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Bm-SP142 is a 35 kDa protease in the silkworm, but its exact functions remain unknown. In this study, sequence alignment revealed that the His-Asp-Ser catalytic triad is embedded in the  TAAHC-DIAL-GDSGGP  sequence motif, establishing Bm-SP142 as a serine protease. Soluble recombinant GST-BmSP142 was expressed and purified, and serine protease activity was confirmed  in vitro . RT-qPCR results indicated that  Bm-SP142  was mainly expressed in the middle part of the silkworm midgut, and  Bm-SP142  transcripts were significantly up-regulated at 24 hours post infection (hpi) in  Bm BDV-resistant strains (798) inoculated with  Bm BDV and  Bm NPV-resistant strains (NB) inoculated with  Bm NPV, but not in  Bm BDV-susceptible strains (306). Surprisingly, transcripts were significantly down-regulated at 12 hpi in  Bm NPV-susceptible strains (HuaBa 35) inoculated with  Bm NPV, compared with healthy silkworms. Recombinant  Bm NPV treated with purified Bm-SP142 effectively impaired its ability to infect BmN cells, and Bm-SP142 decreases the efficiency of  Bm NPV and  Bm BDV propagation in silkworms. Furthermore, overexpression of  Bm-SP142  in BmN cells inhibited viral propagation.

plos one

Serine protease Bm-SP142 was differentially expressed in resistant and susceptible Bombyx mori strains, involving in the defence response to viral infection