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Tight junctions. Structural insight into tight junction disassembly by Clostridium perfringens enterotoxin
Yasunori Saitoh1, Hiroshi Suzuki2, Kazutoshi Tani2
1Cellular and Structural Physiology Institute, Nagoya University, Chikusa, Nagoya 464-8601, Japan. Department of Basic Medical Science, Graduate School of Pharmaceutical Science, Nagoya University, Chikusa, Nagoya 464-8601, Japan.
Science (New York, N.Y.)
|February 14, 2015
Summary
Clostridium perfringens enterotoxin (C-CPE) binds claudin-19, disrupting tight junctions. Structural analysis reveals C-CPE interaction displaces a key helix, explaining TJ disassembly and increased permeability.
Area of Science:
- Molecular biology
- Structural biology
- Cell biology
Background:
- Clostridium perfringens enterotoxin (C-CPE) targets claudins, leading to tight junction (TJ) disassembly and increased epithelial permeability.
- Understanding the molecular interactions between C-CPE and claudins is crucial for elucidating C-CPE's pathogenic mechanisms.
Purpose of the Study:
- To determine the high-resolution structure of the complex formed between mammalian claudin-19 and C-CPE.
- To elucidate the structural basis for C-CPE-mediated disruption of tight junctions.
Main Methods:
- X-ray crystallography was used to obtain the structure of the claudin-19/C-CPE complex at 3.7 Å resolution.
Main Results:
- The structure reveals extensive hydrophobic and hydrophilic interactions between C-CPE and the extracellular segments of claudin-19.
- A critical extracellular helix, essential for TJ strand assembly in claudins, was absent in the claudin-19/C-CPE complex structure.
- This absence suggests that C-CPE binding displaces this helix, potentially leading to TJ disassembly.
Conclusions:
- The C-terminal region of C-CPE interacts with claudin-19, disrupting TJ structure.
- Displacement of a critical extracellular helix by C-CPE binding is a likely mechanism for C-CPE-induced tight junction disassembly and increased paracellular permeability.
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