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Tolls/Toll-like receptors (TLRs) play a key role in innate immunity by detecting the invading microbes and subsequently activating downstream signaling cascades. In this study, two new molluscan Toll members (designed as  HcToll6  and  HcToll7 ) were identified from triangle-shell pearl mussel ( Hyriopsis cumingii ). The obtained  HcToll6  full-length cDNA was 3207 bp consisting of a 2223 bp open reading frame (ORF) that encoded a peptide of 740 amino acids.  HcToll7  cDNA is a 3216 bp molecule that contains an ORF of 2139 bp encoding a protein of 712 amino acids. The deduced  HcToll6  and  HcToll7  proteins share two common structures: extracellular leucine-rich repeat (LRR) domains and intracellular Toll/interleukin-1 receptor (TIR) domain. Quantitative real-time PCR results showed that  HcToll6  and  HcToll7  were mainly expressed in the hepatopancreas and the gills, and they responded rapidly to bacterial stimulation. RNA interference by dsRNA results revealed that  HcToll6  and  HcToll7  RNAi strongly decreased the expression of lysozyme ( HcLyso ) and defensin ( HcDef ) in the gills of RNAi-treated mussels with  Vibrio parahaemolyticus  challenge. As a pattern recognition receptor, the prokaryotic expressed the recombinant LRR domains of  HcToll6  and  HcToll7  (rHcToll6-LRR and rHcToll7-LRR) could bind to Gram-positive and Gram-negative bacteria and had a strong tendency to recognize lipopolysaccharide (LPS) and peptidoglycan (PNG). rHcToll6-LRR and rHcToll7-LRR exhibited a significant  in vitro  bactericidal activity against  V. parahaemolyticus  and  Staphylococcus aureus . These findings provide useful information to characterize Tolls in mussels.

Molecular Characterization of Two Toll Receptors in Hyriopsis cumingii and Their Potential Roles in Antibacterial Response