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. 1976 Apr;13(4):1046–1053. doi: 10.1128/iai.13.4.1046-1053.1976

Interaction of purified leukocidin from Pseudomonas aeruginosa with Bovine polymorphonuclear leukocytes.

W Scharmann
PMCID: PMC420715  PMID: 819371

Abstract

The interaction of purified leukocidin from Pseudomonas aeruginosa, strain 158, with polymorphonuclear leukocytes of cattle (PMLC) was studied by using 125I-labeled toxin. According to the Scatchard plot, PMLC offered two binding sites for leukocidin: one at the surface of the plasma membrane, and a second one that presumably became accessible to the toxin in the course of the cytotoxic action. Toxin once fixed to PMLC at 37 C could not be detached from the cells by either chemical or mechanical treatment. However, active leukocidin was liberated if it was bound to PMLC at 4 C and the temperature of the cell suspension was subsequently increased to 37 C. In the presence of Ca2+, the velocity of toxin fixation was accelerated and the rate of fixation was increased. Preliminary investigations on the identification of the leukocidin-binding material indicated the leukocidin receptor to be an integral protein of the plasma membrane.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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