Campylobacter jejuni targets immunoglobulin-like receptor LMIR5

• C. jejuni interacts directly with C-type lectin and immunoglobulin-like receptors.
• C. jejuni interacts preferentially with LMIR5 among various receptors examined.
• C. jejuni activates transcriptional factor NFAT through DAP12-coupled LMIR5.
• LMIR5 recognizes proteins, RNA-associated proteins, and glycoconjugates.

Campylobacter jejuni causes gastroenteritis and Guillain-Barré syndrome. Host immunity plays an important role in the disease pathogenesis; however, little is known about the immune receptors for C. jejuni. We report here that C. jejuni targets C-type lectin (SIGNR1, SIGNR3) and immunoglobulin-like receptors (TREM2, TREM3, LMIR5, LMIR8). Among these, C. jejuni interacted preferentially with LMIR5, which was selected for further verification using reporter cells. LMIR5 ligation by C. jejuni activated transcriptional factor NFAT through adaptor protein DAP12. Furthermore, LMIR5 activators were identified as protein components, RNA-associated proteins, and 150-kDa high-molecular-weight glycoconjugates. This finding discloses potential receptors that might link C. jejuni to immunopathology.