Please use this identifier to cite or link to this item: https://hdl.handle.net/10356/80455
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dc.contributor.authorSurya, Wahyuen
dc.contributor.authorChooduang, Sivadatchen
dc.contributor.authorChoong, Yeu Khaien
dc.contributor.authorTorres, Jaumeen
dc.contributor.authorBoonserm, Panaddaen
dc.contributor.editorJurat-Fuentes, Juan Luisen
dc.date.accessioned2018-11-02T02:40:31Zen
dc.date.accessioned2019-12-06T13:49:52Z-
dc.date.available2018-11-02T02:40:31Zen
dc.date.available2019-12-06T13:49:52Z-
dc.date.issued2016en
dc.identifier.citationSurya, W., Chooduang, S., Choong, Y. K., Torres, J., & Boonserm, P. (2016). Binary toxin subunits of Lysinibacillus sphaericus are monomeric and form heterodimers after in vitro activation. PLOS ONE, 11(6), e0158356-. doi:10.1371/journal.pone.0158356en
dc.identifier.urihttps://hdl.handle.net/10356/80455-
dc.description.abstractThe binary toxin from Lysinibacillus sphaericus has been successfully used for controlling mosquito-transmitted diseases. An activation step shortens both subunits BinA and BinB before their interaction with membranes and internalization in midgut cells, but the precise role of this activation step is unknown. Herein, we show conclusively using three orthogonal biophysical techniques that protoxin subunits form only monomers in aqueous solution. However, in vitro activated toxins readily form heterodimers. This oligomeric state did not change after incubation of these heterodimers with detergent. These results are consistent with the evidence that maximal toxicity in mosquito larvae is achieved when the two subunits, BinA and BinB, are in a 1:1 molar ratio, and directly link proteolytic activation to heterodimerization. Formation of a heterodimer must thus be necessary for subsequent steps, e.g., interaction with membranes, or with a suitable receptor in susceptible mosquito species. Lastly, despite existing similarities between BinB C-terminal domain with domains 3 and 4 of pore-forming aerolysin, no aerolysin-like SDS-resistant heptameric oligomers were observed when the activated Bin subunits were incubated in the presence of detergents or lipidic membranes.en
dc.description.sponsorshipMOE (Min. of Education, S’pore)en
dc.format.extent14 p.en
dc.language.isoenen
dc.relation.ispartofseriesPLOS ONEen
dc.rights© 2016 Surya et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subjectLysinibacillus Sphaericusen
dc.subjectBinary Toxinen
dc.subjectDRNTU::Science::Biological sciencesen
dc.titleBinary toxin subunits of Lysinibacillus sphaericus are monomeric and form heterodimers after in vitro activationen
dc.typeJournal Articleen
dc.contributor.schoolSchool of Biological Sciencesen
dc.identifier.doi10.1371/journal.pone.0158356en
dc.description.versionPublished versionen
dc.identifier.pmid27341696-
item.fulltextWith Fulltext-
item.grantfulltextopen-
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