How Bacillus thuringiensis has evolved specific toxins to colonize the insect world

Trends in Genetics

Volumn 17, Issue 4, 2001, Pages 193-199

  De Maagd, Ruud A ^a   Bravo, Alejandra ^b   Crickmore, Neil ^c  

^a WAGENINGEN UNIVERSITY   (Netherlands)

^b INSTITUTO DE BIOTECNOLOGÍA   (Mexico)

^c UNIVERSITY OF SUSSEX   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL TOXIN;

AMINO ACID SEQUENCE; BACILLUS THURINGIENSIS; BACTERIAL COLONIZATION; CRYSTAL; HOST; INSECT; NEMATODE; NONHUMAN; PHYLOGENY; PRIORITY JOURNAL; PROTEIN DOMAIN; REVIEW; SPECIES DIFFERENCE; SPOROGENESIS; TOXIN STRUCTURE;

ANIMALS; BACILLUS THURINGIENSIS; BACTERIAL PROTEINS; BACTERIAL TOXINS; ENDOTOXINS; GENE EXPRESSION REGULATION, BACTERIAL; HEMOLYSIN PROTEINS; INSECTS; PHYLOGENY; PROTEIN STRUCTURE, TERTIARY; RECOMBINATION, GENETIC; SPORES, BACTERIAL; VIRULENCE;

BACILLUS THURINGIENSIS; BACTERIA (MICROORGANISMS); HEXAPODA; INSECTA; NEMATODA; POSIBACTERIA; PROKARYOTA;

EID: 0035313205     PISSN: 01689525     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0168-9525(01)02237-5     Document Type: Review

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15. Different domains of Bacillus thuringiensis delta-endotoxins can bind to insect midgut membrane proteins on ligand blots
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27. Rendering a membrane protein soluble in water: A common packing motif in bacterial protein toxins
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29. Helix 4 of the Bacillus thuringiensis Cry1Aa toxin lines the lumen of the ion channel
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