Identification of parasite-responsive cysteine proteases in Manduca sexta
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Céline Serbielle
, Sébastien Moreau , Florian Veillard , Emilien Voldoire , Annie Bézier , Marie-Anne Mannucci , Anne-Nathalie Volkoff , Jean-Michel Drezen , Gilles Lalmanach and Elisabeth Huguet
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.
©2009 by Walter de Gruyter Berlin New York
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- Reviews
- The liaison between apoptotic cells and macrophages – the end programs the beginning
- Activation mechanisms of coagulation factor IX
- Subsite cooperativity in protease specificity
- Minireview
- Retrodifferentiation – a mechanism for cellular regeneration?
- Protein Structure and Function
- The solution structure of pGolemi, a high affinity Mena EVH1 binding miniature protein, suggests explanations for paralog-specific binding to Ena/VASP homology (EVH) 1 domains
- 3D structure of a binary ROP-PRONE complex: the final intermediate for a complete set of molecular snapshots of the RopGEF reaction
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