Reduced cysteine protease activity of the hemolymph of Bombyx mori larvae infected with fp25K-inactivated bombyx mori nucleopolyhedrovirus results in the reduced postmortem host degradation

Abstract

We previously reported that the FP25K gene (fp25K) product of the baculovirus Bombyx mori nucleopolyhedrovirus (BmNPV) is involved in postmortem host degradation. Here, we investigated the mechanism by which reduced postmortem host degradation is caused after the infection of fp25K-mutated BmNPVs. Firstly, we investigated gene expression levels of vcath and chiA both of which products are involved in postmortem host degradation. We found that transcriptional levels of these genes infp25K-mutated BmNPV-infected BmN cells were comparable to those in cells infected with wild-type (wt) BmNPV. Next, we examined the cysteine protease activity in fp25K-mutated BmNPV-infected BmN cells. Although the cysteine protease activity in BmN cells infected with fp25K-mutated BmNPVs was comparable to that of wt BmNPV-infected cells, the released activity in the culture medium is dramatically reduced in that of cells infected with fp25K mutants. We also found that the cysteine protease activity in the hemolymph of fp25K-mutated BmNPV-infected B. mori larvae is drastically reduced compared to that of wt BmNPV-infected larvae. These results show that the release of cysteine protease into the hemolymph of B. mori larvae infected with fp25K-mutated BmNPVs is reduced and, as a consequence, postmortem host degradation of infected insects is lessened.