Crustins are an antimicrobial peptide (AMP) family that plays an important role in innate immunity in crustaceans. It is important to discover new AMPs from natural sources to expand the current database. Here, we identified and characterized a new crustin family member, named Crus1, from . Crus1 shares high identity (48.10%) with , a Type I crustin of that possesses a whey acidic protein (WAP) domain. Crus1 contains 237 amino acids and eight cysteine residues forming conserved 'four-disulfide core' structure. Our recombinant Crus1 (rCrus 1) could inhibit the growth of two Gram-positive bacteria (, sp. T2) and four Gram-negative bacteria (, , , ) with a minimum inhibitory concentration of 3.5-28 μM. It can further induce agglutination of both Gram-positive and Gram-negative bacteria. rCrus1 can bind to bacteria and damage bacterial cell membranes. Furthermore, rCrus1 disrupted biofilm development of and . Our discovery and characterization of this new crustin can be further optimized as a good alternative to antibiotics.
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| http://dx.doi.org/10.3390/pharmaceutics14020413 | DOI Listing |
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