3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity

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dc.contributor.author Landsberg, MJ en
dc.contributor.author Jones, SA en
dc.contributor.author Rothnagel, R en
dc.contributor.author Busby, Jason en
dc.contributor.author Marshall, SDG en
dc.contributor.author Simpson, RM en
dc.contributor.author Lott, Jeremy en
dc.contributor.author Hankamer, B en
dc.contributor.author Hurst, MRH en
dc.contributor.editor Bjorkman, PJ en
dc.date.accessioned 2012-03-01T23:23:12Z en
dc.date.issued 2011 en
dc.identifier.citation Proceedings of the National Academy of Sciences of USA 108(51):20544-20549 2011 en
dc.identifier.issn 0027-8424 en
dc.identifier.uri http://hdl.handle.net/2292/12567 en
dc.description.abstract Toxin complex (Tc) proteins are a class of bacterial protein toxins that form large, multisubunit complexes. Comprising TcA, B, and C components, they are of great interest because many exhibit potent insecticidal activity. Here we report the structure of a novel Tc, Yen-Tc, isolated from the bacterium Yersinia entomophaga MH96, which differs from the majority of bacterially derived Tcs in that it exhibits oral activity toward a broad range of insect pests, including the diamondback moth (Plutella xylostella). We have determined the structure of the Yen-Tc using single particle electron microscopy and studied its mechanism of toxicity by comparative analyses of two variants of the complex exhibiting different toxicity profiles. We show that the A subunits form the basis of a fivefold symmetric assembly that differs substantially in structure and subunit arrangement from its most well characterized homologue, the Xenorhabdus nematophila toxin XptA1. Histopathological and quantitative dose response analyses identify the B and C subunits, which map to a single, surface-accessible region of the structure, as the sole determinants of toxicity. Finally, we show that the assembled Yen-Tc has endochitinase activity and attribute this to putative chitinase subunits that decorate the surface of the TcA scaffold, an observation that may explain the oral toxicity associated with the complex. en
dc.publisher The National Academy of Sciences of the USA en
dc.relation.ispartofseries Proceedings of the National Academy of Sciences of the United States of America en
dc.rights Items in ResearchSpace are protected by copyright, with all rights reserved, unless otherwise indicated. Previously published items are made available in accordance with the copyright policy of the publisher. Details obtained from http://www.sherpa.ac.uk/romeo/issn/1091-6490/ en
dc.rights.uri https://researchspace.auckland.ac.nz/docs/uoa-docs/rights.htm en
dc.title 3D structure of the Yersinia entomophaga toxin complex and implications for insecticidal activity en
dc.type Journal Article en
dc.identifier.doi 10.1073/pnas.1111155108 en
pubs.issue 51 en
pubs.begin-page 20544 en
pubs.volume 108 en
dc.rights.holder Copyright: The National Academy of Sciences of the USA en
dc.identifier.pmid 22158901 en
pubs.end-page 20549 en
dc.rights.accessrights http://purl.org/eprint/accessRights/RestrictedAccess en
pubs.subtype Article en
pubs.elements-id 257753 en
pubs.org-id Science en
pubs.org-id Biological Sciences en
pubs.org-id Science Research en
pubs.org-id Maurice Wilkins Centre (2010-2014) en
pubs.record-created-at-source-date 2011-12-08 en
pubs.dimensions-id 22158901 en

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