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Extracellular serine proteinase cascades have evolved in vertebrates and invertebrates to mediate rapid defense reactions to wounding and infection. We have started to investigate such enzyme system and its regulation by proteinase inhibitors in a biochemical model insect, Manduca sexta. In collaboration with Dr. Kanost's group at Kansas State University, we are investigating the prophenoloxidase-activating pathway, a defense mechanism triggered by invading pathogens. Active phenoloxidase catalyzed the formation of reactive intermediates that are utilized to kill pathogens, seal wounds, and encapsulate parasites.
Prophenoloxidase is activated via limited proteolysis. We have purified three different prophenoloxidase-activating proteinases (PAPs) from M. sexta and examined their expression patterns. Transcription of these clip-domain serine proteinases is regulated in tissue-, development-, and defense-specific manners.
We have isolated cDNA clones for 22 different hemolymph proteinases, some of which are members of the serine proteinase system that coordinates the immune responses in M. sexta hemolymph. A modular protein, designated M. sexta HP14, interacts with ß-1,3-glucan or peptidoglycan, autoactivates, and triggers the prophenoloxidase-activating pathway.
This proteinase pathway is negatively regulated by serine proteinase inhibitors of the serpin superfamily. M. sexta serpin-1 variants, serpin-3, -4, -5, and -6 form stable proteinase-inhibitor complexes with one or more of the pathway components. Since molecular probes (e.g., cDNAs and antisera for HPs and serpins) are available, we are attempting to elucidate the prophenoloxidase-activating pathway, its relationships with other proteinase-mediated immune responses, and inhibitory regulation by serpins.
Extracellular serine proteinase cascades have evolved in vertebrates and invertebrates to mediate rapid defense reactions to wounding and infection. We have started to investigate such enzyme system and its regulation by proteinase inhibitors in a biochemical model insect, Manduca sexta. In collaboration with Dr. Kanost's group at Kansas State University, we are investigating the prophenoloxidase-activating pathway, a defense mechanism triggered by invading pathogens. Active phenoloxidase catalyzed the formation of reactive intermediates that are utilized to kill pathogens, seal wounds, and encapsulate parasites.
Prophenoloxidase is activated via limited proteolysis. We have purified three different prophenoloxidase-activating proteinases (PAPs) from M. sexta and examined their expression patterns. Transcription of these clip-domain serine proteinases is regulated in tissue-, development-, and defense-specific manners.
We have isolated cDNA clones for 22 different hemolymph proteinases, some of which are members of the serine proteinase system that coordinates the immune responses in M. sexta hemolymph. A modular protein, designated M. sexta HP14, interacts with ß-1,3-glucan or peptidoglycan, autoactivates, and triggers the prophenoloxidase-activating pathway.
This proteinase pathway is negatively regulated by serine proteinase inhibitors of the serpin superfamily. M. sexta serpin-1 variants, serpin-3, -4, -5, and -6 form stable proteinase-inhibitor complexes with one or more of the pathway components. Since molecular probes (e.g., cDNAs and antisera for HPs and serpins) are available, we are attempting to elucidate the prophenoloxidase-activating pathway, its relationships with other proteinase-mediated immune responses, and inhibitory regulation by serpins.
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INSECT BIOCHEMISTRY AND MOLECULAR BIOLOGY (2024)
Insect biochemistry and molecular biology (2024): 104048-104048
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