Midgut aminopeptidase N expression profile in castor semilooper (Achaea janata) during sublethal Cry toxin exposure

2021 ◽  
Vol 46 (1) ◽  
Author(s):  
Vinod K. Chauhan ◽  
Narender K. Dhania ◽  
Vadthya Lokya ◽  
Bhoopal Bhuvanachandra ◽  
Kollipara Padmasree ◽  
...  
Keyword(s):  
Expression Profile ◽  
Aminopeptidase N ◽  
Cry Toxin ◽  
Toxin Exposure ◽  
Achaea Janata ◽  
Castor Semilooper

scholarly journals Midgut aminopeptidase N expression profile in Castor semilooper during sublethal Cry toxin exposure

2019 ◽  
Author(s):  
Vinod K. Chauhan ◽  
Narender K. Dhania ◽  
Vadthya Lokya ◽  
Bhoopal Bhuvanachandra ◽  
Kollipara Padmasree ◽  
...  
Keyword(s):  
Sequence Similarity ◽  
Aminopeptidase N ◽  
Sublethal Dose ◽  
Interacting Protein ◽  
Altered Expression ◽  
Cry Toxin ◽  
Long Run ◽  
Lepidopteran Larvae ◽  
Achaea Janata ◽  
Castor Semilooper

AbstractMidgut of lepidopteran larvae is a multifunctional tissue, which performs roles in digestion, absorption, immunity; transmission of pathogens and interaction with ingested various molecules. The proteins localized at the inner apical brush border membrane are primarily digestive proteases but some of them like aminopeptidase N, alkaline phosphatase, cadherins, ABC transporter C2 etc. interact with Crystal (Cry) toxins produced by Bacillus thuringiensis (Bt). In the present study aminopeptidase N (APN) was characterized as Cry toxin interacting protein in larval midgut of castor semilooper, Achaea janata. Transcriptomic and proteomic analyses revealed the presence of multiple isoforms of APNs (APN1, 2, 4, 6 and 9) which have less than 40% sequence similarity but show the presence of characteristic “GAMENEG” and zinc-binding motifs. Feeding of sublethal dose of Cry toxin caused differential expression of various APN isoform. Further, 6th generation Cry toxin exposed larvae showed reduced expression of APN2. This report suggests that A. janata larvae exploit altered expression of APNs to overcome the deleterious effects of Cry toxicity, which might facilitate toxin tolerance in long run.

Ovicidal and toxic effects of certain plant extracts to the castor semilooper, Achaea janata L. (Noctuidae: Lepidoptera)

2017 ◽  
Vol 51 (04) ◽  
Author(s):  
Ashwini A. Devarshi ◽  
S. R. Yankanchi
Keyword(s):  
Fourth Instar ◽  
Toxic Effects ◽  
Vitex Negundo ◽  
Ovicidal Activity ◽  
Leaf Extracts ◽  
Argemone Mexicana ◽  
Cent Mortality ◽  
Achaea Janata ◽  
Castor Semilooper ◽  
Ld50 Value

Ovicidal and toxic effects of crude leaf extracts of Clerodendrum inerme, Clerodendrum splendens, Clerodendrum multiflorum, Vitex negundo and Argemone mexicana were evaluated against the castor semilooper, Achaea janata L. (Noctuidae: Lepidoptera) using different bioassay methods. Among the extracts tested, the highest ovicidal activity was observed in C. splendens as well as A. mexicana with LD50 values of 7.65 and 9.14 mg-1, respectively. Leaf extracts of A. mexicana and C. inerme were toxic to both third and fourth instar larvae of A. janata through topical application. However, the extracts of A. mexicana and C. inerme found to be more toxic to third instar larvae with 70 and 73 per cent mortality, respectively. The lowest LD50 value of 5.33 mg-1 was recorded by A. mexicana extract and was followed by C. inerme extract with LD50 value of 7.26 mg-1. Present results indicated that A. mexicana and C. inerme plants have potential to use in IPM programme.

scholarly journals Interaction of Gene-Cloned and Insect Cell-Expressed Aminopeptidase N of Spodoptera litura with Insecticidal Crystal Protein Cry1C

2002 ◽  
Vol 68 (9) ◽  
pp. 4583-4592 ◽  
Author(s):  
Neema Agrawal ◽  
Pawan Malhotra ◽  
Raj K. Bhatnagar
Keyword(s):  
Insect Cell ◽  
Spodoptera Litura ◽  
Expression System ◽  
Insect Cell Line ◽  
Baculovirus Expression System ◽  
Aminopeptidase N ◽  
Receptor Protein ◽  
Binding Studies ◽  
Toxin Binding ◽  
Cry Toxin

ABSTRACT Insecticidal toxins produced by Bacillus thuringiensis interact with specific receptors located in the midguts of susceptible larvae, and the interaction is followed by a series of biochemical events that lead to the death of the insect. In order to elucidate the mechanism of action of B. thuringiensis toxins, receptor protein-encoding genes from many insect species have been cloned and characterized. In this paper we report the cloning, expression, and characterization of Cry toxin-interacting aminopeptidase N (APN) isolated from the midgut of a polyphagous pest, Spodoptera litura. The S. litura APN cDNA was expressed in the Sf21 insect cell line by using a baculovirus expression system. Immunofluorescence staining of the cells revealed that the expressed APN was located at the surface of Sf21 cells. Treatment of Sf21 cells expressing S. litura APN with phosphatidylinositol-specific phospholipase C demonstrated that the APN was anchored in the membrane by a glycosylphosphatidylinositol moiety. Interaction of the expressed receptor with different Cry toxins was examined by immunofluorescence toxin binding studies and ligand blot and immunoprecipitation analyses. By these experiments we showed that the bioactive toxin, Cry1C, binds to the recombinant APN, while the nonbioactive toxin, Cry1Ac, showed no interaction.

scholarly journals RNA-Seq analysis and de novo transcriptome assembly of Cry toxin susceptible and tolerant Achaea janata larvae

2019 ◽  
Vol 6 (1) ◽  
Author(s):  
Narender K. Dhania ◽  
Vinod K. Chauhan ◽  
R. K. Chaitanya ◽  
Aparna Dutta-Gupta
Keyword(s):  
De Novo ◽  
Transcriptome Assembly ◽  
De Novo Transcriptome Assembly ◽  
Rna Seq ◽  
De Novo Transcriptome ◽  
Cry Toxin ◽  
Achaea Janata

Determination of Cry toxin activity and identification of an aminopeptidase N receptor-like gene in Asymmathetes vulcanorum (Coleoptera: Curculionidae)

2012 ◽  
Vol 111 (1) ◽  
pp. 94-98 ◽  
Author(s):  
Jorge Eduardo Cortázar Gómez ◽  
Silvio Alejandro López-Pazos ◽  
Jairo Cerón
Keyword(s):  
Aminopeptidase N ◽  
Cry Toxin

scholarly journals Functional Interpretation of a Non-Gut Hemocoelic Tissue Aminopeptidase N (APN) in a Lepidopteran Insect Pest Achaea janata

PLoS ONE ◽  
2013 ◽  
Vol 8 (11) ◽  
pp. e79468 ◽  
Author(s):  
Thuirei Jacob Ningshen ◽  
Polamarasetty Aparoy ◽  
Venkat Rao Ventaku ◽  
Aparna Dutta-Gupta
Keyword(s):  
Insect Pest ◽  
Aminopeptidase N ◽  
Functional Interpretation ◽  
Lepidopteran Insect ◽  
Achaea Janata

scholarly journals Denaturation of Either Manduca sexta Aminopeptidase N or Bacillus thuringiensis Cry1A Toxins Exposes Binding Epitopes Hidden under Nondenaturing Conditions

2002 ◽  
Vol 68 (5) ◽  
pp. 2106-2112 ◽  
Author(s):  
Anu Daniel ◽  
Sreedhara Sangadala ◽  
Donald H. Dean ◽  
Michael J. Adang
Keyword(s):  
Bacillus Thuringiensis ◽  
Manduca Sexta ◽  
Brush Border ◽  
Binding Proteins ◽  
Membrane Vesicles ◽  
Aminopeptidase N ◽  
Toxin Binding ◽  
Cry Toxin ◽  
Domain I ◽  
Ligand Blot

ABSTRACT The effect of polypeptide denaturation of Bacillus thuringiensis Cry1A toxins or purified Manduca sexta 120-kDa aminopeptidase N on the specificities of their interactions was investigated. Ligand and dot blotting experiments were conducted with 125I-labeled Cry1Ac, Cry1Ac mutant 509QNR-AAA511 (QNR-AAA), or 120-kDa aminopeptidase N as the probe. Mutant QNR-AAA does not bind the N-acetylgalactosamine moiety on the 120-kDa aminopeptidase. Both 125I-Cry1Ac and 125I-QNR-AAA bound to 210- and 120-kDa proteins from M. sexta brush border membrane vesicles and purified 120-kDa aminopeptidase N on ligand blots. However, on dot blots 125I-QNR-AAA bound brush border vesicles but did not bind purified aminopeptidase except when aminopeptidase was denatured. In the reciprocal experiment, 125I-aminopeptidase bound Cry1Ac but did not bind QNR-AAA. 125I-aminopeptidase bound Cry1Ab to a limited extent but not the Cry1Ab domain I mutant Y153D or Cry1Ca. However, denatured 125I-aminopeptidase detected each Cry1A toxin and mutant but not Cry1Ca on dot blots. The same pattern of recognition occurred with native (nondenatured) 125I-aminopeptidase probe and denatured toxins as the targets. The broader pattern of toxin-binding protein interaction is probably due to peptide sequences being exposed upon denaturation. Putative Cry toxin-binding proteins identified by the ligand blot technique need to be investigated under native conditions early in the process of identifying binding proteins that may serve as functional toxin receptors.

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