Identification of a juvenile hormone esterase gene by matching its peptide mass fingerprint with a sequence from the Drosophila genome project

Campbell, Peter M.; Harcourt, Rebecca; Crone, Erica J.; Claudianos, Charles; Hammock, Bruce D.; Russell, Robyn J.; Oakeshott, John G.

doi:10.1016/s0965-1748(01)00035-2

Cited by 53 publications

(46 citation statements)

References 15 publications

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“…These were also processed by in-gel digestion and LC/MS analysis, this time with an Agilent XCT ion trap mass spectrometer as described elsewhere (Campbell et al, 2001(Campbell et al, , 2008. In the intervening period, a more extensive collection of EST and full-length cDNA sequences from the midgut of H. armigera was developed (below) against which we could compare both the earlier peptide sequence interpretations and the later ion trap MS peptide fragmentation data.…”

Section: Identification Of Protein Bandsmentioning

confidence: 99%

“…The mRNA sequences of the HaAPN 1, 2, 3 and 4 genes were determined using mRNA and cDNA prepared for 3′-and 5′-Rapid Amplification of cDNA Ends (RACE) as previously described (Campbell et al, 2001). For 3′-RACE primers were designed from the peptide sequence reported in Liao et al (2005), highly conserved regions of insect APNs and certain peptides revealed by de novo sequence interpretations of the mass spectral data described above, particularly where they resembled partial gene sequences available for H. armigera or near relatives.…”

Section: Cloning and Sequencing Of Haapn Cdnasmentioning

confidence: 99%

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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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Section: Identification Of Protein Bandsmentioning

confidence: 99%

Section: Cloning and Sequencing Of Haapn Cdnasmentioning

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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“…33,35) The cDNA for JHE has been isolated and characterized from several insect orders including Lepidoptera, [46][47][48][49] Coleoptera 50) and Diptera. 51,52) The interaction mode of JHE with its substrate has been predicted using homology-based molecular modeling techniques. 53) The physiological significance of JHE in the regulation of JH titer has also been studied in detail.…”

Section: Biosynthesis Transport and Metabolism Of Juvenile Hormonementioning

confidence: 99%

Insect juvenile hormone action as a potential target of pest management

Minakuchi

Riddiford

2006

J. Pestic. Sci.

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Juvenile hormone (JH) is a sesquiterpenoid hormone that regulates growth and development in insects. Since JH is a hormone specific to insects and other arthropods, compounds disrupting JH action in insects are expected to be ideal insecticides with low toxicity to non-target organisms. Many natural or synthetic analogs with JH-like or anti-JH activity have been identified, and some potent JH mimics have been used as insecticides. Recent studies on the enzymes in JH biosynthetic and metabolic pathways should be helpful for the discovery of more potent analogs and for the establishment of new means of pest management using recombinant DNA technology. © Pesticide Science Society of Japan Keywords: juvenile hormone (JH), insect metamorphosis, insect growth regulators, biosynthesis and metabolism of JH. Review* To whom correspondence should be addressed. E-mail: chieka_minakuchi@yahoo.com © Pesticide Science Society of Japan doptera. 17,18) Higher Diptera such as D. melanogaster and the blowfly Calliphora vomitoria produce JH III bisepoxide. 19,20) A small amount of methyl farnesoate, a precursor of JH III, was found in cockroach embryos and larvae. [20][21][22] Methyl farnesoate has also been identified in crustaceans 23) and is thought to have a JH-like action in female reproduction. 24)12Ј-OH JH III identified from the corpora allata of the African locust Locusta migratoria migratorioides was reported to exhibit JH activity when a high dose of this compound was topically applied to Tenebrio pupae. 25,26) Biosynthesis, Transport and Metabolism of Juvenile HormoneIn insects, JH is synthesized in the corpora allata via the mevalonate pathway (Fig. 2).27) The mevalonate pathway also exists in mammals and plants, and the early steps from acetylCoA to farnesyl diphosphate are conserved among these organisms. Importantly, insects and other arthropods do not synthesize cholesterol de novo but have to acquire it from dietary sources because they lack the genes encoding squalene synthase and other subsequent enzymes of the sterol branch. 28,29) Another peculiarity of the mevalonate pathway in insects is the capacity to synthesize JH via the isoprenoid branch.The genes encoding the enzymes in the mevalonate pathway from acetyl-CoA to farnesyl diphosphate have been identified in the genome of D. melanogaster and the malaria mosquito Anopheles gambiae, and in an EST library of the pine engraver Ips pini.27) However, it has been difficult to identify the genes encoding enzymes from farnesyl diphosphate to JH

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“…Mass spectroscopy on the whole protein was performed using sinapinic acid as the matrix and BSA as the standard. The in-gel tryptic digest and subsequent mass spectroscopy were carried out essentially as described previously (27), except that the gel pieces were not treated with dithiothreitol and iodoacetamide. Theoretical molecular mass and trypsin digest patterns were calculated using Protein Prospector (prospector.ucsf.edu/, version 3.4.1).…”

Section: Methodsmentioning

confidence: 99%

A Novel Secreted Protein Toxin from the Insect Pathogenic Bacterium Xenorhabdus nematophila

Brown

Cao

Hines

et al. 2004

Journal of Biological Chemistry

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The bacterium Xenorhabdus nematophila is an insect pathogen that produces several proteins that enable it to kill insects. Screening of a cosmid library constructed from X. nematophila strain A24 identified a gene that encoded a novel protein that was toxic to insects. The 42-kDa protein encoded by the toxin gene was expressed and purified from a recombinant system, and was shown to kill the larvae of insects such as Galleria mellonella and Helicoverpa armigera when injected at doses of around 30 -40 ng/g larvae. Sequencing and bioinformatic analysis suggested that the toxin was a novel protein, and that it was likely to be part of a genomic island involved in pathogenicity. When the native bacteria were grown under laboratory conditions, a soluble form of the 42-kDa toxin was secreted only by bacteria in the phase II state. Preliminary histological analysis of larvae injected with recombinant protein suggested that the toxin primarily acted on the midgut of the insect. Finally, some of the common strategies used by the bacterial pathogens of insects, animals, and plants are discussed.

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Identification of a juvenile hormone esterase gene by matching its peptide mass fingerprint with a sequence from the Drosophila genome project

Cited by 53 publications

References 15 publications

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

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

Insect juvenile hormone action as a potential target of pest management

A Novel Secreted Protein Toxin from the Insect Pathogenic Bacterium Xenorhabdus nematophila

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