Oligomer assembly of Bacillus thuringiensis Cyt2Aa2 on lipid membranes reveals a thread-like structure
Bacillus thuringiensis, a well-known insecticidal bacterium, produces several insecticidal proteins, including cytolytic (Cyt) proteins. Cyt proteins bind directly to the lipid membrane and form large protein complexes. In addition to the protein ladder bands, information on the oligomeric structure...
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Elsevier
2025-06-01
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| Online Access: | http://www.sciencedirect.com/science/article/pii/S2590171025000074 |
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| author | Chontida Tangsongcharoen Jose L. Toca-Herrera Boonhiang Promdonkoy Kanokporn Srisucharitpanit Sudarat Tharad |
| author_facet | Chontida Tangsongcharoen Jose L. Toca-Herrera Boonhiang Promdonkoy Kanokporn Srisucharitpanit Sudarat Tharad |
| author_sort | Chontida Tangsongcharoen |
| collection | DOAJ |
| description | Bacillus thuringiensis, a well-known insecticidal bacterium, produces several insecticidal proteins, including cytolytic (Cyt) proteins. Cyt proteins bind directly to the lipid membrane and form large protein complexes. In addition to the protein ladder bands, information on the oligomeric structure in lipid membranes is necessary to understand the mechanism of Cyt proteins on target cells. In this work, we have investigated the oligomeric Cyt2Aa2 complex with synthetic lipid and with erythrocyte membranes. When the activated Cyt2Aa2 protein was incubated with these lipid membranes, the protein ladder pattern relevant to hemolytic activity was detected in SDS-PAGE. Moreover, AFM topographic images revealed a fusilli-like structure and a ring-like structure for synthetic POPC and POPC/Chol, respectively. Furthermore, TEM micrographs provided an additional information on the oligomeric structure of Cyt2Aa2 in erythrocytes. Cyt2Aa2 appears to oligomerise/aggregate into mixed structures between the filamentous structure and small protein complexes in erythrocytes. In addition, a nanopore was found to be a substructure of the filamentous structure. These results strengthen the understanding of Cyt2Aa2 behavior in these two membrane systems, the fusilli and ring-like structures, depending on the type of lipid membrane. Furthermore, the structure of Cyt2Aa2 in insect target membranes remains to be investigated. |
| format | Article |
| id | doaj-art-8ea88f30bcde44368523c5ed32346342 |
| institution | OA Journals |
| issn | 2590-1710 |
| language | English |
| publishDate | 2025-06-01 |
| publisher | Elsevier |
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| spelling | doaj-art-8ea88f30bcde44368523c5ed323463422025-08-20T02:05:07ZengElsevierToxicon: X2590-17102025-06-012610022010.1016/j.toxcx.2025.100220Oligomer assembly of Bacillus thuringiensis Cyt2Aa2 on lipid membranes reveals a thread-like structureChontida Tangsongcharoen0Jose L. Toca-Herrera1Boonhiang Promdonkoy2Kanokporn Srisucharitpanit3Sudarat Tharad4Faculty of Allied Health Sciences, Burapha University, Chonburi, 20131, ThailandInstitut für Biophysik, Department für Bionanowissenschaften, Universität für Bodenkultur Wien (BOKU), Vienna, 1190, AustriaNational Center for Genetic Engineering and Biotechnology, National Science and Technology, Development Agency, Pathumthani, 12120, ThailandFaculty of Allied Health Sciences, Burapha University, Chonburi, 20131, ThailandDepartment of Biology, Faculty of Science, Burapha University, Chonburi, 20131, Thailand; Corresponding author.Bacillus thuringiensis, a well-known insecticidal bacterium, produces several insecticidal proteins, including cytolytic (Cyt) proteins. Cyt proteins bind directly to the lipid membrane and form large protein complexes. In addition to the protein ladder bands, information on the oligomeric structure in lipid membranes is necessary to understand the mechanism of Cyt proteins on target cells. In this work, we have investigated the oligomeric Cyt2Aa2 complex with synthetic lipid and with erythrocyte membranes. When the activated Cyt2Aa2 protein was incubated with these lipid membranes, the protein ladder pattern relevant to hemolytic activity was detected in SDS-PAGE. Moreover, AFM topographic images revealed a fusilli-like structure and a ring-like structure for synthetic POPC and POPC/Chol, respectively. Furthermore, TEM micrographs provided an additional information on the oligomeric structure of Cyt2Aa2 in erythrocytes. Cyt2Aa2 appears to oligomerise/aggregate into mixed structures between the filamentous structure and small protein complexes in erythrocytes. In addition, a nanopore was found to be a substructure of the filamentous structure. These results strengthen the understanding of Cyt2Aa2 behavior in these two membrane systems, the fusilli and ring-like structures, depending on the type of lipid membrane. Furthermore, the structure of Cyt2Aa2 in insect target membranes remains to be investigated.http://www.sciencedirect.com/science/article/pii/S2590171025000074Bacillus thuringiensisCytolytic proteinCyt2Aa2 proteinOligomer assemblyFusilli-like structureThread-like filament structure |
| spellingShingle | Chontida Tangsongcharoen Jose L. Toca-Herrera Boonhiang Promdonkoy Kanokporn Srisucharitpanit Sudarat Tharad Oligomer assembly of Bacillus thuringiensis Cyt2Aa2 on lipid membranes reveals a thread-like structure Toxicon: X Bacillus thuringiensis Cytolytic protein Cyt2Aa2 protein Oligomer assembly Fusilli-like structure Thread-like filament structure |
| title | Oligomer assembly of Bacillus thuringiensis Cyt2Aa2 on lipid membranes reveals a thread-like structure |
| title_full | Oligomer assembly of Bacillus thuringiensis Cyt2Aa2 on lipid membranes reveals a thread-like structure |
| title_fullStr | Oligomer assembly of Bacillus thuringiensis Cyt2Aa2 on lipid membranes reveals a thread-like structure |
| title_full_unstemmed | Oligomer assembly of Bacillus thuringiensis Cyt2Aa2 on lipid membranes reveals a thread-like structure |
| title_short | Oligomer assembly of Bacillus thuringiensis Cyt2Aa2 on lipid membranes reveals a thread-like structure |
| title_sort | oligomer assembly of bacillus thuringiensis cyt2aa2 on lipid membranes reveals a thread like structure |
| topic | Bacillus thuringiensis Cytolytic protein Cyt2Aa2 protein Oligomer assembly Fusilli-like structure Thread-like filament structure |
| url | http://www.sciencedirect.com/science/article/pii/S2590171025000074 |
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