Editor-in-Chief: Brüne, Bernhard
Editorial Board Member: Buchner, Johannes / Lei, Ming / Ludwig, Stephan / Sies, Helmut / Turk, Boris / Wittinghofer, Alfred
SCImago Journal Rank (SJR) 2015: 1.607
Source Normalized Impact per Paper (SNIP) 2015: 0.751
Impact per Publication (IPP) 2015: 2.609
Identification of parasite-responsive cysteine proteases in Manduca sexta
1Institut de Recherche sur la Biologie de l'Insecte, Université François Rabelais, UMR CNRS 6035, Faculté des Sciences et Techniques, Parc de Grandmont, F-37200 Tours, France
2INSERM U 618 ‘Protéases et Vectorisation Pulmonaires’ IFR 135 ‘Imagerie Fonctionnelle’, Université François Rabelais, Faculté de Médecine, 10 Boulevard Tonnellé, F-37032 Tours cedex, France
3Biologie Intégrative et Virologie des Insectes, UMR1231 INRA – Université Montpellier II, Place Eugène Bataillon, F-34095 Montpellier cedex, France
aPresent address: GEMI, CNRS UMR 2724, 911 avenue Agropolis, F-34394 Montpellier cedex 5, France.
Citation Information: Biological Chemistry. Volume 390, Issue 5/6, Pages 493–502, ISSN (Online) 1437-4315, ISSN (Print) 1431-6730, DOI: 10.1515/BC.2009.061, April 2009
- Published Online:
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.
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