TLR3 forms a laterally aligned multimeric complex along double-stranded RNA for efficient signal transduction

Kentaro Sakaniwa, Akiko Fujimura, Takuma Shibata, Hideki Shigematsu, Toru Ekimoto, Masaki Yamamoto, Mitsunori Ikeguchi, Kensuke Miyake, Umeharu Ohto () and Toshiyuki Shimizu ()
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Kentaro Sakaniwa: The University of Tokyo, 7-3-1 Hongo
Akiko Fujimura: The University of Tokyo, 7-3-1 Hongo
Takuma Shibata: The University of Tokyo, 4-6-1 Shirokanedai
Hideki Shigematsu: RIKEN SPring-8 Center, 1-1-1 Kouto
Toru Ekimoto: Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku
Masaki Yamamoto: RIKEN SPring-8 Center, 1-1-1 Kouto
Mitsunori Ikeguchi: Yokohama City University, 1-7-29, Suehiro-cho, Tsurumi-ku
Kensuke Miyake: The University of Tokyo, 4-6-1 Shirokanedai
Umeharu Ohto: The University of Tokyo, 7-3-1 Hongo
Toshiyuki Shimizu: The University of Tokyo, 7-3-1 Hongo

Nature Communications, 2023, vol. 14, issue 1, 1-8

Abstract: Abstract Toll-like receptor 3 (TLR3) is a member of the TLR family, which plays an important role in the innate immune system and is responsible for recognizing viral double-stranded RNA (dsRNA). Previous biochemical and structural studies have revealed that a minimum length of approximately 40–50 base pairs of dsRNA is necessary for TLR3 binding and dimerization. However, efficient TLR3 activation requires longer dsRNA and the molecular mechanism underlying its dsRNA length-dependent activation remains unknown. Here, we report cryo-electron microscopy analyses of TLR3 complexed with longer dsRNA. TLR3 dimers laterally form a higher multimeric complex along dsRNA, providing the basis for cooperative binding and efficient signal transduction.

Date: 2023
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-35844-2

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DOI: 10.1038/s41467-023-35844-2

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