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Crustins are crucial antimicrobial peptides in shrimp and play very important roles in innate immunity. In this research, a Type I crustin from  Penaeus monodon  (Carcinin Pm 1) contained 108 residues was studied. The first 16 residues are signal peptide. It contained ten cysteines but did not form an intact whey acidic protein (WAP) domain. Carcinin Pm 1 was observed to widely distribute in all tissues, while highly expressed in intestine. The expression level of Carcinin Pm 1 in hepatopancreas was up-regulated 12- 20 times during 4-12h post challenged by  Vibrio parahaemolyticus . And the transcription in heart, stomach and gills was also significantly enhanced at 4h post challenge. The mature peptide was expressed successfully in  Eschericha coli  by fusing to a SUMO protein, with protein production around 8 mg/mL. After cleavage with SUMO protease, carcininPm1 was obtained indicating its potential applications.

Anti-Vibrio Response of CarcininPm 1 from Penaeus monodon and Its Heterologous Expression