Common genomic structure for the Lepidoptera cadherin-like genes

Bel, Yolanda; Escriche, Baltasar

doi:10.1016/j.gene.2006.07.001

Cited by 25 publications

(24 citation statements)

References 52 publications

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“…The function of cad88C is not reported in the literature. Bel and Escriche (41) noted that in zebrafish and mammals an orthologue of lepidopteran midgut cadherins, cadherin 23, is involved in maintenance of hair bundles (stereocilia) of the inner ear, related to signal mechanotransduction.…”

Section: Discussionmentioning

confidence: 99%

Anopheles gambiae Cadherin AgCad1 Binds the Cry4Ba Toxin of Bacillus thuringiensis israelensis and a Fragment of AgCad1 Synergizes Toxicity

et al. 2008

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A midgut cadherin AgCad1 cDNA was cloned from Anopheles gambiae larvae and analyzed for its possible role as a receptor for the Cry4Ba toxin of Bacillus thuringiensis strain israelensis. The AgCad1 cadherin encodes a putative 1735-residue protein organized into an extracellular region of 11 cadherin repeats (CR) and a membrane-proximal extracellular domain (MPED). AgCad1 mRNA was detected in midgut of larvae by polymerase chain reaction (PCR). The AgCad1 protein was localized, by immunochemistry of sectioned larvae, predominately to the microvilli in posterior midgut. The localization of Cry4Ba binding was determined by the same technique, and toxin bound microvilli in posterior midgut. The AgCad1 protein was present in brush border membrane fractions prepared from larvae, and Cry4Ba toxin bound the same-sized protein on blots of those fractions. The AgCad1 protein was expressed transiently in Drosophila melanogaster Schneider 2 (S2) cells. 125 I-Cry4Ba toxin bound AgCad1 from S2 cells in a competitive manner. Cry4Ba bound to beads extracted 200 kDa AgCad1 and a 29 kDa fragment of AgCad1 from S2 cells. A peptide containing the AgCad1 region proximal to the cell (CR11-MPED) was expressed in Escherichia coli. Although Cry4Ba showed limited binding to CR11-MPED, the peptide synergized the toxicity of Cry4Ba to larvae. AgCad1 in the larval brush border is a binding protein for Cry4Ba toxin. On the basis of binding results and CR11-MPED synergism of Cry4Ba toxicity, AgCad1 is probably a Cry4Ba receptor.Mosquitoes in the genus Anopheles vector plasmodia that cause malaria, a major public health problem in the world. In some habitats, Anopheline species are controlled by nonchemical larvicides based on the bacterium Bacillus thuringiensis (Bt) 1 serovariety israelensis de Barjac. The specific toxicity of Bti to Anopheles and Aedes spp. is due to the protein components of the parasporal crystal (reviewed in ref 1).The parasporal crystal of Bti is composed of three major insecticidal Cry proteins (Cry4Aa, Cry4Ba, and Cry11Aa) and cytolytic proteins (Cyt1 and Cyt2). The Cry4Ba insecticidal protein is highly toxic to Anopheles and Aedes larvae but not to Culex larvae (2,3). The Cry4Ba toxin crystal structure shows that it is very similar to other Cry toxins with their three-domain † This research was supported by National Institutes of Health Grant R01 AI 29092 to D. H. Dean (The Ohio State University) and M.J.A. Inhibition of toxicity is accepted evidence for function as a Cry toxin receptor. Typically, a peptide fragment of the receptor (21) or a phage mimic of the receptor (20) attenuates Cry in vivo toxicity to larvae. Recently, we reported an opposite effect in which a fragment of Bt-R 1 cadherin, the Cry1A receptor from Manduca sexta (21,22), not only bound toxin but enhanced Cry1A toxicity against lepidopteran larvae (23). If the binding residues within cadherin repeat 12 (CR) were removed, the resulting peptide lost the ability to bind toxin and lost its function as a toxin synergist.In this work, we descri...

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Section: Discussionmentioning

confidence: 99%

Anopheles gambiae Cadherin AgCad1 Binds the Cry4Ba Toxin of Bacillus thuringiensis israelensis and a Fragment of AgCad1 Synergizes Toxicity

et al. 2008

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“…Therefore, the cdh cDNA from four randomly selected Europe-R individuals was completely sequenced, and the differences with respect to the reference cdh sequence DQ000165 are summarized in Table 2. The most remarkable change in the sequence occurred at position 1630, which falls into cadherin repeat (CR) 5 in the protein, according to the numeric system of Bel and Escriche (2006). At this position, two different sequence changes were observed: a deletion of three base pairs (that leads to the substitution of two Val by one Arg in amino acid 544 of the protein) (GenBank accession no.…”

Section: Sequence Analysis Of Cdh Mrnamentioning

confidence: 99%

“…No differences were found among the samples examined. Comparison with the reference sequence DQ000165 showed 11 SNPs that in two The 12-cadherin repeat domains were defined following Bel and Escriche (2006). CR, cadherin repeat; MPR, membrane proximal region (335 bp); TM, transmembrane region (69 bp); IR, intracellular region.…”

Section: Sequence Analysis Of the Putative Cry1ab Binding Regionmentioning

confidence: 99%

“…In the three Lepidoptera species Heliothis virescens (Fabricius) (Gahan et al, 2001), Pectinophora gossypiella (Saunders) (Morin et al, 2003), and Helicoverpa armigera (Hü bner) (Xu et al, 2005), resistance to Cry1Ac has been shown to be conferred by mutations in the 12-cadherin-domain protein. This is a transmembrane protein of unknown function, which has 11 or 12 cadherin-repeat domains in the extracellular part of the protein and that seems to have a common structure in Lepidoptera (Bel and Escriche, 2006;Pigott and Ellar, 2007).…”

Section: Introductionmentioning

confidence: 99%

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Variability in the cadherin gene in an Ostrinia nubilalis strain selected for Cry1Ab resistance

Bel

Siqueira

Siegfried

et al. 2009

Insect Biochemistry and Molecular Biology

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“…Until now, insect cadherins have been proven or suggested to interact with Cry toxins in at least six lepidopteran (2), two dipteran (12)(13)(14), and two coleopteran (15,16) species. A toxin-binding cadherin receptor is composed of five domains: signal peptide (SP), 8 to 12 cadherin repeats (CRs), membrane-proximal extracellular domain (MPED), transmembrane region (TM), and internal cytoplasmic domain (IC) (17). In Manduca sexta cadherin, MsBtR1, three Cry1A binding sites are indicated in CR7 (18,19), CR11 (20), and CR12 (21).…”

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confidence: 99%

A Spodoptera exigua Cadherin Serves as a Putative Receptor for Bacillus thuringiensis Cry1Ca Toxin and Shows Differential Enhancement of Cry1Ca and Cry1Ac Toxicity

Ren

Chen

Zhang

et al. 2013

Appl Environ Microbiol

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bCrystal toxin Cry1Ca from Bacillus thuringiensis has an insecticidal spectrum encompassing lepidopteran insects that are tolerant to current commercially used B. thuringiensis crops (Bt crops) expressing Cry1A toxins and may be useful as a potential bioinsecticide. The mode of action of Cry1A is fairly well understood. However, whether Cry1Ca interacts with the same receptor proteins as Cry1A remains unproven. In the present paper, we first cloned a cadherin-like gene, SeCad1b, from Spodoptera exigua (relatively susceptible to Cry1Ca). SeCad1b was highly expressed in the larval gut but scarcely detected in fat body, Malpighian tubules, and remaining carcass. Second, we bacterially expressed truncated cadherin rSeCad1bp and its interspecific homologue rHaBtRp from Helicoverpa armigera (more sensitive to Cry1Ac) containing the putative toxin-binding regions. Competitive binding assays showed that both Cry1Ca and Cry1Ac could bind to rSeCad1bp and rHaBtRp, and they did not compete with each other. Third, Cry1Ca ingestion killed larvae and decreased the weight of surviving larvae. Dietary introduction of SeCad1b double-stranded RNA (dsRNA) reduced approximately 80% of the target mRNA and partially alleviated the negative effect of Cry1Ca on larval survival and growth. Lastly, rSeCad1bp and rHaBtRp differentially enhanced the negative effects of Cry1Ca and Cry1Ac on the larval mortalities and growth of S. exigua and H. armigera. Thus, we provide the first lines of evidence to suggest that SeCad1b from S. exigua is a functional receptor of Cry1Ca.

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Common genomic structure for the Lepidoptera cadherin-like genes

Cited by 25 publications

References 52 publications

Anopheles gambiae Cadherin AgCad1 Binds the Cry4Ba Toxin of Bacillus thuringiensis israelensis and a Fragment of AgCad1 Synergizes Toxicity

Anopheles gambiae Cadherin AgCad1 Binds the Cry4Ba Toxin of Bacillus thuringiensis israelensis and a Fragment of AgCad1 Synergizes Toxicity

Variability in the cadherin gene in an Ostrinia nubilalis strain selected for Cry1Ab resistance

A Spodoptera exigua Cadherin Serves as a Putative Receptor for Bacillus thuringiensis Cry1Ca Toxin and Shows Differential Enhancement of Cry1Ca and Cry1Ac Toxicity

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