Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.

The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major corn pest of significant economic importance in the United States. The continuous need to control this corn maize pest and the development of field-evolved resistance toward all existing transgenic maize (Zea mays L....

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Autores principales:	Jean-Louis Kouadio, Stephen Duff, Michael Aikins, Meiying Zheng, Timothy Rydel, Danqi Chen, Eric Bretsnyder, Chunsheng Xia, Jun Zhang, Jason Milligan, Artem Evdokimov, Jeffrey Nageotte, Yong Yin, William Moar, Kara Giddings, Yoonseong Park, Agoston Jerga, Jeffrey Haas
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/3f6fb312ef194d51b07483aa8e45f3c1
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spelling	oai:doaj.org-article:3f6fb312ef194d51b07483aa8e45f3c12021-12-02T20:17:05ZStructural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.1932-620310.1371/journal.pone.0258052https://doaj.org/article/3f6fb312ef194d51b07483aa8e45f3c12021-01-01T00:00:00Zhttps://doi.org/10.1371/journal.pone.0258052https://doaj.org/toc/1932-6203The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major corn pest of significant economic importance in the United States. The continuous need to control this corn maize pest and the development of field-evolved resistance toward all existing transgenic maize (Zea mays L.) expressing Bacillus thuringiensis (Bt) insecticidal proteins against WCR has prompted the development of new insect-protected crops expressing distinct structural classes of insecticidal proteins. In this current study, we describe the crystal structure and functional characterization of Mpp75Aa1.1, which represents the first corn rootworm (CRW) active insecticidal protein member of the ETX_MTX2 sub-family of beta-pore forming proteins (β-PFPs), and provides new and effective protection against WCR feeding. The Mpp75Aa1.1 crystal structure was solved at 1.94 Å resolution. The Mpp75Aa1.1 is processed at its carboxyl-terminus by WCR midgut proteases, forms an oligomer, and specifically interacts with putative membrane-associated binding partners on the midgut apical microvilli to cause cellular tissue damage resulting in insect death. Alanine substitution of the surface-exposed amino acids W206, Y212, and G217 within the Mpp75Aa1.1 putative receptor binding domain I demonstrates that at least these three amino acids are required for WCR activity. The distinctive spatial arrangement of these amino acids suggests that they are part of a receptor binding epitope, which may be unique to Mpp75Aa1.1 and not present in other ETX_MTX2 proteins that do not have WCR activity. Overall, this work establishes that Mpp75Aa1.1 shares a mode of action consistent with traditional WCR-active Bt proteins despite significant structural differences.Jean-Louis KouadioStephen DuffMichael AikinsMeiying ZhengTimothy RydelDanqi ChenEric BretsnyderChunsheng XiaJun ZhangJason MilliganArtem EvdokimovJeffrey NageotteYong YinWilliam MoarKara GiddingsYoonseong ParkAgoston JergaJeffrey HaasPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 16, Iss 10, p e0258052 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Jean-Louis Kouadio Stephen Duff Michael Aikins Meiying Zheng Timothy Rydel Danqi Chen Eric Bretsnyder Chunsheng Xia Jun Zhang Jason Milligan Artem Evdokimov Jeffrey Nageotte Yong Yin William Moar Kara Giddings Yoonseong Park Agoston Jerga Jeffrey Haas Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.
description	The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major corn pest of significant economic importance in the United States. The continuous need to control this corn maize pest and the development of field-evolved resistance toward all existing transgenic maize (Zea mays L.) expressing Bacillus thuringiensis (Bt) insecticidal proteins against WCR has prompted the development of new insect-protected crops expressing distinct structural classes of insecticidal proteins. In this current study, we describe the crystal structure and functional characterization of Mpp75Aa1.1, which represents the first corn rootworm (CRW) active insecticidal protein member of the ETX_MTX2 sub-family of beta-pore forming proteins (β-PFPs), and provides new and effective protection against WCR feeding. The Mpp75Aa1.1 crystal structure was solved at 1.94 Å resolution. The Mpp75Aa1.1 is processed at its carboxyl-terminus by WCR midgut proteases, forms an oligomer, and specifically interacts with putative membrane-associated binding partners on the midgut apical microvilli to cause cellular tissue damage resulting in insect death. Alanine substitution of the surface-exposed amino acids W206, Y212, and G217 within the Mpp75Aa1.1 putative receptor binding domain I demonstrates that at least these three amino acids are required for WCR activity. The distinctive spatial arrangement of these amino acids suggests that they are part of a receptor binding epitope, which may be unique to Mpp75Aa1.1 and not present in other ETX_MTX2 proteins that do not have WCR activity. Overall, this work establishes that Mpp75Aa1.1 shares a mode of action consistent with traditional WCR-active Bt proteins despite significant structural differences.
format	article
author	Jean-Louis Kouadio Stephen Duff Michael Aikins Meiying Zheng Timothy Rydel Danqi Chen Eric Bretsnyder Chunsheng Xia Jun Zhang Jason Milligan Artem Evdokimov Jeffrey Nageotte Yong Yin William Moar Kara Giddings Yoonseong Park Agoston Jerga Jeffrey Haas
author_facet	Jean-Louis Kouadio Stephen Duff Michael Aikins Meiying Zheng Timothy Rydel Danqi Chen Eric Bretsnyder Chunsheng Xia Jun Zhang Jason Milligan Artem Evdokimov Jeffrey Nageotte Yong Yin William Moar Kara Giddings Yoonseong Park Agoston Jerga Jeffrey Haas
author_sort	Jean-Louis Kouadio
title	Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.
title_short	Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.
title_full	Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.
title_fullStr	Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.
title_full_unstemmed	Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.
title_sort	structural and functional characterization of mpp75aa1.1, a putative beta-pore forming protein from brevibacillus laterosporus active against the western corn rootworm.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/3f6fb312ef194d51b07483aa8e45f3c1
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Structural and functional characterization of Mpp75Aa1.1, a putative beta-pore forming protein from Brevibacillus laterosporus active against the western corn rootworm.

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