A Toxic Fragment from the Entomocidal Crystal Protein of<i>Bacillus thuringiensis</i>

Nagamatsu, Yasunori; Itai, Yuichi; Hatanaka, Chitoshi; Funatsu, Gunki; Hayashi, Katsuya

doi:10.1080/00021369.1984.10866193

Cited by 12 publications

(4 citation statements)

References 7 publications

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“…In the case of the 130 kDa lepidopteran toxins, the major proteolytic event in the insect gut is the removal of almost 600 amino acids from the C-terminus, which is a prerequisite for conversion of the inactive protoxin into the toxic form (Aronson et al, 1986). Other experiments (Nagamatsu et al, 1984;Hofte et al, 1986) showed that only 28 amino acids were removed from the N-terminus during the activation of the lepidopteran toxins. Studies on deletion mutants suggested that processing beyond this point would result in loss of activity in vivo H6fte et al, 1986).…”

Section: Discussionmentioning

confidence: 96%

Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis

Carroll

Ellar

1989

Biochemical Journal

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Insecticidal protein delta-endotoxin crystals harvested from sporulated cultures of Bacillus thuringiensis var. tenebrionis contain a major polypeptide of 67 kDa and minor polypeptides of 73, 72, 55 and 46 kDa. During sporulation, only the 73 kDa polypeptide could be detected at stage I. The 67 kDa polypeptide was first detected at stage II and increased in concentration throughout the later stages of sporulation and after crystal release, with a concomitant decrease in the 73 kDa polypeptide. This change could be blocked by the addition of proteinase inhibitors. Trypsin or insect-gut-extract treatment of the delta-endotoxin crystals after solubilization resulted in a cleavage product of 55 kDa with asparagine-159 of the deduced amino acid sequence of the toxin [Höfte, Seurinck, van Houtven & Vaeck (1987) Nucleic Acids Res. 15, 71-83; Sekar, Thompson, Maroney, Bookland & Adang (1987) Proc. Natl. Acad. Sci. U.S.A. 84, 7036-7040; McPherson, Perlak, Fuchs, Marrone, Lavrik & Fischhoff (1988) Biotechnology 6, 61-66] at the N-terminus. This polypeptide was found to be as toxic in vivo as native delta-endotoxin.

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Section: Discussionmentioning

confidence: 96%

Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis

Carroll

Ellar

1989

Biochemical Journal

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“…The toxin was prepared by tryptic digestion of CryIAa protein from B. thuringiensis sotto T84A1 as described [1]. The accession no.…”

Section: Methodsmentioning

confidence: 99%

“…Insecticidal crystalline inclusion (called crystal protein, or Cry; also, δ‐endotoxin) of Bacillus thuringiensis is the most widely used microbial pesticide, harmless to vertebrates or plants. The protein inclusions undergo limited proteolysis in the larval intestinal lumen and release toxic fragments (toxins) [1,2], causing midgut epithelial cells to swell and burst [3–5].…”

Section: Introductionmentioning

confidence: 99%

The cadherin‐like protein is essential to specificity determination and cytotoxic action of the Bacillus thuringiensis insecticidal CryIAa toxin

et al. 1999

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The Bacillus thuringiensis CryIAa toxin binds a cadherin-like protein (BtR175) on the brush-border membranes of the Bombyx mori midgut columnar cells, which are the targets. By introducing the BtR175 gene with a baculovirus, Spodoptera frugiperda Sf9 cells expressed BtR175 protein on the cell membrane and became susceptible to the CryIAa toxin. The toxin bound the cadherin repeat adjacent to the membrane and made a pore that passed inorganic ions, causing the cell to swell and burst. This was not observed with a BtR175 variant lacking the toxin-binding site. This in vitro experiment mimicked the specific insecticidal action of the toxin in vivo well.z 1999 Federation of European Biochemical Societies.

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“…5). Nagamatsu et al 16) also reported that the toxic fragment considered of two isomers with differ-ent charges. They thought that this heterogeneity was caused by different degrees of deamidation of essentially the same polypeptide.…”

Section: Resultsmentioning

confidence: 99%

Structure of the subunit protein of bipyramidal .DELTA.-endotoxin produced by Bacillus thuringiensis kurstaki strain HD-1.

Tojo

1986

Agricultural and Biological Chemistry

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A Toxic Fragment from the Entomocidal Crystal Protein ofBacillus thuringiensis

Cited by 12 publications

References 7 publications

Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis

Proteolytic processing of a coleopteran-specific δ-endotoxin produced by Bacillus thuringiensis var. tenebrionis

The cadherin‐like protein is essential to specificity determination and cytotoxic action of the Bacillus thuringiensis insecticidal CryIAa toxin

Structure of the subunit protein of bipyramidal .DELTA.-endotoxin produced by Bacillus thuringiensis kurstaki strain HD-1.

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