Hemolymph protease-17b activates proHP6 to stimulate melanization and Toll signaling in Manduca sexta.

ABSTRACT: Manduca sexta hemolymph protease-6 (HP6) plays a central role in coordinating antimicrobial responses, such as prophenoloxidase (PPO) activation and Toll signaling. Our previous studies indicated that HP5 and GP6 activate proHP6 in larval hemolymph and extraembryonic tissues, respectively. Here, we report the characterization of HP17b as another HP6 activating enzyme and its regulation by multiple serpins in hemolymph. The precursor of HP17b expressed in baculovirus infected Sf9 cells became spontaneously cleaved at two sites, and these products were purified together in one preparation named HP17b', a mixture of proHP17b, a 35 kDa intermediate, and HP17b. HP17b' converted proHP6 to HP6. As reported before, HP6 converted precursors of PPO activating protease-1 (PAP1) and HP8 to their activ

SUBMITTER: Wang Y 

PROVIDER: S-EPMC11558693 | biostudies-literature | 2024 Nov

REPOSITORIES: biostudies-literature