Insect paralysis by baculovirus-mediated expression of a mite neurotoxin gene

Tomalski, Michael D.; Miller, Lois K.

doi:10.1038/352082a0

Cited by 258 publications

(96 citation statements)

References 16 publications

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“…This is shortened with the parental baculovirus infection to about 7 days and to 5-6 days with recombinant SPx baculovirus. Similar results have been obtained with recombinant baculoviruses expressing neurotoxins of the scorpion A. australis or the mite Pyemotes tritici 5 [6,7,49]. We think that further improvements could be obtained by adjusting the secretion pathway to imitate the native one.…”

Section: Discussionsupporting

confidence: 79%

“…The two helices have quite different characters. The first, PLLILGS (3)(4)(5)(6)(7)(8)(9), is apolar, whereas the second, IQ-AIHDAQR (17)(18)(19)(20)(21)(22)(23)(24)(25), contains polar and charged amino acids. This will result in different interactions with cell membranes.…”

Section: Discussionmentioning

confidence: 99%

“…It seems likely that when not exported, this peptide is either destroyed inside the cell or is toxic for the cells. Sequence analysis suggested that the part LPLLILGSLLMTPPVIQA (2)(3)(4)(5)(6)(7)(8)(9)(10)(11)(12)(13)(14)(15)(16)(17)(18)(19), which looks like a transmembrane segment is similar to signal peptides of a variety of proteins [34]. If without an authentic signal peptide this fragment is seen by the expressing cell as a signal peptide, it could be degraded by the appropriate enzymatic system such as one that cleaves the signal peptide of preprolactine within its hydrophobic core, between two leucine clusters [35].…”

Section: Discussionmentioning

confidence: 99%

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Poneratoxin, a neurotoxin from ant venom

Szołajska

Poznański

Ferber

et al. 2004

European Journal of Biochemistry

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Poneratoxin is a small neuropeptide found in the venom of the ant Paraponera clavata. It is stored in the venom reservoir as an inactive 25-residue peptide. Here we describe both chemically synthesized poneratoxin and poneratoxin obtained by expression in insect cells. When expressed in insect cells, poneratoxin was observed attached to cell membranes. Both synthetic and recombinant ponerotoxins were soluble below pH 4.5. The structure of synthetic poneratoxin was characterized by circular dichroism and solved by nuclear magnetic resonance. In an environment imitating a lipid bilayer, at pH within the range of insect hemolymph, synthetic poneratoxin has a V shape, with two a-helices connected by a b-turn. Insect larvae were paralyzed by injection of either of the purified toxins, with the recombinant one acting faster. The recombinant toxin-producing baculovirus reduced the average survival time of the insect host by 25 h compared with unmodified virus. Mass spectrometry analysis showed that the recombinant toxin has an N-terminal 21-residue extension, possibly improving its stability and/or stabilizing the membrane-bound state. The potential use of poneratoxin for the construction of biological insecticide is discussed.

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Section: Discussionsupporting

confidence: 79%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Poneratoxin, a neurotoxin from ant venom

Szołajska

Poznański

Ferber

et al. 2004

European Journal of Biochemistry

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“…Additionally, in excess of 50% identity has been reported between lepidopteran baculovirus granulin and polyhedrin sequences (8). The introduction of foreign genes in lieu of the polyhedrin gene to increase the efficacy of the virus, has resulted in varying success (9)(10)(11)(12).…”

Section: Introductionmentioning

confidence: 99%

Untitled

Fielding

Davison

1999

Virus Genes

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Abstract. The polyhedrin gene (polh) was identified from the Trichoplusia ni (Tni) single capsid nuclear polyhedrosis virus (SNPV). An EcoRI fragment containing the truncated polyhedrin gene was detected by hybridization with an AcMNPV expression vector probe; the remaining portion of the gene was amplified by reverse PCR. An open reading frame (ORF) of 741 nucleotides (nt), encoding a putative protein of 246 amino acids (a.a) with M r 28,780 Da was identified. The 5 t -noncoding region contained the putative late (TAAG) transcription initiation motif. The 3 t end, downstream of the translation stop codon, lacked an obvious putative poly (A) signal. Nucleotide and amino acid homology are greater than 80% to that of Mamestra brassicae polyhedrin sequences. Results suggest that T. niSNPV is a member of the group II nuclear polyhedrosis viruses. IntroductionThe Family Baculoviridae are invertebrate-specific pathogens that contain a single circular supercoiled double stranded DNA molecule that ranges in size from 80-220 kilobases (1). In excess of 600 insect species are susceptible to baculovirus infection, with a single virus isolate normally restricted to one host or a few closely related species.

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“…Recombinant baculoviruses which express toxins have been constructed and shown to have an improved insecticidal activity (1)(2)(3)(4)(5).…”

Section: Introductionmentioning

confidence: 99%

Construction of occluded recombinant baculoviruses containing the full-length cry1Ab and cry1Ac genes from Bacillus thuringiensis

Ribeiro

Crook

1998

Braz J Med Biol Res

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The administration of baculoviruses to insects for bioassay purposes is carried out, in most cases, by contamination of food surfaces with a known amount of occlusion bodies (OBs). Since per os infection is the natural route of infection, occluded recombinant viruses containing crystal protein genes (cry1Ab and cry1Ac) from Bacillus thuringiensis were constructed for comparison with the baculovirus prototype Autographa californica nucleopolyhedrovirus (AcNPV). The transfer vector pAcUW2B was used for construction of occluded recombinant viruses. The transfer vector containing the crystal protein genes was cotransfected with linearized DNA from a non-occluded recombinant virus. The isolation of recombinant viruses was greatly facilitated by the reduction of background "wild type" virus and the increased proportion of recombinant viruses. Since the recombinant viruses containing full-length and truncated forms of the crystal protein genes did not seem to improve the pathogenicity of the recombinant viruses when compared with the wild type AcNPV, and in order to compare expression levels of the full-length crystal proteins produced by nonoccluded and occluded recombinant viruses the full-length cry1Ab and cry1Ac genes were chosen for construction of occluded recombinant viruses. The recombinant viruses containing full-length and truncated forms of the crystal protein genes did not seem to improve its pathogenicity but the size of the larvae infected with the recombinant viruses was significantly smaller than that of larvae infected with the wild type virus.

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Insect paralysis by baculovirus-mediated expression of a mite neurotoxin gene

Cited by 258 publications

References 16 publications

Poneratoxin, a neurotoxin from ant venom

Poneratoxin, a neurotoxin from ant venom

Untitled

Construction of occluded recombinant baculoviruses containing the full-length cry1Ab and cry1Ac genes from Bacillus thuringiensis

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