E. coli a-hemolysin: a membrane-active protein toxin

Brazilian Journal of Medical and Biological Research

F.m. Goñi¹  H. Ostolaza¹ 

[1] ,Universidad del País Vasco

关键词: alpha-hemolysin;    bacterial toxins;    RTX toxins;    lipid-protein interactions;    calcium-binding proteins;    model membranes;   

DOI  :  10.1590/S0100-879X1998000800002

来源: SciELO

【 摘 要 】

Alpha-Hemolysin is synthesized as a 1024-amino acid polypeptide, then intracellularly activated by specific fatty acylation. A second activation step takes place in the extracellular medium through binding of Ca2+ ions. Even in the absence of fatty acids and Ca2+ HlyA is an amphipathic protein, with a tendency to self-aggregation. However, Ca2+-binding appears to expose hydrophobic patches on the protein surface, facilitating both self-aggregation and irreversible insertion into membranes. The protein may somehow bind membranes in the absence of divalent cations, but only when Ca2+ (or Sr2+, or Ba2+) is bound to the toxin in aqueous suspensions, i.e., prior to its interaction with bilayers, can a-hemolysin bind irreversibly model or cell membranes in such a way that the integrity of the membrane barrier is lost, and cell or vesicle leakage ensues. Leakage is not due to the formation of proteinaceous pores, but rather to the transient disruption of the bilayer, due to the protein insertion into the outer membrane monolayer, and subsequent perturbations in the bilayer lateral tension. Protein or glycoprotein receptors for a-hemolysin may exist on the cell surface, but the toxin is also active on pure lipid bilayers.

【 授权许可】

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