Tandem duplication of alkaline phosphatase genes and polymorphism in the intergenic sequence in Bombyx mori

Itoh, Masanobu; Inoue, Tsuneo; Kanamori, Yasushi; Nishida, Shinichi; Yamaguchi, Masamitsu

doi:10.1007/s00438-003-0880-9

Cited by 11 publications

(9 citation statements)

References 31 publications

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“…In B. mori, membrane-anchored and soluble forms of ALP can be found in the midgut epithelium of larvae (Eguchi 1995). The similarity between their gene sequences is 60%-79% (Itoh et al 2003). The membraneanchored form (m-ALP) is tethered to the membrane by a GPI-anchor, whereas the soluble form is localized primarily in the cavity of the goblet cells (Eguchi 1995).…”

Section: Discussionmentioning

confidence: 98%

Comparison of the localization of Bacillus thuringiensis Cry1A δ-endotoxins and their binding proteins in larval midgut of tobacco hornworm, Manduca sexta

et al. 2005

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Tobacco hornworm, Manduca sexta, is a model insect for studying the action of Bacillus thuringiensis (Bt) Cry toxins on lepidopterans. The proteins, which bind Bt toxins to midgut epithelial cells, are key factors involved in the insecticidal functions of the toxins. Three Cry1A-binding proteins, viz., aminopeptidase N (APN), the cadherin-like Bt-R 1 , and membrane-type alkaline phosphatase (m-ALP), were localized, by immunohistochemistry, in sections from the anterior, middle, and posterior regions of the midgut from second instar M. sexta larvae. Both APN and m-ALP were distributed predominantly along microvilli in the posterior region and to a lesser extent on the apical tip of microvilli in the anterior and middle regions. Bt-R 1 was localized at the base of microvilli in the anterior region, over the entire microvilli in the middle region, and at both the apex and base of microvilli in the posterior region. The localization of rhodamine-labeled Cry1Aa, Cry1Ab, and Cry1Ac binding was determined on sections from the same midgut regions. Cry1Aa and Cry1Ab bound to the apical tip of microvilli almost equally in all midgut regions. Binding of Cry1Ac was much stronger in the posterior region than in the anterior and middle regions. Thus, binding sites for Bt proteins and Cry1A toxins are co-localized on the microvilli of M. sexta midgut epithelial cells.

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Section: Discussionmentioning

confidence: 98%

Comparison of the localization of Bacillus thuringiensis Cry1A δ-endotoxins and their binding proteins in larval midgut of tobacco hornworm, Manduca sexta

et al. 2005

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“…The current work is aimed at identifying the specific molecular mechanism responsible for the downregulation of selected ALP genes in 456 larvae to demonstrate linkage with resistance. While the presence of this mechanism is speculative at this point, it is possible that gene proximity, which occurs with the genes for membranebound ALP (mALP) and soluble ALP (sALP) in B. mori larvae (55), may explain the selective downregulation of the SfmALP2 and SfsALP genes compared to the expression of the gene for SfmALP1, which may be the product of an alternative gene at a distant locus. This selective downregulation of ALP genes may explain the lack of significant fitness costs, as reported for larvae from the 456 strain (12).…”

Section: Discussionmentioning

confidence: 99%

Field-Evolved Mode 1 Resistance of the Fall Armyworm to Transgenic Cry1Fa-Expressing Corn Associated with Reduced Cry1Fa Toxin Binding and Midgut Alkaline Phosphatase Expression

Jakka

Gong

Hasler³

et al. 2016

Appl Environ Microbiol

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dInsecticidal protein genes from the bacterium Bacillus thuringiensis (Bt) are expressed by transgenic Bt crops (Bt crops) for effective and environmentally safe pest control. The development of resistance to these insecticidal proteins is considered the most serious threat to the sustainability of Bt crops. Resistance in fall armyworm (Spodoptera frugiperda) populations from Puerto Rico to transgenic corn producing the Cry1Fa insecticidal protein resulted, for the first time in the United States, in practical resistance, and Bt corn was withdrawn from the local market. In this study, we used a field-collected Cry1Fa corn-resistant strain (456) of S. frugiperda to identify the mechanism responsible for field-evolved resistance. Binding assays detected reduced Cry1Fa, Cry1Ab, and Cry1Ac but not Cry1Ca toxin binding to midgut brush border membrane vesicles (BBMV) from the larvae of strain 456 compared to that from the larvae of a susceptible (Ben) strain. This binding phenotype is descriptive of the mode 1 type of resistance to Bt toxins. A comparison of the transcript levels for putative Cry1 toxin receptor genes identified a significant downregulation (>90%) of a membrane-bound alkaline phosphatase (ALP), which translated to reduced ALP protein levels and a 75% reduction in ALP activity in BBMV from 456 compared to that of Ben larvae. We cloned and heterologously expressed this ALP from susceptible S. frugiperda larvae and demonstrated that it specifically binds with Cry1Fa toxin. This study provides a thorough mechanistic description of field-evolved resistance to a transgenic Bt crop and supports an association between resistance and reduced Cry1Fa toxin binding and levels of a putative Cry1Fa toxin receptor, ALP, in the midguts of S. frugiperda larvae.

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“…These proteins were reported to be detectable in the hemolymph before day 3 of fifth larval instar in a stagespecific expression. Molecular cloning of two tandemly duplicated alkaline phosphatases was reported for B. mori, i.e., a membranebound type and a soluble type 18) . Membrane-bound alkaline phosphatase (#156) was identified in this analysis.…”

Section: Protein Identificationsmentioning

confidence: 99%

Protein profile of silkworm midgut of fifth-instar day-3 larvae

et al. 2005

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SUMMARYProteomic analysis was performed on the midgut of fifth-instar day-3 female silkworm (Bombyx mori, strain p50) larvae. Though silkworm genome analysis has not yet been completed, the Drosophila genome and silkworm expression sequence tag (EST) data were applied to the analysis of the midgut proteins in the database (DB) for identification. The spots, which were excised manually from two-dimensional electrophoresis (2-DE) gels, were treated with 4-vinylpyridine for alkylation. Each spot was analyzed by capillary highperformance liquid chromatography coupled with ion-trap mass spectrometry (MS) after proteolysis using a trypsin. Nearly 60% of the proteins analyzed by MS were identified. These included many kinds of cytoskeleton proteins, ATPase, and chaperonins.

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Tandem duplication of alkaline phosphatase genes and polymorphism in the intergenic sequence in Bombyx mori

Cited by 11 publications

References 31 publications

Comparison of the localization of Bacillus thuringiensis Cry1A δ-endotoxins and their binding proteins in larval midgut of tobacco hornworm, Manduca sexta

Comparison of the localization of Bacillus thuringiensis Cry1A δ-endotoxins and their binding proteins in larval midgut of tobacco hornworm, Manduca sexta

Field-Evolved Mode 1 Resistance of the Fall Armyworm to Transgenic Cry1Fa-Expressing Corn Associated with Reduced Cry1Fa Toxin Binding and Midgut Alkaline Phosphatase Expression

Protein profile of silkworm midgut of fifth-instar day-3 larvae

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