Abstract
Clostridium perfringens epsilon toxin (Etx) is an extremely
potent toxin, causing fatal enterotoxaemia in many animals.
Several amino acids in domains I and II have been proposed
to be critical for Etx to interact with MDCK cells. However,
the critical amino acids in domain III remain undefined.
Therefore, we assessed the effects of aromatic amino acids
in domain III on Etx activity in this study. All of the results
indicated that Y71 was critical for the cytotoxic activity of
Etx towards MDCK cells, and this activity was dependent
on the existence of an aromatic ring residue in position 71.
Additionally, mutations in Y71 did not affect the binding of
Etx to MDCK cells, indicating that Y71 is not a receptor binding
site for Etx. In summary, we identified an amino acid
in domain III that is important for the cytotoxic activity of
Etx, thereby providing information on the structure-function
relationship of Etx.
Citations
Citations to this article as recorded by

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