ArticleThe Biochemical journal2003
Recombinantly expressed isoenzymic aminopeptidases from Helicoverpa armigera (American cotton bollworm) midgut display differential interaction with closely related Bacillus thuringiensis insecticidal proteins.
Article in The Biochemical journal, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 71 citations in OpenAlex.
- Cry1Ac toxin binding in the velvetbean caterpillarFrontiers in physiology · 2024Article
- Midgut aminopeptidase N expression profile in castor semilooper (Journal of biosciences · 2021Article
- Analysis of Cry1Ah Toxin-Binding Reliability to Midgut Membrane Proteins of the Asian Corn Borer.Toxins · 2020Article
- Proteomic Mapping of Multifunctional Complexes Within Triatomine Saliva.Frontiers in cellular and infection microbiology · 2020Article
- Newly identified APN splice isoforms suggest novel splicing mechanisms may underlie circRNA circularization in moth.FEBS open bio · 2019Article
- Aminopeptidase N1 is involved in Bacillus thuringiensis Cry1Ac toxicity in the beet armyworm, Spodoptera exigua.Scientific reports · 2017Article
- Cry1Ac and Vip3Aa proteins fromPeerJ · 2017Article
- A P-Glycoprotein Is Linked to Resistance to the Bacillus thuringiensis Cry3Aa Toxin in a Leaf Beetle.Toxins · 2016Article
- Identification of ABCC2 as a binding protein of Cry1Ac on brush border membrane vesicles from Helicoverpa armigera by an improved pull-down assay.MicrobiologyOpen · 2016Article
- Expression of recombinant and mosaic Cry1Ac receptors from Helicoverpa armigera and their influences on the cytotoxicity of activated Cry1Ac to Spodoptera litura Sl-HP cells.Cytotechnology · 2016Article
- APN1 is a functional receptor of Cry1Ac but not Cry2Ab in Helicoverpa zea.Scientific reports · 2016Article
- Next Generation Sequencing Identifies Five Major Classes of Potentially Therapeutic Enzymes Secreted by Lucilia sericata Medical Maggots.BioMed research international · 2016Article
- Sugarcane giant borer transcriptome analysis and identification of genes related to digestion.PloS one · 2015Article
- Evolutionary diversification of aminopeptidase N in Lepidoptera by conserved clade-specific amino acid residues.Molecular phylogenetics and evolution · 2014Article
- A proteomic approach to study the mechanism of tolerance to Bt toxins in Ostrinia furnacalis larvae selected for resistance to Cry1Ab.Transgenic research · 2013Article
- Identification and characterization of Aedes aegypti aminopeptidase N as a putative receptor of Bacillus thuringiensis Cry11A toxin.Insect biochemistry and molecular biology · 2009Article
- Diversity of aminopeptidases, derived from four lepidopteran gene duplications, and polycalins expressed in the midgut of Helicoverpa armigera: identification of proteins binding the delta-endotoxin, Cry1Ac of Bacillus thuringiensis.Insect biochemistry and molecular biology · 2008Article
- A novel aminopeptidase in the fat body of the moth Achaea janata as a receptor for Bacillus thuringiensis Cry toxins and its comparison with midgut aminopeptidase.The Biochemical journal · 2007Article
- Role of receptors in Bacillus thuringiensis crystal toxin activity.Microbiology and molecular biology reviews : MMBR · 2007Review
- Characterization of a membrane-bound aminopeptidase purified from Acyrthosiphon pisum midgut cells. A major binding site for toxic mannose lectins.The FEBS journal · 2006Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Several investigators have independently identified membrane-associated aminopeptidases in the midgut of insect larvae as the initial interacting ligand to the insecticidal crystal proteins of Bacillus thuringiensis. Though several isoenzymes of aminopeptidases have been identified from the midgut of an insect and their corresponding cDNA cloned, only one of the isoform has been expressed heterologously and studied for its binding to Cry toxins. Here we report the cloning and expression of two aminopeptidases N from Helicoverpa armigera (American cotton bollworm) (HaAPNs). The full-length cDNA of H. armigera APN1 (haapn1) is 3205 bp in size and encodes a 1000-amino-acid protein, while H. armigera APN2 (haapn2) is 3116 bp in size and corresponds to a 1012-amino-acid protein. Structurally these proteins show sequence similarity to other insect aminopeptidases and possess characteristic aminopeptidase motifs. Both the genes have been expressed in Trichoplusia ni (cabbage looper) cells using a baculovirus expression vector. The expressed aminopeptidases are membrane-associated, catalytically active and glycosylated. Ligand-blot analysis of both these aminopeptidases with bioactive Cry1Aa, Cry1Ab and Cry1Ac proteins displayed differential interaction. All the three toxins bound to HaAPN1, whereas only Cry1Ac interacted with HaAPN2. This is the first report demonstrating differential Cry-toxin-binding abilities of two different aminopeptidases from a susceptible insect.
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