C-type lectin with a QPN motif from swimming crab Portunus trituberculatus displays broad nonself-recognition ability and functions as an opsonin.

In the immune system, C-type lectins, as pattern recognition receptors, have an important function. Carbohydrate-recognition domains (CRDs) endow C-type lectins with the function of recognizing and scavenging non-self factors. In the present study, a new C-type lectin (designated as PtCTL-9 according to the order of discovery) from swimming crab (Portunus trituberculatus) was characterized. QPN (Gln-Pro-Asn) and FHS (Phe-His-Ser) were identified as the key motifs that determine carbohydrate binding. Motif QPN was mutated to QPD (Gln-Pro-Asp) (M1) and EPN (Glu-Pro-Asn) (M2) to study its immune function and for comparative analysis. The results showed that PtCTL-9 displayed broad non-self immunity. PtCTL-9 could also function as an opsonin to promote phagocytosis and the in vitro encapsulation of hemocytes. These results indicated that PtCTL-9 has an extensive nonself-recognition ability, regulates pathogen clearance, and its QPN motif is important in PtCTL-9's immune function. • A C-type lectin PtCTL-9 with a novel QPN motif was identified from Portunus trituberculatus. • PtCTL-9 possessed strong binding activity to nonself particles while its two mutants displayed weak binding activity. • PtCTL-9 inhibited the growth of S. cerevisiae. • PtCTL-9 promoted phagocytosis and encapsulation activity of hemocytes in vitro. [ABSTRACT FROM AUTHOR]