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 |