Genes encoding cysteine-motifs have been identified in ichnoviruses and bracoviruses. Proteins are characterized by one or more cysteine-knot structural motifs (Dupuy et al., 2006; Gill et al, 2006) with conserved cysteine residues spaced with hypervariable residues (Dupas et al. 2003). In vivo expression of CsIV VHv1.1 protein in H. virescens using recombinant baculovirus showed that this protein is involved in reducing the encapsulation response to washed wasp eggs. The localization of the protein on the surface of plasmatocytes and within gran-ulocytes suggests that the effect on encapsulation is mediated via surface receptors (Li and Webb, 1994). Furthermore, injection of recombinant VHv1.1 resulted in increased mortality of H. virescens larvae infected with baculoviruses providing further evidence for the role of cysteine-motif proteins in immunosuppressive activities (Fath-Goodin et al., 2006). Interestingly, TSP14, which is a cysteine-motif protein derived from teratocytes, is associated with inhibition of insect growth and development in H. virescens parasitized by M. croceipes wasps (Rana et al., 2002). Feeding caterpillars with recombinant VHv1.1 also had an impact on larval growth (Fath-Goodin et al., 2006). Since cysteine-motif proteins have been shown to have the capacity to reduce in vitro translation of RNAs from different host tissues, it has been postulated that these proteins may act by inhibiting translation, leading to disruption of immune responses and development (Kim, 2005; Fath-Goodin et al., 2006).
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