide, accumulates in cytoplasmic vesicles oriented towards the cell membrane. Ae-ENO binds to and activates a plasminogen-like molecule inducing digestion of the host tissue and thereby ensuring successful parasitism.These results support the hypothesis that plasminogen-like proteins exist in invertebrates. Interestingly the activation of a plasminogen-like protein is mediated by a mechanisms involving the surface enolase/fibrinolytic system considered, until now, exclusive of vertebrates, and that instead is conserved across species.To our knowledge, this is the first example of enolase mediated Plg-like binding and activation in insect cells, demonstrating the existence of an ECM degradation process via a Plg-like protein in invertebrates.
Databáze: OpenAIRE