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Identification of parasite-responsive cysteine proteases in Manduca sexta

  • Céline Serbielle , Sébastien Moreau , Florian Veillard , Emilien Voldoire , Annie Bézier , Marie-Anne Mannucci , Anne-Nathalie Volkoff , Jean-Michel Drezen , Gilles Lalmanach and Elisabeth Huguet
Published/Copyright: April 10, 2009

Abstract

Parasites have evolved different virulence strategies to manipulate host physiological functions. The parasitoid wasp Cotesia congregata induces developmental arrest and immune suppression of its Lepidopteran host Manduca sexta. In this interaction, a symbiotic virus (C. congregata Bracovirus, CcBV) associated with the wasp is essential for parasitism success. The virus is injected into the host with wasp eggs and virus genes are expressed in host tissues. Among potential CcBV virulence genes, cystatins, which are tight binding inhibitors of C1A cysteine proteases, are suspected to play an important role in the interaction owing to their high level of expression. So far, however, potential in vivo targets in M. sexta are unknown. Here, we characterized for the first time four M. sexta C1A cysteine proteases corresponding to cathepsin L and cathepsin B and two different ‘26–29 kDa’ cysteine proteases (MsCath1 and MsCath2). Our analyses revealed that MsCath1 and MsCath2 are transcriptionally downregulated in the course of parasitism. Moreover, viral Cystatin1 and MsCath1 co-localize in the plasma following parasitism, strongly suggesting that they interact. We also show that parasitism induces a general increase of cysteine protease activity which is later controlled. The potential involvement of cysteine proteases in defense against parasitoids is discussed.


Corresponding author

Received: 2009-01-16
Accepted: 2009-05-18
Published Online: 2009-04-10
Published in Print: 2009-05-28

©2009 by Walter de Gruyter Berlin New York

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