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

An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Two specific membrane-bound aminopeptidase N isoforms from Aedes aegypti larvae serve as functional receptors for the Bacillus thuringiensis Cry4Ba toxin implicating counterpart specificity
Creator	Angsuthanasombat, Chanan Aroonkesorn, Aratee Katzenmeier, Gerd Pootanakit, Kusol
Source	Elsevier; Medline; PMC
abstract	Abstract 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.
has issue date	2015-05-29(xsd:dateTime)
bibo:doi	10.1016/j.bbrc.2015.04.026
bibo:pmid	25871797
has license	els-covid
sha1sum (hex)	abf7357ff5204fc96ea4a9d5a7447ce3456ff16e
schema:url	https://doi.org/10.1016/j.bbrc.2015.04.026
resource representing a document's title	Two specific membrane-bound aminopeptidase N isoforms from Aedes aegypti larvae serve as functional receptors for the Bacillus thuringiensis Cry4Ba toxin implicating counterpart specificity
has PubMed Central identifier	PMC7124302
has PubMed identifier	25871797
schema:publication	Biochemical and Biophysical Research Communications
resource representing a document's body	covid:abf7357ff5204fc96ea4a9d5a7447ce3456ff16e#body_text
is schema:about of	named entity 'cells' named entity 'A. aegypti' named entity 'membrane-bound proteins' named entity 'AMINOPEPTIDASE N' named entity 'MEMBRANE' named entity 'COMPONENT' named entity 'BINDING' named entity 'MODELING' named entity 'BACILLUS THURINGIENSIS' named entity 'IMPORTANT' named entity 'CONTAINING' named entity 'EXPRESSED' named entity 'GPI' named entity 'TOXINS' named entity 'INSECT' named entity 'INVOLVED' named entity 'LARVAL' named entity 'DOMAIN' named entity 'THESE' named entity 'SPECIFIC' named entity '107' named entity 'ROLE' named entity 'COULD BE' named entity 'AMINOPEPTIDASE' covid:arg/abf7357ff5204fc96ea4a9d5a7447ce3456ff16e named entity 'BOUND' named entity 'SERVE' named entity 'PLACED' named entity 'VARIABLE' named entity 'FUNCTIONAL' named entity 'AMINOPEPTIDASE N' named entity 'RECEPTORS' named entity 'LARVAE' named entity 'ISOFORMS' named entity 'SPECIFIC' named entity 'FUNCTIONAL' named entity 'TOXIN' named entity 'CELLS' named entity 'STRUCTURES' named entity 'FAMILY' named entity 'INDIVIDUAL' named entity 'SPODOPTERA FRUGIPERDA' named entity 'CRITICAL' named entity 'INCREASED SENSITIVITY' named entity 'AEDES AEGYPTI' named entity 'CYTOTOXICITY ASSAY' named entity 'RESPONSIBLE' named entity 'SF9 CELLS' named entity 'NEGATIVELY CHARGED' named entity 'AEDES AEGYPTI' named entity 'MEMBRANE' named entity 'IMMUNOLOCALIZATION' named entity 'RECEPTORS' named entity 'CELL MEMBRANE' named entity 'DOUBLE' named entity 'TOXICITY' named entity 'PROTEINS' named entity 'MIDGUT' named entity 'REVEALED' named entity 'CRY' named entity 'BACILLUS THURINGIENSIS' named entity 'SPECIFICITY' named entity 'KDA' named entity 'LENGTH' named entity 'PREDICTED' named entity 'SIMILAR' named entity 'MEDIATING' named entity 'ALKALINE PHOSPHATASE ' named entity 'CONSERVED' named entity 'DETERMINANT' named entity 'THOUGHT' named entity 'ACTIVE' named entity 'RESULTS' named entity 'SEQUENCE ANALYSIS' named entity 'RECEPTOR' named entity 'ISOFORMS' named entity 'CLONED' named entity 'APN'

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