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Two specific membrane-bound aminopeptidase N isoforms from Aedes aegypti larvae serve as functional receptors for the Bacillus thuringiensis Cry4Ba toxin implicating counterpart specificity

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dc.contributor.authorAratee Aroonkesornen_US
dc.contributor.authorKusol Pootanakiten_US
dc.contributor.authorGerd Katzenmeieren_US
dc.contributor.authorChanan Angsuthanasombaten_US
dc.contributor.otherMahidol Universityen_US
dc.contributor.otherBiophysics Institute for Research and Development (BIRD)en_US
dc.date.accessioned2018-11-23T09:43:09Z
dc.date.available2018-11-23T09:43:09Z
dc.date.issued2015-05-08en_US
dc.description.abstract© 2015 Elsevier Inc. All rights reserved. The interaction between Bacillus thuringiensis Cry toxins and their receptors on midgut cells of susceptible insect larvae is the critical determinant in toxin specificity. Besides GPI-linked alkaline phosphatase in Aedes aegypti mosquito-larval midguts, membrane-bound aminopeptidase N (AaeAPN) is widely thought to serve as a Cry4Ba receptor. Here, two full-length AaeAPN isoforms, AaeAPN2778 and AaeAPN2783, predicted to be GPI-linked were cloned and successfully expressed in Spodoptera frugiperda (Sf9) cells as 112- and 107-kDa membrane-bound proteins, respectively. In the cytotoxicity assay, Sf9 cells expressing each of the two AaeAPN isoforms showed increased sensitivity to the Cry4Ba mosquito-active toxin. Double immunolocalization revealed specific binding of Cry4Ba to each individual AaeAPN expressed on the cell membrane surface. Sequence analysis and homology-based modeling placed these two AaeAPNs to the M1 aminopeptidase family as they showed similar four-domain structures, with the most conserved domain II being the catalytic component. Additionally, the most variable domain IV containing negatively charged surface patches observed only in dipteran APNs could be involved in insect specificity. Overall results demonstrated that these two membrane-bound APN isoforms were responsible for mediating Cry4Ba toxicity against AaeAPN-expressed Sf9 cells, suggesting their important role as functional receptors for the toxin counterpart in A. aegypti mosquito larvae.en_US
dc.identifier.citationBiochemical and Biophysical Research Communications. Vol.461, No.2 (2015), 300-306en_US
dc.identifier.doi10.1016/j.bbrc.2015.04.026en_US
dc.identifier.issn10902104en_US
dc.identifier.issn0006291Xen_US
dc.identifier.other2-s2.0-84937762462en_US
dc.identifier.urihttps://hdl.handle.net/20.500.14594/35457
dc.rightsMahidol Universityen_US
dc.rights.holderSCOPUSen_US
dc.source.urihttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84937762462&origin=inwarden_US
dc.subjectBiochemistry, Genetics and Molecular Biologyen_US
dc.titleTwo specific membrane-bound aminopeptidase N isoforms from Aedes aegypti larvae serve as functional receptors for the Bacillus thuringiensis Cry4Ba toxin implicating counterpart specificityen_US
dc.typeArticleen_US
dspace.entity.typePublication
mu.datasource.scopushttps://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84937762462&origin=inwarden_US
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