Identification of a Conserved Prophenoloxidase Activation Pathway in Cotton Bollworm Helicoverpa armigera
Autor: | Qianran Wang, Mengyi Yin, Chuanfei Yuan, Xijia Liu, Zhihong Hu, Zhen Zou, Manli Wang |
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Jazyk: | angličtina |
Rok vydání: | 2020 |
Předmět: |
lcsh:Immunologic diseases. Allergy
0301 basic medicine Proteases medicine.medical_treatment serine protease Immunology melanization Helicoverpa armigera Transfection law.invention Cell Line 03 medical and health sciences 0302 clinical medicine baculovirus law Manduca medicine Immunology and Allergy Animals Original Research Serine protease Enzyme Precursors Protease biology Chemistry prophenoloxidase fungi Prophenoloxidase biology.organism_classification In vitro DNA Virus Infections Nucleopolyhedroviruses Recombinant Proteins Cell biology Enzyme Activation Lepidoptera 030104 developmental biology Manduca sexta Factor Xa biology.protein Recombinant DNA Insect Proteins Drosophila lcsh:RC581-607 Catechol Oxidase 030215 immunology Signal Transduction |
Zdroj: | Frontiers in Immunology Frontiers in Immunology, Vol 11 (2020) |
ISSN: | 1664-3224 |
Popis: | Melanization is a prominent insect humoral response for encapsulation of and killing invading pathogens. It is mediated by a protease cascade composed of a modular serine protease (SP), and clip domain SPs (cSPs), which converts prophenoloxidase (PPO) into active phenoloxidase (PO). To date, melanization pathway in cotton bollworm Helicoverpa armigera, an important agricultural pest, remains largely unclear. To biochemically reconstitute the pathway in vitro, the putative proteases along with modified proteases containing the factor Xa cleavage site were expressed by Drosophila S2 cell expression system. Purified recombinant proteins were used to examine their role in activating PPO. It is revealed that cascade is initiated by a modular SP-SP41, followed by cSP1 and cSP6. The three-step SP41/cSP1/cSP6 cascade could further activate PPO, and the PO activity was significantly enhanced in the presence of two cSP homologs (cSPHs), cSPH11 and cSPH50, suggesting the latter are cofactors for PPO activation. Moreover, baculovirus infection was efficiently blocked by the reconstituted PPO activation cascade, and the effect was boosted by cSPH11 and cSPH50. Taken together, we unraveled a conserved PPO activation cascade in H. armigera, which is similar to that exists in lepidopteran biochemical model Manduca sexta and highlighted its role in antagonizing viral infection. |
Databáze: | OpenAIRE |
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