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The term "Clostridium perfringens cell surface receptors" does not refer to a single, specific molecule, but rather to several different cell surface receptors utilized by various toxins produced by Clostridium perfringens to gain entry into host cells. For example: - The **iota toxin** binds its B subunit (Ib) to an as-yet-uncharacterized cell surface receptor to facilitate entry and translocation of the enzymatic subunit (Ia), which ADP-ribosylates actin and disrupts the cytoskeleton, resulting in cell rounding and death[1][3]. The exact molecular identity of this cell surface receptor remains uncharacterized. - The **enterotoxin** (CpE) from C. perfringens specifically targets **claudin-3 and claudin-4** proteins on epithelial cells as functional receptors, leading to cytotoxicity and gastrointestinal disease[4]. - Other toxins (such as TcdA, TcdB, TpeL) may use additional protein receptors, including LDL-receptor-related protein-1 (LRP1), chondroitin sulfate proteoglycan 4 (CSPG4), poliovirus receptor-like 3 (PVRL3), and members of the Frizzled receptor family, but these are primarily associated with Clostridioides (formerly Clostridium) difficile and not classic C. perfringens strains[2]. Because multiple, structurally diverse receptors are involved and many have not yet been definitively identified for all C. perfringens toxins, the term is not a precise molecular entity and should not be treated as a canonical single target.
Mediates binding and entry of C. perfringens toxins (e.g., iota toxin, enterotoxin) by serving as the cellular docking site for the toxin's binding component[1][3][4]
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