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Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3
Melanization reaction, resulting from the activation of prophenoloxidase, is a vital immune response in insects for encapsulating and killing the invasive organisms. Prophenoloxidase needs to be proteolytically activated by its upstream prophenoloxidase-activating protease (PAP) in melanization. Ide...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2017
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5372168/ https://www.ncbi.nlm.nih.gov/pubmed/28358031 http://dx.doi.org/10.1038/srep45256 |
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author | Chu, Yuan Hong, Fang Liu, Qizhi An, Chunju |
author_facet | Chu, Yuan Hong, Fang Liu, Qizhi An, Chunju |
author_sort | Chu, Yuan |
collection | PubMed |
description | Melanization reaction, resulting from the activation of prophenoloxidase, is a vital immune response in insects for encapsulating and killing the invasive organisms. Prophenoloxidase needs to be proteolytically activated by its upstream prophenoloxidase-activating protease (PAP) in melanization. Identification and characterization of PAPs facilitates the understanding of the molecular mechanisms involved in insect immunity. We here cloned a full-length cDNA for a serine protease, named as SP105, from Asian corn borer, Ostrinia furnacalis (Guenée). The open reading frame of SP105 encodes 424-amino acid residue protein with a 19-residue signal peptide. Sequence comparison indicates that SP105 is most similar to Manduca sexta PAP3, a defined prophenoloxidase-activating protease. qRT-PCR analysis showed that SP105 mRNA levels increased significantly after a bacterial injection. Recombinant SP105 directly cleaved and activated Asian corn borer prophenoloxidase and therefore acted as the prophenoloxidase-activating protease. Additionally, SP105 formed SDS-stable complexes with a serine protease inhibitor, serpin-3, and its activity in activating prophenoloxidase was efficiently inhibited by serpin-3. Our work thus illustrated a prophenoloxidase-activating protease and revealed its regulation by serpin-3. The results would allow further advances in the understanding of the melanization in Asian corn borer and other insects. |
format | Online Article Text |
id | pubmed-5372168 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-53721682017-03-31 Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3 Chu, Yuan Hong, Fang Liu, Qizhi An, Chunju Sci Rep Article Melanization reaction, resulting from the activation of prophenoloxidase, is a vital immune response in insects for encapsulating and killing the invasive organisms. Prophenoloxidase needs to be proteolytically activated by its upstream prophenoloxidase-activating protease (PAP) in melanization. Identification and characterization of PAPs facilitates the understanding of the molecular mechanisms involved in insect immunity. We here cloned a full-length cDNA for a serine protease, named as SP105, from Asian corn borer, Ostrinia furnacalis (Guenée). The open reading frame of SP105 encodes 424-amino acid residue protein with a 19-residue signal peptide. Sequence comparison indicates that SP105 is most similar to Manduca sexta PAP3, a defined prophenoloxidase-activating protease. qRT-PCR analysis showed that SP105 mRNA levels increased significantly after a bacterial injection. Recombinant SP105 directly cleaved and activated Asian corn borer prophenoloxidase and therefore acted as the prophenoloxidase-activating protease. Additionally, SP105 formed SDS-stable complexes with a serine protease inhibitor, serpin-3, and its activity in activating prophenoloxidase was efficiently inhibited by serpin-3. Our work thus illustrated a prophenoloxidase-activating protease and revealed its regulation by serpin-3. The results would allow further advances in the understanding of the melanization in Asian corn borer and other insects. Nature Publishing Group 2017-03-30 /pmc/articles/PMC5372168/ /pubmed/28358031 http://dx.doi.org/10.1038/srep45256 Text en Copyright © 2017, The Author(s) http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Chu, Yuan Hong, Fang Liu, Qizhi An, Chunju Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3 |
title | Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3 |
title_full | Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3 |
title_fullStr | Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3 |
title_full_unstemmed | Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3 |
title_short | Serine protease SP105 activates prophenoloxidase in Asian corn borer melanization, and is regulated by serpin-3 |
title_sort | serine protease sp105 activates prophenoloxidase in asian corn borer melanization, and is regulated by serpin-3 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5372168/ https://www.ncbi.nlm.nih.gov/pubmed/28358031 http://dx.doi.org/10.1038/srep45256 |
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