The Heliothis virescens 170kDa aminopeptidase functions as “Receptor A” by mediating specific Bacillus thuringiensis Cry1A δ-endotoxin binding and pore formation

Luo, Ke; Sangadala, Sreedhara; Masson, Luke; Mazza, Alberto; Brousseau, Roland; Adang, Michael J.

doi:10.1016/s0965-1748(97)00052-0

Cited by 136 publications

(145 citation statements)

References 37 publications

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“…By use of SPR analysis, Cry1Aa, Cry1Ab, and Cry1Ac, but not Cry1Ca or Cry1Ea, were shown to interact with the purified APN, and only Cry1Ac binding to APN could be inhibited with GalNAc. Unlike the observation with M. sexta, all Cry1A proteins were thought to bind to H. virescens APN at two sites, as determined by the observed 2:1 molar ratio of bound toxin to receptor, and by the good fit of experimental data to a two-binding-site model based on kinetics (116). In a later study (8), Cry1Fa was shown to bind to this APN by ligand blot analysis, and thus it appeared that class 1 H. virescens APN was not exclusively a Cry1A-binding protein.…”

Section: Apnmentioning

confidence: 62%

“…Binding was also tested by SPR analysis and under these conditions Cry1Ac, but not Cry1Aa or Cry1Ab, bound to native APN and Cry1Ac binding could be completely blocked with competing GalNAc (177). The binding of Cry1Ac to APN was reported to occur in a 1:1 ratio, in contrast to the 2:1 ratio reported for the interaction between Cry1Ac and class 1 M. sexta APN (120) and class 1 H. virescens APN (116). Cloned, exogenously expressed L. dispar APN has also been studied (48).…”

Section: Apnmentioning

confidence: 94%

“…A 170-kDa class 1 APN from H. virescens has also been identified as a Cry1A-binding protein (116). Like M. sexta APN, the first H. virescens APN was isolated by Cry1Ac affinity chromatography using GalNAc to elute the protein.…”

Section: Apnmentioning

confidence: 99%

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Role of Receptors in Bacillus thuringiensis Crystal Toxin Activity

Pigott

Ellar

2007

Microbiol Mol Biol Rev

595

598

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SUMMARY Bacillus thuringiensis produces crystalline protein inclusions with insecticidal or nematocidal properties. These crystal (Cry) proteins determine a particular strain's toxicity profile. Transgenic crops expressing one or more recombinant Cry toxins have become agriculturally important. Individual Cry toxins are usually toxic to only a few species within an order, and receptors on midgut epithelial cells have been shown to be critical determinants of Cry specificity. The best characterized of these receptors have been identified for lepidopterans, and two major receptor classes have emerged: the aminopeptidase N (APN) receptors and the cadherin-like receptors. Currently, 38 different APNs have been reported for 12 different lepidopterans. Each APN belongs to one of five groups that have unique structural features and Cry-binding properties. While 17 different APNs have been reported to bind to Cry toxins, only 2 have been shown to mediate toxin susceptibly in vivo. In contrast, several cadherin-like proteins bind to Cry toxins and confer toxin susceptibility in vitro, and disruption of the cadherin gene has been associated with toxin resistance. Nonetheless, only a small subset of the lepidopteran-specific Cry toxins has been shown to interact with cadherin-like proteins. This review analyzes the interactions between Cry toxins and their receptors, focusing on the identification and validation of receptors, the molecular basis for receptor recognition, the role of the receptor in resistant insects, and proposed models to explain the sequence of events at the cell surface by which receptor binding leads to cell death.

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Section: Apnmentioning

confidence: 62%

Section: Apnmentioning

confidence: 94%

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Role of Receptors in Bacillus thuringiensis Crystal Toxin Activity

Pigott

Ellar

2007

Microbiol Mol Biol Rev

595

598

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“…From the remaining data some peptides matched sequences of aminopeptidases previously identified as Cry1Ac-binding proteins from either H. virescens (Banks et al, 2001;Luo et al, 1997) or M. sexta (Knight et al, 1994). All the high-quality mass spectral data were used to generate de novo sequence interpretations of six residues or more.…”

Section: Resultsmentioning

confidence: 99%

Diversity of aminopeptidases, derived from four lepidopteran gene duplications, and polycalins expressed in the midgut of Helicoverpa armigera: Identification of proteins binding the δ-endotoxin, Cry1Ac of Bacillus thuringiensis

Angelucci

Barrett-Wilt²,

Hunt

et al. 2008

Insect Biochemistry and Molecular Biology

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Helicoverpa armigera midgut proteins that bind the Bacillus thuringiensis (Bt) δ-endotoxin Cry1Ac were purified by affinity chromatography. SDS-PAGE showed that several proteins were eluted with N-acetylgalactosamine and no further proteins were detected after elution with urea. Tandem mass spectral data for tryptic peptides initially indicated that the proteins resembled aminopeptidases (APNs) from other lepidopterans and cDNA sequences for seven APNs were isolated from H. armigera through a combination of cloning with primers derived from predicted peptide sequences and established EST libraries. Phylogenetic analysis showed lepidopteran APN genes in nine clades of which five were part of a lepidopteran-specific radiation. The Cry1Ac-binding proteins were then identified with four of the seven HaAPN genes. Three of those four APNs are likely orthologs of APNs characterised as Cry1Ac-binding proteins in other lepidopterans. The fourth Cry1Ac-binding APN has orthologs not previously identified as Cry1Ac-binding partners. The HaAPN genes were expressed predominantly in the midgut through larval development. Each showed consistent expression along the length of the midgut but five of the genes were expressed at levels about two orders of magnitude greater than the remaining two. The remaining mass spectral data identified sequences encoding polycalin proteins with multiple lipocalin-like domains. A polycalin has only been previously reported in another lepidopteran, Bombyx mori, but polycalins in both species are now linked with binding of Bt Cry toxins. This is the first report of hybrid, lipocalin-like domains in shorter polycalin sequences that are not present in the longest sequence. We propose that these hybrid domains are generated by alternative splicing of the mRNA.

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“…As aminopeptidades N (APNs) são metaloproteases dependentes de zinco que clivam as extremidades N-terminais de cadeias polipeptídicas e tem uma participação primordial na digestão dos insetos (Terra, W.R. & Ferreira, C., 1994). A partir de 1994, APNs conectadas à membrana apical por âncoras do tipo glicofosfatidilinositol (GPI) passaram a ser identificadas como receptores para as toxinas Cry (Luo, K. et al, 1997;Valaitis, A.P. et al, 1995).…”

Section: Receptoresunclassified

Modelos caracterizando a interação entre as toxinas da família Cry1A de Bacillus thuringiensis e o receptor BT-R1 de Manduca sexta

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The Heliothis virescens 170kDa aminopeptidase functions as “Receptor A” by mediating specific Bacillus thuringiensis Cry1A δ-endotoxin binding and pore formation

Cited by 136 publications

References 37 publications

Role of Receptors in Bacillus thuringiensis Crystal Toxin Activity

Role of Receptors in Bacillus thuringiensis Crystal Toxin Activity

Diversity of aminopeptidases, derived from four lepidopteran gene duplications, and polycalins expressed in the midgut of Helicoverpa armigera: Identification of proteins binding the δ-endotoxin, Cry1Ac of Bacillus thuringiensis

Modelos caracterizando a interação entre as toxinas da família Cry1A de Bacillus thuringiensis e o receptor BT-R1 de Manduca sexta

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