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Tyrosine 331 and phenylalanine 334 in Clostridium perfringens α‐toxin are essential for cytotoxic activity
Author(s) -
Jepson Marie,
Bullifent Helen L.,
Crane Dennis,
Flores-Diaz Marietta,
Alape-Giron Alberto,
Jayasekeera Pramukh,
Lingard Bryan,
Moss David,
Titball Richard W.
Publication year - 2001
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/s0014-5793(01)02385-7
Subject(s) - clostridium perfringens , toxin , cytotoxic t cell , tyrosine , phospholipase c , phospholipase , chemistry , biochemistry , biology , enzyme , bacteria , in vitro , genetics
Differences in the biological properties of the Clostridium perfringens phospholipase C (α‐toxin) and the C. bifermentans phospholipase C (Cbp) have been attributed to differences in their carboxy‐terminal domains. Three residues in the carboxy‐terminal domain of α‐toxin, which have been proposed to play a role in membrane recognition (D 269 , Y 331 and F 334 ), are not conserved in Cbp (Y, L and I respectively). We have characterised D 269 Y, Y 331 L and F 334 I variant forms of α‐toxin. Variant D 269 Y had reduced phospholipase C activity towards aggregated egg yolk phospholipid but increased haemolytic and cytotoxic activity. Variants Y 331 L and F 334 I showed a reduction in phospholipase C, haemolytic and cytotoxic activities indicating that these substitutions contribute to the reduced haemolytic and cytotoxic activity of Cbp.