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J Bacteriol. 1968 March; 95(3): 1153-1168
Copyright © 1968 American Society for Microbiology. All Rights Reserved.

Interaction of Staphylococcal {alpha}-Toxin with Artificial and Natural Membranes1

John H. Freer, John P. Arbuthnott2 and Alan W. Bernheimer

a Department of Microbiology, New York University School of Medicine, New York, New York 10016

ABSTRACT

Comparison of hemolytic activity and chromate-releasing activity of partially purified preparations of staphylococcal {alpha}-toxin indicated the presence of a lytic factor other than {alpha}-toxin. This lytic release factor (RF) was isolated from the preparations and was shown to be active against both lipid spherules and erythrocytes. Heat-purified {alpha}-toxin (HP {alpha}-toxin) disrupted spherules, with the formation of fragments which always showed the presence of ring structures similar in dimensions (ca. 90 A) to pure {alpha} 12S-toxin. The interaction of HP {alpha}-toxin with spherules was accompanied by loss of hemolytic activity and adsorption of toxic protein. The {alpha} 12S-toxin, although only weakly hemolytic, was shown to be lytic for spherules. An {alpha} 12S-free toxin rapidly disrupted spherules, with formation of fragments with attached rings similar in dimensions to the {alpha} 12S molecule. Lipid monolayer experiments showed that HP {alpha}-toxin could penetrate lipid monolayers by virtue of a hydrophobic interaction. Effects of HP {alpha}-toxin on rabbit and human erythrocyte ghosts were similar to its effects on spherules, in that rings appeared on membrane fragments. Toxin-lysed rabbit erythrocytes showed similar rings on the resulting membrane fragments. However, rings were not seen on toxin-treated rabbit erythrocytes in the prelytic lag phase; this result and the fact that human erythrocytes are largely insensitive to {alpha}-toxin were interpreted as evidence against a lytic mechanism involving ring formation as the primary event. Rings were interpreted as toxin polymers similar to {alpha} 12S molecules, formed from specifically orientated active toxin molecules at the surface of lipid structures. Possible mechanisms for toxin lysis of spherules and erythrocytes are discussed.

FOOTNOTES

2 Present address: Department of Microbiology, The University, Glasgow, W1, Scotland.

1 Part of this work was presented at the 154th national meeting of the American Chemical Society, Chicago, Ill., September, 1967.

J Bacteriol. 1968 March; 95(3): 1153-1168
Copyright © 1968 American Society for Microbiology. All Rights Reserved.



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