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Intermolecular ionic interactions serve as a possible switch for stem release in the staphylococcal bi-component toxin for β-barrel pore assembly

Author:
Takeda, Kein, Tanaka, Yoshikazu, Abe, Naoki, Kaneko, Jun
Source:
Toxicon 2018 v.155 pp. 43-48
ISSN:
0041-0101
Subject:
electrostatic interactions, erythrocytes, hemolysis, mutation
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.
Agid:
6191153