Comparative biochemistry of entomocidal parasporal crystals of selected Bacillus thuringiensis strains

Tyrell, D J; Bulla, Lee A.; Andrews, Robert E.; Kramer, Karl J.; Davidson, Loren I.; Nordin, P.

doi:10.1128/jb.145.2.1052-1062.1981

Cited by 140 publications

(55 citation statements)

References 26 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…This is probably achieved by a combination of the alkaline pH of the insect gut and proteolytic activity either from the insect or from the crystal itself or both. To date the toxic polypeptide has not been isolated, but it appears that the proteins of Bti are different from those of other Bt's [10]. The acetate-soluble polypeptide obtained in this study may represent either the toxin or its degradation product.…”

Section: Discussionmentioning

confidence: 83%

Characterization of proteolytic activity associated with Bacillus thuringiensis var. israelensis crystals

Chilcott

1983

FEMS Microbiology Letters

View full text Add to dashboard Cite

Section: Discussionmentioning

confidence: 83%

Characterization of proteolytic activity associated with Bacillus thuringiensis var. israelensis crystals

Chilcott

1983

FEMS Microbiology Letters

View full text Add to dashboard Cite

“…Finally, the observed slight differences in mobilities of the 27 kDa toxins with SDS-PAGE is unlikely to be explained by the interchange of alanine and proline. There have been several reports of glycosylation of mosquitocidal B. thuringiensis 8-endotoxins [16][17][18]. This or other post-translational modifications (differing in the two cell types) may contribute to the differences in mobility.…”

Section: Resultsmentioning

confidence: 99%

Assessment of the toxicity of the cloned 27 kDa toxin of Bacillus thuringiensis var. morrisoni strain PG14

Earp

1988

FEMS Microbiology Letters

View full text Add to dashboard Cite

Expression of the cloned 27 kDa toxin gene from Bacillus thuringiensis strain PG14 in Bacillus subtilis facilitated the evaluation of the in vivo and in vitro toxicities of the pure toxin. This toxin is known to differ from the 27 kDa δ‐endotoxin of var. israelensis by a single amino acid. Comparison of toxicity values with data obtained from similarly produced 27 kDa toxin from var. israelensis suggested that the amino acid difference has no detectable effect on the potency of the toxin under the assay conditions employed.

show abstract

“…The primary antibody was goat antibody against alkaline-solubilized parasporal crystals from Bt subsp. kurstaki HD-1 Dipel (Tyrell et at.. 1981). The secondary antibody was horseradish peroxidase-con)ugated rabbit antigoat IgG (Kirkegaard and Perry Laboratories).…”

Section: Construction Of Chimeric Cionesmentioning

confidence: 99%

Larvicidal activity of chimeric Bacillus thuringiensis protoxins

Raymond

John

Bulla

1990

Molecular Microbiology

View full text Add to dashboard Cite

Bacillus thuringiensis subspecies kurstaki (Btk) and subspecies berliner (Btb) both produce lepidopteran-specific larvicidal protoxins with different activities against the same insect species. Toxic activity resides in the amino-terminal half of both protoxins, whereas the carboxy-terminal half of the molecules is not required for toxicity. The protoxins are 90% homologous, with a major cluster of differences in the amino-terminal half, and a 26 consecutive amino-acid insertion within the carboxy-terminal half of the Btk protoxin. Protoxin chimeras composed of the amino-terminal half of one subspecies and the carboxy-terminal half of the other were generated. Wild-type and chimeric protoxins were compared in bioassays against tobacco hornworm larvae. The amino-terminal half, the toxin itself, dictates specific larvicidal activity.

show abstract

Comparative biochemistry of entomocidal parasporal crystals of selected Bacillus thuringiensis strains

Abstract: pel (Abbott Laboratories, North Chicago, Ill.); B. thuringiensis subsp. alesti was a gift from P.

Cited by 140 publications

References 26 publications

Characterization of proteolytic activity associated with Bacillus thuringiensis var. israelensis crystals

Characterization of proteolytic activity associated with Bacillus thuringiensis var. israelensis crystals

Assessment of the toxicity of the cloned 27 kDa toxin of Bacillus thuringiensis var. morrisoni strain PG14

Larvicidal activity of chimeric Bacillus thuringiensis protoxins

Contact Info

Product

Resources

About