Identification and functional characterization of bactericidal permeability/ increasing protein (BPI) from frog Nanorana yunnanensis (Paa yunnanensis)

Bactericidal permeability/increasing protein (BPI) and lipopolysaccharide-binding protein (LBP) have been most extensively studied in mammals, but little information is available regarding BPI and LBP in Amphibia. In this study we showed that the cDNA of BPI in the frog N. yunnanensis (P. yunnanensis) encoded a 490-amino-acid-long protein, the predicted tertiary structure appears closely similar to mammalian BPIs in terms of sequence and structure. Like mammalian BPI gene, the frog gene nybpi was widely expressed in various tissues and was inducible by challenge with LPS or Gram-negative bacterium. We also showed that recombinant NyBPI, resembling mammalian BPIs, specifically binds with LPS. In addition, the recombinant NyBPI displayed antibacterial activity against Gram-negative bacteria Vibrio anguillarum in a dose-dependent manner. These results indicate that NyBPI may play an important role in an immune response against bacteria in amphibians.