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.
From: School of Life Sciences, University of Hyderabad, Hyderabad 500046, India.
The Biochemical journal
- Publish Date: Jul 2007
- ISSN: 1470-8728
- Volume: 405
- Issue: 2
- Pages: 287-97
- Medium: Internet
- Language: English
- Citation (JAMA): Budatha Madhusudhan, Meur Gargi, Dutta-Gupta Aparna, et al. 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.. Biochem. J. Jul 2007;405:287-97
Abstract
Bacillus thuringiensis insecticidal crystal proteins bind to cell-surface receptors which represent a family of aminopeptidases [APN (aminopeptidase N)] present on the brush border membrane of insect midgut cells of susceptible insects leading to pore formation and death of the insect. We report here for the first time the presence of a novel APN in the fat body of the moth Achaea janata. Northern blotting detected at least one APN-specific transcript in the fat body, whereas two transcripts of different sizes were detected in the midgut. We have cloned two full-length APN cDNAs of 3015 bp and 2850 bp from fat body and midgut respectively, which encode proteins of 1004 and 950 amino acids. These two APNs share only 33% amino acid sequence identity, but both display the typical APN features, such as the N-terminal signal peptide, several putative glycosylation sites, C-terminal glycosylphosphatidylinositol anchor signal, the APN-specific zinc-binding/gluzincin motif HEXXHX(18)E and gluzincin motif GAMENWG. The fat body APN manifested a variation in its expression with respect to tissue and developmental stage. In spite of the abundance of the APN transcript in the fat body, fairly low APN activity was detected in this tissue. The fat-body- and midgut-specific APNs showed differential interaction with various Cry1A toxins. Besides, the level of toxicity of different Cry subtypes varied enormously with mode/site of delivery, such as intrahaemocoelic injections and feeding bioassays. These data indicate that the fat body might be a potential alternative Cry toxin target site in the moth.
Mesh Headings (Keywords): Amino Acid Sequence, Aminopeptidases, Animals, Antigens, CD13, Bacterial Proteins, Bacterial Toxins, Cloning, Molecular, Endotoxins, Fat Body, Glycosylphosphatidylinositols, Hemolysin Proteins, Immunoblotting, Insect Proteins, Larva, Molecular Sequence Data, Moths, Phylogeny, Receptors, Cell Surface, Sequence Alignment, Tissue Distribution
Check for Full Text / PubMed Unique Identifier (PMID): 17402938
This abstract is part of PubMed, a service of the U.S. National Library of Medicine. PubMed includes more than 17 million citations from MEDLINE and other life science journals for biomedical articles. See Copyright and Disclaimers.
Linked medical terms appearing on this page are added by Healia to help readers find more information and are not part of the original PubMed document.
The data herein was last updated on July 8th, 2008 and may not reflect the most current and accurate data available from NLM.