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Structural and functional insights into the first Bacillus thuringiensis vegetative insecticidal protein of the Vpb4 fold, active against western corn rootworm
The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major maize pest in the United States causing significant economic loss. The emergence of field-evolved resistant WCR to Bacillus thuringiensis (Bt) traits has prompted the need to discover and deploy new insecticidal prot...
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Published in: | PloS one 2021-12, Vol.16 (12), p.e0260532 |
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creator | Kouadio, Jean-Louis Zheng, Meiying Aikins, Michael Duda, David Duff, Stephen Chen, Danqi Zhang, Jun Milligan, Jason Taylor, Christina Mamanella, Patricia Rydel, Timothy Kessenich, Colton Panosian, Timothy Yin, Yong Moar, William Giddings, Kara Park, Yoonseong Jerga, Agoston Haas, Jeffrey |
description | The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major maize pest in the United States causing significant economic loss. The emergence of field-evolved resistant WCR to Bacillus thuringiensis (Bt) traits has prompted the need to discover and deploy new insecticidal proteins in transgenic maize. In the current study we determined the crystal structure and mode of action (MOA) of the Vpb4Da2 protein (formerly known as Vip4Da2) from Bt, the first identified insecticidal Vpb4 protein with commercial level control against WCR. The Vpb4Da2 structure exhibits a six-domain architecture mainly comprised of antiparallel β-sheets organized into β-sandwich layers. The amino-terminal domains 1-3 of the protein share structural homology with the protective antigen (PA) PA14 domain and encompass a long β-pore forming loop as in the clostridial binary-toxB module. Domains 5 and 6 at the carboxyl-terminal half of Vpb4Da2 are unique as this extension is not observed in PA or any other structurally-related protein other than Vpb4 homologs. These unique Vpb4 domains adopt the topologies of carbohydrate-binding modules known to participate in receptor-recognition. Functional assessment of Vpb4Da2 suggests that domains 4-6 comprise the WCR receptor binding region and are key in conferring the observed insecticidal activity against WCR. The current structural analysis was complemented by in vitro and in vivo characterizations, including immuno-histochemistry, demonstrating that Vpb4Da2 follows a MOA that is consistent with well-characterized 3-domain Bt insecticidal proteins despite significant structural differences. |
doi_str_mv | 10.1371/journal.pone.0260532 |
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(ANL), Argonne, IL (United States). Advanced Photon Source (APS) ; Bulla, Lee</creatorcontrib><description>The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major maize pest in the United States causing significant economic loss. The emergence of field-evolved resistant WCR to Bacillus thuringiensis (Bt) traits has prompted the need to discover and deploy new insecticidal proteins in transgenic maize. In the current study we determined the crystal structure and mode of action (MOA) of the Vpb4Da2 protein (formerly known as Vip4Da2) from Bt, the first identified insecticidal Vpb4 protein with commercial level control against WCR. The Vpb4Da2 structure exhibits a six-domain architecture mainly comprised of antiparallel β-sheets organized into β-sandwich layers. The amino-terminal domains 1-3 of the protein share structural homology with the protective antigen (PA) PA14 domain and encompass a long β-pore forming loop as in the clostridial binary-toxB module. Domains 5 and 6 at the carboxyl-terminal half of Vpb4Da2 are unique as this extension is not observed in PA or any other structurally-related protein other than Vpb4 homologs. These unique Vpb4 domains adopt the topologies of carbohydrate-binding modules known to participate in receptor-recognition. Functional assessment of Vpb4Da2 suggests that domains 4-6 comprise the WCR receptor binding region and are key in conferring the observed insecticidal activity against WCR. The current structural analysis was complemented by in vitro and in vivo characterizations, including immuno-histochemistry, demonstrating that Vpb4Da2 follows a MOA that is consistent with well-characterized 3-domain Bt insecticidal proteins despite significant structural differences.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0260532</identifier><identifier>PMID: 34928980</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino Acid Sequence ; Analysis ; Animals ; Antigens ; Bacillus thuringiensis ; Bacillus thuringiensis - metabolism ; Bacterial Proteins - chemistry ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; BASIC BIOLOGICAL SCIENCES ; Binding ; Biology and Life Sciences ; Carbohydrates ; Chromatography ; Coleoptera - drug effects ; Coleoptera - growth & development ; Corn ; Crop science ; Crystal structure ; Crystallography, X-Ray ; Diabrotica virgifera virgifera ; Economic impact ; Entomology ; Genetically modified crops ; Histochemistry ; Homology ; Insecticide resistance ; Insecticides - chemistry ; Insecticides - pharmacology ; Intestines - metabolism ; Larva - drug effects ; Larva - metabolism ; Management ; Mode of action ; Modules ; Molecular weight ; Mutagenesis, Site-Directed ; Physical Sciences ; Pore formation ; Protective antigen ; Protein folding ; Protein Multimerization ; Protein Structure, Tertiary ; Proteins ; Receptors ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - pharmacology ; Research and Analysis Methods ; Structural analysis ; Structure ; Structure-function relationships ; Topology ; Zea mays - metabolism ; Zea mays - parasitology</subject><ispartof>PloS one, 2021-12, Vol.16 (12), p.e0260532</ispartof><rights>COPYRIGHT 2021 Public Library of Science</rights><rights>2021 Kouadio et al. This is an open access article distributed under the terms of the Creative Commons Attribution License: http://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. 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(ANL), Argonne, IL (United States). Advanced Photon Source (APS)</creatorcontrib><title>Structural and functional insights into the first Bacillus thuringiensis vegetative insecticidal protein of the Vpb4 fold, active against western corn rootworm</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major maize pest in the United States causing significant economic loss. The emergence of field-evolved resistant WCR to Bacillus thuringiensis (Bt) traits has prompted the need to discover and deploy new insecticidal proteins in transgenic maize. In the current study we determined the crystal structure and mode of action (MOA) of the Vpb4Da2 protein (formerly known as Vip4Da2) from Bt, the first identified insecticidal Vpb4 protein with commercial level control against WCR. The Vpb4Da2 structure exhibits a six-domain architecture mainly comprised of antiparallel β-sheets organized into β-sandwich layers. The amino-terminal domains 1-3 of the protein share structural homology with the protective antigen (PA) PA14 domain and encompass a long β-pore forming loop as in the clostridial binary-toxB module. Domains 5 and 6 at the carboxyl-terminal half of Vpb4Da2 are unique as this extension is not observed in PA or any other structurally-related protein other than Vpb4 homologs. These unique Vpb4 domains adopt the topologies of carbohydrate-binding modules known to participate in receptor-recognition. Functional assessment of Vpb4Da2 suggests that domains 4-6 comprise the WCR receptor binding region and are key in conferring the observed insecticidal activity against WCR. The current structural analysis was complemented by in vitro and in vivo characterizations, including immuno-histochemistry, demonstrating that Vpb4Da2 follows a MOA that is consistent with well-characterized 3-domain Bt insecticidal proteins despite significant structural differences.</description><subject>Amino Acid Sequence</subject><subject>Analysis</subject><subject>Animals</subject><subject>Antigens</subject><subject>Bacillus thuringiensis</subject><subject>Bacillus thuringiensis - metabolism</subject><subject>Bacterial Proteins - chemistry</subject><subject>Bacterial Proteins - genetics</subject><subject>Bacterial Proteins - metabolism</subject><subject>BASIC BIOLOGICAL SCIENCES</subject><subject>Binding</subject><subject>Biology and Life Sciences</subject><subject>Carbohydrates</subject><subject>Chromatography</subject><subject>Coleoptera - drug effects</subject><subject>Coleoptera - growth & development</subject><subject>Corn</subject><subject>Crop science</subject><subject>Crystal structure</subject><subject>Crystallography, X-Ray</subject><subject>Diabrotica virgifera virgifera</subject><subject>Economic impact</subject><subject>Entomology</subject><subject>Genetically modified crops</subject><subject>Histochemistry</subject><subject>Homology</subject><subject>Insecticide resistance</subject><subject>Insecticides - chemistry</subject><subject>Insecticides - pharmacology</subject><subject>Intestines - metabolism</subject><subject>Larva - drug effects</subject><subject>Larva - metabolism</subject><subject>Management</subject><subject>Mode of action</subject><subject>Modules</subject><subject>Molecular weight</subject><subject>Mutagenesis, Site-Directed</subject><subject>Physical Sciences</subject><subject>Pore formation</subject><subject>Protective antigen</subject><subject>Protein folding</subject><subject>Protein Multimerization</subject><subject>Protein Structure, Tertiary</subject><subject>Proteins</subject><subject>Receptors</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - pharmacology</subject><subject>Research and Analysis Methods</subject><subject>Structural analysis</subject><subject>Structure</subject><subject>Structure-function relationships</subject><subject>Topology</subject><subject>Zea mays - 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(ANL), Argonne, IL (United States). 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Hybrid</collection><collection>OSTI.GOV</collection><collection>PubMed Central (Full Participant titles)</collection><collection>Directory of Open Access Journals</collection><jtitle>PloS one</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kouadio, Jean-Louis</au><au>Zheng, Meiying</au><au>Aikins, Michael</au><au>Duda, David</au><au>Duff, Stephen</au><au>Chen, Danqi</au><au>Zhang, Jun</au><au>Milligan, Jason</au><au>Taylor, Christina</au><au>Mamanella, Patricia</au><au>Rydel, Timothy</au><au>Kessenich, Colton</au><au>Panosian, Timothy</au><au>Yin, Yong</au><au>Moar, William</au><au>Giddings, Kara</au><au>Park, Yoonseong</au><au>Jerga, Agoston</au><au>Haas, Jeffrey</au><au>Bulla, Lee</au><aucorp>Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural and functional insights into the first Bacillus thuringiensis vegetative insecticidal protein of the Vpb4 fold, active against western corn rootworm</atitle><jtitle>PloS one</jtitle><addtitle>PLoS One</addtitle><date>2021-12-20</date><risdate>2021</risdate><volume>16</volume><issue>12</issue><spage>e0260532</spage><pages>e0260532-</pages><issn>1932-6203</issn><eissn>1932-6203</eissn><abstract>The western corn rootworm (WCR), Diabrotica virgifera virgifera LeConte, is a major maize pest in the United States causing significant economic loss. The emergence of field-evolved resistant WCR to Bacillus thuringiensis (Bt) traits has prompted the need to discover and deploy new insecticidal proteins in transgenic maize. In the current study we determined the crystal structure and mode of action (MOA) of the Vpb4Da2 protein (formerly known as Vip4Da2) from Bt, the first identified insecticidal Vpb4 protein with commercial level control against WCR. The Vpb4Da2 structure exhibits a six-domain architecture mainly comprised of antiparallel β-sheets organized into β-sandwich layers. The amino-terminal domains 1-3 of the protein share structural homology with the protective antigen (PA) PA14 domain and encompass a long β-pore forming loop as in the clostridial binary-toxB module. Domains 5 and 6 at the carboxyl-terminal half of Vpb4Da2 are unique as this extension is not observed in PA or any other structurally-related protein other than Vpb4 homologs. These unique Vpb4 domains adopt the topologies of carbohydrate-binding modules known to participate in receptor-recognition. Functional assessment of Vpb4Da2 suggests that domains 4-6 comprise the WCR receptor binding region and are key in conferring the observed insecticidal activity against WCR. The current structural analysis was complemented by in vitro and in vivo characterizations, including immuno-histochemistry, demonstrating that Vpb4Da2 follows a MOA that is consistent with well-characterized 3-domain Bt insecticidal proteins despite significant structural differences.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>34928980</pmid><doi>10.1371/journal.pone.0260532</doi><tpages>e0260532</tpages><orcidid>https://orcid.org/0000-0001-8407-6050</orcidid><orcidid>https://orcid.org/0000-0002-8001-8491</orcidid><orcidid>https://orcid.org/0000-0002-6428-3519</orcidid><orcidid>https://orcid.org/0000-0003-4381-1017</orcidid><orcidid>https://orcid.org/0000-0002-8943-319X</orcidid><orcidid>https://orcid.org/0000000184076050</orcidid><orcidid>https://orcid.org/0000000264283519</orcidid><orcidid>https://orcid.org/0000000280018491</orcidid><orcidid>https://orcid.org/000000028943319X</orcidid><orcidid>https://orcid.org/0000000343811017</orcidid><oa>free_for_read</oa></addata></record> |
fulltext | fulltext |
identifier | ISSN: 1932-6203 |
ispartof | PloS one, 2021-12, Vol.16 (12), p.e0260532 |
issn | 1932-6203 1932-6203 |
language | eng |
recordid | cdi_plos_journals_2612009230 |
source | PubMed Central (Open Access); Publicly Available Content Database |
subjects | Amino Acid Sequence Analysis Animals Antigens Bacillus thuringiensis Bacillus thuringiensis - metabolism Bacterial Proteins - chemistry Bacterial Proteins - genetics Bacterial Proteins - metabolism BASIC BIOLOGICAL SCIENCES Binding Biology and Life Sciences Carbohydrates Chromatography Coleoptera - drug effects Coleoptera - growth & development Corn Crop science Crystal structure Crystallography, X-Ray Diabrotica virgifera virgifera Economic impact Entomology Genetically modified crops Histochemistry Homology Insecticide resistance Insecticides - chemistry Insecticides - pharmacology Intestines - metabolism Larva - drug effects Larva - metabolism Management Mode of action Modules Molecular weight Mutagenesis, Site-Directed Physical Sciences Pore formation Protective antigen Protein folding Protein Multimerization Protein Structure, Tertiary Proteins Receptors Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification Recombinant Proteins - pharmacology Research and Analysis Methods Structural analysis Structure Structure-function relationships Topology Zea mays - metabolism Zea mays - parasitology |
title | Structural and functional insights into the first Bacillus thuringiensis vegetative insecticidal protein of the Vpb4 fold, active against western corn rootworm |
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