Conformational Properties of the Neurotoxins and Cytotoxins Isolated from Elapid Snake Venoms

Dufton, Mark J.; Hider, Robert C.

doi:10.3109/10409238309102792

Cited by 211 publications

(133 citation statements)

References 144 publications

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“…2). Within experimental error, the spectra of Ea, and Ea~ superimposed, indicating that the dominant ~ sheet structure of erabutoxin [9] is preserved also in Ea~.…”

Section: Structurementioning

confidence: 81%

A recombinant snake neurotoxin generated by chemical cleavage of a hybrid protein recovers full biological properties

Boyot¹,

Pillet²,

Ducancel³

et al. 1990

FEBS Letters

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We previously reported the production of a fused snake neurotoxin composed of protein A and erabutoxin a in E. coli [1]. The hybrid had much lower toxicity and affinity for the acetylcholine nicotinic receptor than natural erabutoxin. By treating the hybrid with cyanogen bromide we generated a toxin which was purified in a single step by RP-HPLC. This compound, produced in a good yield, recovered all properties of native erabutoxin a, implying that the lower toxic activities of the hybrid were due to the bulky protein A and not to an incorrect folding of the toxin.This work serves as a basis for future studies of toxin-receptor interactions using engineered toxin mutants.

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“…2). Within experimental error, the spectra of Ea, and Ea~ superimposed, indicating that the dominant ~ sheet structure of erabutoxin [9] is preserved also in Ea~.…”

Section: Structurementioning

confidence: 81%

A recombinant snake neurotoxin generated by chemical cleavage of a hybrid protein recovers full biological properties

Boyot¹,

Pillet²,

Ducancel³

et al. 1990

FEBS Letters

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show abstract

“…Short-chain neurotoxins constitute a large family of structurally and functionally homologous proteins, the polypeptide chains (60-62 residues) of which differ in sequence (review [12]). To identify monoclonal antibodies that recognize conserved areas we screened antibody-secreting hybrid cells with two widely divergent short-chain neurotoxins.…”

Section: Resultsmentioning

confidence: 99%

A monoclonal antibody which recognized the functional site of snake neurotoxins and which neutralizes all short‐chain variants

et al. 1986

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We isolated a neurotoxin-specific monoclonal antibody (Mab) which is capable of recognizing and neutralizing all short-chain toxin variants that have been tested, including those with widely divergent sequences. The epitope incorporates the three invariant residues Lys-27, Trp-29 and Lys-47 which form part of the site by which the toxins bind to the nicotinic acetylcholine receptor. To our knowledge, this is the first Mab which possesses the universal capacity of neutralizing all natural variants of a toxic protein. Monoclonal antibody Toxin Acetylcholine receptor

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“…The antigenic determinant is located around the top of the central loop ( fig.3). On the basis of the sequence homology and chemical modification studies, the side chains of the amino acid residues located on one surface of the threestranded antiparallel-pleated P-sheet structure are suggested to be essential for neurotoxicity [ 12,131. These include K27, W29, D3 1, R36, and K47.…”

Section: Discussionmentioning

confidence: 99%

“…Both toxins contain 71 amino acid residues and only 5 amino acid residues of G32, S34, R53, D66 and D67 in TX B are replaced by A32, 134, K53, N66 and N67 in TX III. The primary structures of these long neurotoxins were compared [12,13] on the basis of the present results of the cross-reactivity experiments. The amino acid sequence common to cr-BTx, TX B, and Ls III was found to be C33-S34-S35-R36-G37-K38.…”

Section: Localization Of the Antigenic Determinantmentioning

confidence: 99%

Neutralizing monoclonal antibody specific for α‐bungarotoxin: Preparation and characterization of the antibody, and localization of antigenic region of α‐bungarotoxin

et al. 1989

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We prepared an a-bungarotoxin-specific monoclonal antibody that neutralizes the biological activity of the toxin in vivo. The antigenic determinant combining specifically with this antibody was determined on the basis of cross-reaction experiments using three other long neurotoxins and peptide fragments of a-bungarotoxin. The antigenic determinant was located on the peptide fragment containing S34-S35-R36-G37-K38, which forms a part of the expected site that binds to the acetylcholine receptor proteins Monoclonal antibody; Bungarotoxin, a-; Antigenic determinant

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Conformational Properties of the Neurotoxins and Cytotoxins Isolated from Elapid Snake Venoms

Cited by 211 publications

References 144 publications

A recombinant snake neurotoxin generated by chemical cleavage of a hybrid protein recovers full biological properties

A recombinant snake neurotoxin generated by chemical cleavage of a hybrid protein recovers full biological properties

A monoclonal antibody which recognized the functional site of snake neurotoxins and which neutralizes all short‐chain variants

Neutralizing monoclonal antibody specific for α‐bungarotoxin: Preparation and characterization of the antibody, and localization of antigenic region of α‐bungarotoxin

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