Identification of peptidoglycan recognition proteins in hemocytes and kidney of common periwinkle Littorinalittorea

Peptidoglycan Recognition Proteins (PGRPs) are a diverse group of proteins involved in innate immunity. In particular, PGRPs have been shown to participate in immune pattern recognition in various mollusks. However, they have not been described in Caenogastropoda, a large molluscan group comprising sea, freshwater and land snails. In this study, four short PGRPs with molecular weights ranging from 21 to 34 kDa and their isoforms were identified and structurally characterized in the kidney and hemocytic transcriptomes of a caenogastropod mollusk Littorina littorea. All of them (LlPGRP1-4) are secretory, possess a signal peptide and a characteristic N-terminal N-acetylmuramoyl-l-alanine amidase (Ami) domain with conserved Zn²⁺ binding- and amidase catalytic sites. The shortest proteins, LlPGRP1 and LlPGRP2, have no additional conserved motifs on the N-terminus. In longer and most abundantly expressed LlPGRP3 and LlPGRP4 the Ami-domain is combined with an N-terminal SH3-domain and a cysteine-rich motif, respectively. Expression analysis showed that LlPGRPs of the common periwinkle were uninvolved in the immune response to infection with trematode Himasthla elongata though they might act in antibacterial defense.