pubmed-article:7529493 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:7529493 | lifeskim:mentions | umls-concept:C0004597 | lld:lifeskim |
pubmed-article:7529493 | lifeskim:mentions | umls-concept:C0441635 | lld:lifeskim |
pubmed-article:7529493 | lifeskim:mentions | umls-concept:C0022009 | lld:lifeskim |
pubmed-article:7529493 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:7529493 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
pubmed-article:7529493 | lifeskim:mentions | umls-concept:C1533691 | lld:lifeskim |
pubmed-article:7529493 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
pubmed-article:7529493 | pubmed:dateCreated | 1995-2-3 | lld:pubmed |
pubmed-article:7529493 | pubmed:abstractText | A peptide with a sequence corresponding to the highly conserved alpha-5 segment of the Cry delta-endotoxin family (amino acids 193-215 of Bacillus thuringiensis CryIIIA [Gazit and Shai (1993) Biochemistry 32, 3429-3436]), was investigated with respect to its interaction with insect membranes, cytotoxicity in vitro towards Spodoptera frugiperda (Sf-9) cells, and its propensity to form ion channels in planar lipid membranes (PLMs). Selectively labelled analogues of alpha-5 at either the N-terminal amino acid or the epsilon-amine of its lysine, were used to monitor the interaction of the peptides with insect membranes. The fluorescent emission spectra of the 7-nitrobenz-2-oxa-1,3-diazole-4-yl (NBD)-labelled alpha-5 peptides displayed a blue shift upon binding to insect (Spodoptera littoralis) mid-gut membranes, reflecting the relocation of the fluorescent probes to an environment of increased apolarity, i.e. within the lipidic constituent of the membrane. Moreover, midgut membrane-bound NBD-labelled alpha-5 peptides were protected from enzymic proteolysis. Functional characterization of alpha-5 has revealed that it is cytotoxic to Sf-9 insect cells, and that it forms ion channels in PLMs with conductances ranging from 30 to 1000 pS. A proline-substituted analogue of alpha-5 is less cytolytic and slightly more exposed to enzymic digestion. Molecular modelling utilizing simulated annealing via molecular dynamics suggests that a transbilayer pore may be formed by alpha-5 monomers that assemble to form a left-handed coiled coil of approximately parallel helices. These findings further support a role for alpha-5 in the toxic mechanism of delta-endotoxins, and assign alpha-5 as one of the transmembrane helices which form the toxic pore. The suggested role is consistent with the recent finding that cleavage of CryIVB delta-endotoxin in a loop between alpha-5 and alpha-6 is highly important for its larvicidal activity [Angsuthanasombat, Crickmore and Ellar (1993) FEMS Microbiol. Lett. 111, 255-262]. | lld:pubmed |
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pubmed-article:7529493 | pubmed:language | eng | lld:pubmed |
pubmed-article:7529493 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7529493 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:7529493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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pubmed-article:7529493 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:7529493 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:7529493 | pubmed:month | Dec | lld:pubmed |
pubmed-article:7529493 | pubmed:issn | 0264-6021 | lld:pubmed |
pubmed-article:7529493 | pubmed:author | pubmed-author:BachDD | lld:pubmed |
pubmed-article:7529493 | pubmed:author | pubmed-author:GazitEE | lld:pubmed |
pubmed-article:7529493 | pubmed:author | pubmed-author:SansomM SMS | lld:pubmed |
pubmed-article:7529493 | pubmed:author | pubmed-author:ChejanovskyNN | lld:pubmed |
pubmed-article:7529493 | pubmed:author | pubmed-author:KerrI DID | lld:pubmed |
pubmed-article:7529493 | pubmed:author | pubmed-author:ShaiYY | lld:pubmed |
pubmed-article:7529493 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:7529493 | pubmed:day | 15 | lld:pubmed |
pubmed-article:7529493 | pubmed:volume | 304 ( Pt 3) | lld:pubmed |
pubmed-article:7529493 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:7529493 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:7529493 | pubmed:pagination | 895-902 | lld:pubmed |
pubmed-article:7529493 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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