Single-reversal charge in the β10-β11 receptor-binding loop of Bacillus thuringiensis Cry4Aa and Cry4Ba toxins reflects their different toxicity against Culex spp. larvae

Biochemical and Biophysical Research Communications

Volumn 450, Issue 2, 2014, Pages 948-952

  Visitsattapongse, Sarinporn ^a   Sakdee, Somsri ^a   Leetacheewa, Somphob ^a   Angsuthanasombat, Chanan ^a,b  

^a MAHIDOL UNIVERSITY   (Thailand)

^b Laboratory of Molecular Biophysics and Structural Biochemistry Biophysics Institute for Research and Development (BIRD)   (Thailand)

Author keywords

Bacillus thuringiensis; Charge reversal mutation; Cry4 toxins; Culex mosquito larvae; Receptor binding loop

Indexed keywords

BACILLUS THURINGIENSIS CRY4AA TOXIN; BACILLUS THURINGIENSIS CRY4BA TOXIN; BACILLUS THURINGIENSIS TOXIN; BETA 10 RECEPTOR; BETA 11 RECEPTOR; BETA ADRENERGIC RECEPTOR; LYSINE; PROLINE; THREONINE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; ARTICLE; BINDING AFFINITY; CELL INCLUSION; CONTROLLED STUDY; CULEX PIPIENS; CULEX QUINQUEFASCIATUS; IN VITRO STUDY; LARVA; LIGAND BINDING; MICROVILLUS; MIDGUT; MUTATION; NONHUMAN; PRIORITY JOURNAL; RECEPTOR BINDING;

BACILLUS THURINGIENSIS; CHARGE-REVERSAL MUTATION; CRY4 TOXINS; CULEX MOSQUITO-LARVAE; RECEPTOR-BINDING LOOP;

AMINO ACID SEQUENCE; ANIMALS; BACILLUS THURINGIENSIS; BACTERIAL PROTEINS; CULEX; ENDOTOXINS; HEMOLYSIN PROTEINS; LARVA; MOLECULAR SEQUENCE DATA; MOSQUITO CONTROL; MUTATION; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS;

EID: 84905092360     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.06.090     Document Type: Article

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