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* Department of Bacterial Toxinology and A cDNA encoding the Clostridium perfringens enterotoxin receptor gene (CPE-R) was cloned
from an expression library of enterotoxin-sensitive Vero cells. The nucleotide sequence of CPE-R showed
that the enterotoxin receptor consists of 209 amino acids with a calculated molecular mass of 22,029 D. This
receptor is highly hydrophobic, contains four putative
transmembrane segments, and has significant similarity to the rat androgen withdrawal apoptosis protein RVP1
and the mouse oligodendrocyte specific protein, the
functions of which are unknown. The expression of
CPE-R was detected in the enterotoxin-sensitive Vero,
Hep3B, and Intestine 407 cell lines, but not in the enterotoxin-insensitive K562 and JY cell lines. The CPE-R
gene product expressed in enterotoxin-resistant L929
cells bound to enterotoxin specifically and directly and with high affinity and rendered the cells sensitive to the
toxin, indicating that the cloned receptor is functional.
Results showed that enterotoxin could not assemble
into a complex with a defined structure unless it interacted with the receptor. From these results, it is proposed that the enterotoxin receptor is required for both target cell recognition and poreformation in the cell
membrane.
Department of Immunoregulation, Research Institute for Microbial Diseases, Osaka
University, Osaka 565, Japan
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