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Updated: Feb 4, 2026

Deciphering the Molecular Mechanism and Function of Pore-Forming Toxins Using Leishmania major
Published on: October 28, 2022
Intermolecular ionic interactions serve as a possible switch for stem release in the staphylococcal bi-component
Kein Takeda1, Yoshikazu Tanaka2, Naoki Abe1
1Department of Microbial Biotechnology, Graduate School of Agricultural Sciences, Tohoku University, Aramaki Aza Aoba, Sendai 980-8572, Japan.
Abstract:
The β-strand stem release system of staphylococcal β-barrel pore-forming toxin γ-hemolysin was investigated. Mutations at K15 and R16 in the cap domain of Hlg2 decreased hemolytic activity more markedly than their effect on erythrocyte binding. In addition, D122N mutation of LukF prestem lost the activity with Hlg2 R16A, indicating that electrostatic interactions between residues in the Hlg2 cap and prestem of adjacent LukF in the ring-shaped complex might serve as a switch for stem release.
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