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Hydrophobic photolabelling of pertussis toxin subunits interacting with lipids
Author(s) -
Montecucco Cesare,
Tomasi Maurizio,
Schiavo Giampietro,
Rappuoli Rino
Publication year - 1986
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(86)80105-3
Subject(s) - pertussis toxin , toxin , micelle , chemistry , phospholipid , membrane , biochemistry , penetration (warfare) , biophysics , g protein , biology , receptor , organic chemistry , operations research , aqueous solution , engineering
The hydrophobic surfaces presumably involved in the membrane interaction of pertussis toxin have been mapped by a new detergent‐binding assay. This is based on the interdispersion among detergent micelles of trace amounts of radioactive photoreactive phospholipid analogues, able to cross‐link to the protein thereby labelling its detergent‐binding domains. The assay has proven to be very sensitive. Subunits B 1 , B 2 and B 3 of pertussis toxin were found to interact with the lipid micelles suggesting that they may be involved in the membrane penetration step of the intoxication process.