Identification, expression and antibacterial activity of a tachylectin-related homolog in amphioxus Branchiostoma belcheri with implications for involvement of the digestive system in acute phase response.

Tachylectin-related proteins have been identified in various organisms from slime molds to sponges to bony fish, yet little is known to date about it in protochordate amphioxus, an important organism occupying a nodal position from invertebrates to vertebrates. Moreover, if the protein acts as an immune-relevant molecule remains controversial. Here we demonstrated the presence of a tachylectin-related gene in Branchiostoma belcheri. The predicted gene product, termed BbTL, consists of 305 amino acids with a putative N-terminal signal peptide and 6 tachylectin-typical tandem repeats of 30-33 amino acids. In situ hybridization histochemistry indicates a tissue-specific expression pattern of BbTL in adult amphioxus with the most abundant expression in the hepatic caecum and hind-gut. Quantitative real-time PCR reveals that challenge with LPS results in a significant up-regulation of BbTL expression in the guts. In addition, the recombinant BbTL expressed in Pichia pastoris is able to inhibit the growth of Gram-negative bacterium Escherichia coli in a dose-dependent manner. All these suggest that BbTL, like most other tachylectin-related proteins, is involved in the host immune defense, and the digestive system of B. belcheri appears the major immune tissue responding to LPS challenge.