Differential inhibition of BmRelish1-dependent transcription in lepidopteran cells by bracovirus ankyrin-repeat proteins

In the tripartite parasitization system of the lepidopteran host Manduca sexta, the endoparasitoid wasp Cotesia congregata and its endosymbiotic virus, C. congregata Bracovirus (CcBV), the expression of viral proteins is necessary for successful parasitization. Here we have examined the in vitro effects of six members of the ankyrin-repeat protein family (Ank) of CcBV, which are thought to interfere with the host’s induced innate immune responses, on the transcriptional activity of a heterologous lepidopteran Rel/NFκB transcription factor, Relish1 of Bombyx mori. Using as transcriptional activator BmRelish1-d2 (R1d2), a constitutively active mutant of the major regulator of the Imd pathway, BmRelish1, in conjunction with a reporter gene controlled by a B. mori antimicrobial peptide gene promoter, we have found that 5 of the 6 examined Anks suppress R1d2-dependent transcriptional activity to various degrees. Immunofluorescence studies have also revealed that while some of the Ank proteins have a rather strict cytoplasmic localization, others are detected both in the cytoplasm and the nucleus of the expressing cells and that colocalization with R1d2 occurs exclusively in the nucleus. Thus, our results suggest that functional and spatial differences among the various CcBV Ank family members may be responsible for the observed differential inhibition of R1d2 activity.

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► Six ankyrin-repeat proteins (Anks) of Cotesia congregata Bracovirus are studied.
► Immunofluorescence analysis revealed variation in their subcellular localization.
► Five Anks suppress an active mutant of the silkworm NFκB homologue, Relish1.
► Some Anks colocalize with Relish1 mutant and interact with intact Relish1.
► Functional and spatial differences between CcBV Ank family members are deciphered.