Characterization of non-lytic cytolysin-membrane intermediates

In order to understand the nature of cytolysin-membrane interactions, the characteristics of stable, non-lytic cytolysin-target cell intermediates formed at low ionic strength, neutral pH, and at physiological ionic strength, pH 6.0, were examined. Protease treatment of cytolysin-RBC intermediates f...

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Published inMolecular immunology Vol. 28; no. 11; p. 1263
Main Authors Kuta, A E, Bashford, C L, Pasternak, C A, Reynolds, C W, Henkart, P A
Format Journal Article
LanguageEnglish
Published England 01.11.1991
Subjects
Animals
Cell Membrane - drug effects
Chymotrypsin - pharmacology
Cytotoxins - chemistry
Cytotoxins - pharmacology
Hemolysis - drug effects
Humans
Hydrogen-Ion Concentration
In Vitro Techniques
Mice
Phosphatidylcholines - pharmacology
Phosphatidylserines - pharmacology
Pronase - pharmacology
Rats
Sodium Chloride - pharmacology
Sphingomyelins - pharmacology
Trypsin - pharmacology
Tumor Cells, Cultured
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Summary:In order to understand the nature of cytolysin-membrane interactions, the characteristics of stable, non-lytic cytolysin-target cell intermediates formed at low ionic strength, neutral pH, and at physiological ionic strength, pH 6.0, were examined. Protease treatment of cytolysin-RBC intermediates formed at low ionic strength inhibited subsequent hemolysis when the intermediates were exposed to physiological ionic strength and pH. Similarly, when such intermediates were treated with anti-granule and anti-cytolysin antibodies a significant dose-dependent inhibition of hemolysis was observed. These results suggested that in this non-lytic state the cytolysin molecule was exposed on the RBC surface. If low ionic strength or pH 6.0 generated intermediates were washed in 0.5 M NaCl, hemolytic activity was greatly reduced and cytolysin activity could be recovered from the medium. In addition to RBC, both murine (Yac-1 and Lettre ascites) and human (K562) tumor targets formed cytolysin-target cell intermediates at low ionic strength and at low pH. Multilamellar vesicles composed of either phosphatidylcholine, sphingomyelin or phosphatidylserine inhibited the binding of cytolysin to RBC at both low ionic strength and pH 6.0 indicating a lack of polar head group specificity for cytolysin binding.
ISSN:0161-5890
DOI:10.1016/0161-5890(91)90013-A