A Crustin from Hydrothermal Vent Shrimp: Antimicrobial Activity and Mechanism

Crustin is a type of antimicrobial peptide and plays an important role in the innate immunity of arthropods. We report here the identification and characterization of a crustin (named Crus1) from the shrimp Rimicaris sp. inhabiting the deep-sea hydrothermal vent in Manus Basin (Papua New Guinea). Crus1 shares the highest identity (51.76%) with a Type I crustin of Penaeus vannamei and possesses a whey acidic protein (WAP) domain, which contains eight cysteine residues that form the conserved 'four-disulfide core' structure. Recombinant Crus1 (rCrus1) bound to peptidoglycan and lipoteichoic acid, and effectively killed Gram-positive bacteria in a manner that was dependent on pH, temperature, and disulfide linkage. rCrus1 induced membrane leakage and structure damage in the target bacteria, but had no effect on bacterial protoplasts. Serine substitution of each of the 8 Cys residues in the WAP domain did not affect the bacterial binding capacity but completely abolished the bactericidal activity of rCrus1. These results provide new insights into the characteristic and mechanism of the antimicrobial activity of deep sea crustins.

Automated summary

Crus1, a type of antimicrobial peptide from deep-sea shrimp, effectively kills Gram-positive bacteria by inducing membrane leakage and structure damage in a pH, temperature, and disulfide linkage-dependent manner. Serine substitution of cysteine residues in the WAP domain does not affect bacterial binding capacity but completely abolishes the bactericidal activity of rCrus1.