A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond

A diverse family of metalloproteases (MPs) is distributed in eukaryotes. However, the functions of MPs are still understudied. We report that seven MPs belonging to the M35 family are encoded in the genome of the insect pathogenic fungus Metarhizium robertsii. By gene deletions and insect bioassays,...

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Autores principales:	Antian Huang, Mengting Lu, Erjun Ling, Ping Li, Chengshu Wang
Formato:	article
Lenguaje:	EN
Publicado:	Taylor & Francis Group 2020
Materias:	metarhizium metalloprotease melanization immune suppression virulence Infectious and parasitic diseases RC109-216
Acceso en línea:	https://doaj.org/article/871c927f28fd40fe90d4e688bf80b7d1
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spelling	oai:doaj.org-article:871c927f28fd40fe90d4e688bf80b7d12021-11-17T14:21:58ZA M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond2150-55942150-560810.1080/21505594.2020.1731126https://doaj.org/article/871c927f28fd40fe90d4e688bf80b7d12020-12-01T00:00:00Zhttp://dx.doi.org/10.1080/21505594.2020.1731126https://doaj.org/toc/2150-5594https://doaj.org/toc/2150-5608A diverse family of metalloproteases (MPs) is distributed in eukaryotes. However, the functions of MPs are still understudied. We report that seven MPs belonging to the M35 family are encoded in the genome of the insect pathogenic fungus Metarhizium robertsii. By gene deletions and insect bioassays, we found that one of the M35-family MPs, i.e. MrM35-4, is required for fungal virulence against insect hosts. MrM35-4 is a secretable enzyme and shows a proteolytic activity implicated in facilitating fungal penetration of insect cuticles. After gene rescue and overexpression, insect bioassays indicated that MrM35-4 contributes to inhibiting insect cuticular and hemocyte melanization activities. Enzymatic cleavage assays revealed that the recombinant prophenoloxidases PPO1 and PPO2 of Drosophila melanogaster could be clipped by MrM35-4 in a manner differing from a serine protease that can activate PPO activities. In addition, it was found that MrM35-4 is involved in suppressing antifungal gene expression in insects. Consistent with the evident apoptogenic effect of MrM35-4 on host cells, we found that the PPO mutant flies differentially succumbed to the infections of the wild-type and mutant strains of M. robertsii. Thus, MrM35-4 plays a multifaceted role beyond targeting PPOs during fungus-insect interactions, which represents a previously unsuspected strategy employed by Metarhizium to outmaneuver insect immune defenses.Antian HuangMengting LuErjun LingPing LiChengshu WangTaylor & Francis Grouparticlemetarhiziummetalloproteasemelanizationimmune suppressionvirulenceInfectious and parasitic diseasesRC109-216ENVirulence, Vol 11, Iss 1, Pp 222-237 (2020)
institution	DOAJ
collection	DOAJ
language	EN
topic	metarhizium metalloprotease melanization immune suppression virulence Infectious and parasitic diseases RC109-216
spellingShingle	metarhizium metalloprotease melanization immune suppression virulence Infectious and parasitic diseases RC109-216 Antian Huang Mengting Lu Erjun Ling Ping Li Chengshu Wang A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond
description	A diverse family of metalloproteases (MPs) is distributed in eukaryotes. However, the functions of MPs are still understudied. We report that seven MPs belonging to the M35 family are encoded in the genome of the insect pathogenic fungus Metarhizium robertsii. By gene deletions and insect bioassays, we found that one of the M35-family MPs, i.e. MrM35-4, is required for fungal virulence against insect hosts. MrM35-4 is a secretable enzyme and shows a proteolytic activity implicated in facilitating fungal penetration of insect cuticles. After gene rescue and overexpression, insect bioassays indicated that MrM35-4 contributes to inhibiting insect cuticular and hemocyte melanization activities. Enzymatic cleavage assays revealed that the recombinant prophenoloxidases PPO1 and PPO2 of Drosophila melanogaster could be clipped by MrM35-4 in a manner differing from a serine protease that can activate PPO activities. In addition, it was found that MrM35-4 is involved in suppressing antifungal gene expression in insects. Consistent with the evident apoptogenic effect of MrM35-4 on host cells, we found that the PPO mutant flies differentially succumbed to the infections of the wild-type and mutant strains of M. robertsii. Thus, MrM35-4 plays a multifaceted role beyond targeting PPOs during fungus-insect interactions, which represents a previously unsuspected strategy employed by Metarhizium to outmaneuver insect immune defenses.
format	article
author	Antian Huang Mengting Lu Erjun Ling Ping Li Chengshu Wang
author_facet	Antian Huang Mengting Lu Erjun Ling Ping Li Chengshu Wang
author_sort	Antian Huang
title	A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond
title_short	A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond
title_full	A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond
title_fullStr	A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond
title_full_unstemmed	A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond
title_sort	m35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond
publisher	Taylor & Francis Group
publishDate	2020
url	https://doaj.org/article/871c927f28fd40fe90d4e688bf80b7d1
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A M35 family metalloprotease is required for fungal virulence against insects by inactivating host prophenoloxidases and beyond

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