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.

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 Mouse Receptor Interacting Protein 3 Does Not Contain a Caspase-Recruiting or a Death Domain but Induces Apoptosis and Activates NF-κB

1999 ◽  
Vol 19 (10) ◽  
pp. 6500-6508 ◽  
Author(s):  
Nanette J. Pazdernik ◽  
David B. Donner ◽  
Mark G. Goebl ◽  
Maureen A. Harrington
Keyword(s):  
Sequence Similarity ◽  
Kinase Domain ◽  
Dominant Negative ◽  
Dominant Negative Mutant ◽  
Death Domain ◽  
Interacting Protein ◽  
C Terminus ◽  
Catalytically Active ◽  
Induced Apoptosis

ABSTRACT The death domain-containing receptor superfamily and their respective downstream mediators control whether or not cells initiate apoptosis or activate NF-κB, events critical for proper immune system function. A screen for upstream activators of NF-κB identified a novel serine-threonine kinase capable of activating NF-κB and inducing apoptosis. Based upon domain organization and sequence similarity, this novel kinase, named mRIP3 (mouse receptor interacting protein 3), appears to be a new RIP family member. RIP, RIP2, and mRIP3 contain an N-terminal kinase domain that share 30 to 40% homology. In contrast to the C-terminal death domain found in RIP or the C-terminal caspase-recruiting domain found in RIP2, the C-terminal tail of mRIP3 contains neither motif and is unique. Despite this feature, overexpression of the mRIP3 C terminus is sufficient to induce apoptosis, suggesting that mRIP3 uses a novel mechanism to induce death. mRIP3 also induced NF-κB activity which was inhibited by overexpression of either dominant-negative NIK or dominant-negative TRAF2. In vitro kinase assays demonstrate that mRIP3 is catalytically active and has autophosphorylation site(s) in the C-terminal domain, but the mRIP3 catalytic activity is not required for mRIP3 induced apoptosis and NF-κB activation. Unlike RIP and RIP2, mRIP3 mRNA is expressed in a subset of adult tissues and is thus likely to be a tissue-specific regulator of apoptosis and NF-κB activity. While the lack of a dominant-negative mutant precludes linking mRIP3 to a known upstream regulator, characterizing the expression pattern and the in vitro functions of mRIP3 provides insight into the mechanism(s) by which cells modulate the balance between survival and death in a cell-type-specific manner.

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 Coevolution ofaah: Adps-Like Gene with the Host Bacterium Revealed by Comparative Genomic Analysis

2012 ◽  
Vol 2012 ◽  
pp. 1-9 ◽  
Author(s):  
Liyan Ping ◽  
Matthias Platzer ◽  
Gaiping Wen ◽  
Nicolas Delaroque
Keyword(s):  
Stop Codon ◽  
Sequence Similarity ◽  
General Pattern ◽  
Genomic Analysis ◽  
Dna Binding Proteins ◽  
Comparative Genomic Analysis ◽  
Comparative Genomic ◽  
Host Bacterium ◽  
High Sequence Similarity ◽  
Lepidopteran Larvae

A protein named AAH was isolated from the bacteriumMicrobacterium arborescensSE14, a gut commensal of the lepidopteran larvae. It showed not only a high sequence similarity to Dps-like proteins (DNA-binding proteins from starved cell) but also reversible hydrolase activity. A comparative genomic analysis was performed to gain more insights into its evolution. The GC profile of theaahgene indicated that it was evolved from a low GC ancestor. Its stop codon usage was also different from the general pattern of Actinobacterial genomes. The phylogeny ofdps-like proteins showed strong correlation with the phylogeny of host bacteria. A conserved genomic synteny was identified in some taxonomically related Actinobacteria, suggesting that the ancestor genes had incorporated into the genome before the divergence of Micrococcineae from other families. Theaahgene had evolved new function but still retained the typical dodecameric structure.

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

scholarly journals Biochemical characterization of androgen receptor-interacting protein 4

2006 ◽  
Vol 393 (3) ◽  
pp. 789-795 ◽  
Author(s):  
Andrii Domanskyi ◽  
Katja T. Virtanen ◽  
Jorma J. Palvimo ◽  
Olli A. Jänne
Keyword(s):  
Androgen Receptor ◽  
Biochemical Characterization ◽  
Specific Activity ◽  
Protein Complexes ◽  
Sequence Similarity ◽  
Protein Family ◽  
Interacting Protein ◽  
Attachment Sites

ARIP4 [AR (androgen receptor)-interacting protein 4] is a member of the SNF2-like family of proteins. Its sequence similarity to known proteins is restricted to the centrally located SNF2 ATPase domain. ARIP4 is an active ATPase, and dsDNA (double-stranded DNA) and ssDNA (single-stranded DNA) enhance its catalytic activity. We show in the present study that ARIP4 interacts with AR and binds to DNA and mononucleosomes. The N-terminal region of ARIP4 mediates interaction with AR. Kinetic parameters of the ARIP4 ATPase are similar to those of BRG-1 and SNF2h, two members of the SNF2-like protein family, but the specific activity of ARIP4 protein purified to >90% homogeneity is approximately ten times lower, being 120 molecules of ATP hydrolysed by an ARIP4 molecule per min in contrast with approx. 1000 ATP molecules hydrolysed per min by ATP-dependent chromatin remodellers. Unlike other members of the SNF2 family, ARIP4 does not appear to form large protein complexes in vivo or remodel mononucleosomes in vitro. ARIP4 is covalently modified by sumoylation, and mutation of six potential SUMO (small ubiquitin-related modifier) attachment sites abolished the ability of ARIP4 to bind DNA, hydrolyse ATP and activate AR function. We conclude that, similar to its closest homologues in the SNF2-like protein family, ATRX (α-thalassemia, mental retardation, X-linked) and Rad54, ARIP4 does not seem to be a classical chromatin remodelling protein.

Molecular mechanisms underlying K+ current downregulation in canine tachycardia-induced heart failure

2005 ◽  
Vol 288 (6) ◽  
pp. H2887-H2896 ◽  
Author(s):  
Fadi G. Akar ◽  
Richard C. Wu ◽  
George J. Juang ◽  
Yanli Tian ◽  
Mirka Burysek ◽  
...  
Keyword(s):  
Heart Failure ◽  
Molecular Mechanisms ◽  
Canine Model ◽  
Delayed Rectifier ◽  
Interacting Protein ◽  
Altered Expression ◽  
Protein Levels ◽  
Delayed Rectifier Current ◽  
Repolarization Reserve ◽  
Genes Encoding

Heart failure (HF) is characterized by marked prolongation of action potential duration and reduction in cellular repolarization reserve. These changes are caused in large part by HF-induced K+ current downregulation. Molecular mechanisms underlying these changes remain unclear. We determined whether downregulation of K+ currents in a canine model of tachycardia-induced HF is caused by altered expression of underlying K+ channel α- and β-subunits encoding these currents. K+ channel subunit expression was quantified in normal and failing dogs at the mRNA and protein levels in epicardial (Epi), midmyocardial (Mid), and endocardial (Endo) layers of left ventricle. Analysis of mRNA and protein levels of candidate genes encoding the transient outward K+ current ( Ito) revealed marked reductions in canine cKv4.3 expression in HF in Epi (44% mRNA, 39% protein), Mid (52% mRNA, 34% protein), and Endo (49% mRNA, 73% protein) layers and a paradoxical enhancement (41% Epi, 97% Mid, 113% Endo) in cKv1.4 protein levels, without significant changes in Kv channel-interacting protein cKChIP2 expression. Expression of cKir2.1, the gene underlying inward rectifier K+ current ( IK1), was unaffected by HF at mRNA and protein levels despite significant reduction in IK1, whereas canine ether-à-go-go-related gene (cERG), which encodes the rapidly activating component of the delayed rectifier current ( IK), exhibited increased protein expression. HF was not accompanied by significant changes in cKvLQT1 or cMinK mRNA and protein levels. These data indicate that 1) downregulation of Ito in HF is associated with decreased cKv4.3 and not cKv1.4 or cKChIP2, and 2) alterations in both the rapidly activating and slowly activating components of IK as well as IK1 in nonischemic dilated cardiomyopathy are not caused by changes in either transcript or immunoreactive protein levels of relevant channel subunits, which suggests posttranslational modification of these currents by HF.

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
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