Molecular cloning and characterisation of two homologues of Mannose-Binding Lectin in rainbow trout.

Mannose-binding lectin (MBL) is a C-type lectin which participates in the innate immune system as an activator of the complement system and as opsonin after binding to certain carbohydrate structures on microorganisms and pathogens. C-type lectins are all Ca(2+)-dependent molecules and they share a tightly folded carbohydrate recognition domain (CRD). In this report the isolation and characterisation of cDNA transcripts encoding two mannose-binding lectin isoforms MBL-1 and MBL-2 from rainbow trout (Oncorhynchus mykiss) is presented. The deduced amino acid sequences of trout MBL-1 and MBL-2 (185 and 186 aa, respectively) present 83% identity to each other, exhibiting the highest identity score 46, 46 and 42% with the Atlantic salmon, shishamo smelt and zebrafish counterparts, respectively. The identity to birds and mammalian MBLs ranges from 25 to 33%. The trout MBL-1 and MBL-2 contain the EPN motif of mannose-binding C-type lectins, important for mannose specificity and they are expressed exclusively in liver and spleen, respectively.