Expression of A Chain and B Chain of β-Bungarotoxin from Taiwan Banded Krait: The Functional Implication of the Interchain Disulfide ... View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2001-07

AUTHORS

Pei-Fung Wu, Long-Sen Chang

ABSTRACT

β-Bungarotoxin (β-Bgt), the main presynaptic neurotoxin purified from the venom of Bungarus multicinctus, consists of two dissimilar polypeptide chains, the A chain and B chain, cross-linked by an interchain disulfide bond. The A and B chain cDNAs were subcloned into expression vectors pT7-7 and pET20b(+), respectively, and transformed into Escherichia coli strain BL21(DE3). The expressed protein was isolated from the inclusion bodies of E. coli and subjected to refolding into its folded structure. The yields of the refolded A and B chains increased markedly by at least 100-fold after substituting Ser for Cys15 of A chain and Cys55 of B chain, which formed an interchain disulfide bond. Either the A(C15S) chain or B(C55S) chain alone or in combination cannot exhibit the phospholipase A2 activity or synaptosome binding activity of β-Bgt. Nevertheless, the results of competitive enzyme-linked immunoassay, CD spectra, and fluorescence measurement revealed that the A(C15S) chain and B(C55S) chain possessed a native-like structure like the subunits of native β-Bgt. Moreover, the interfacial interaction between the A and B chains explored by glutaraldehyde cross-linking revealed the essential aspects of the intact interchain disulfide bond in this interaction. This suggests that the formation of the interchain disulfide bond should not be a crucial step for the formation of folded A and B chains in the venom glands, and that the integrity of the interchain disulfide linkage favors the subunit interaction that consequently fulfills the functional mechanism of β-Bgt. More... »

PAGES

413-421

Identifiers

URI

http://scigraph.springernature.com/pub.10.1023/a:1012237005574

DOI

http://dx.doi.org/10.1023/a:1012237005574

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1046741131

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/11732693


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