UNASSIGNED: Crustins are cationic cysteine-rich antimicrobial peptides (AMPs) that contain multiple domains (glycine-rich, cysteine-rich, or proline-rich) at the N-terminus and whey acidic protein (WAP) domains at the C-terminus. Crustins have multiple functions, including protease inhibition and antimicrobial activity. Other functions of crustins need to be clarified. In this study, a novel crustin with a cysteine-rich region, and a single WAP domain, belonging to type I crustins, was identified in @entity20481 and designated as MjCru I-1. MjCru I-1 was expressed in various tissues. The expression of MjCru I-1 was upregulated in the hemocytes of shrimp challenged with bacteria. MjCru I-1 could bind to bacteria by binding to the cell wall molecules of the bacteria, such as lipopolysaccharide (LPS), peptidoglycan (PGN), and lipoteichoic acid (LTA). The synthesized WAP domain of MjCru I-1 but not synthesized Cys-rich domain has antibacterial and agglutinative activities. Scanning electron microscope assay showed that the bacterial cells treated with sMjCru I-1 appeared to be disrupted and cracked compared with those of the control samples. The knockdown of MjCru I-1 could reduce bacterial clearance and injection of MjCru I-1 could significantly increase the survival rate of shrimp infected with @entity2551 and @entity794 compared with those of the control samples. Further study discovered that MjCru I-1 could increase the hemocyte phagocytosis against @entity2551 and @entity794 . These results suggest that MjCru I-1 has dual functions, bactericidal and phagocytosis promoting activities, in the antibacterial immunity of shrimp.

A novel crustin from XXXX promotes hemocyte phagocytosis.

@entity2551 :: ('55601', 'Species') :: ['Vibrio anguillarum', 'V.  anguillarum'] @entity794 :: ('1280', 'Species') :: ['Staphylococcus aureus', 'S.  aureus'] @entity20481 :: ('27405', 'Species') :: ['Marsupenaeus japonicus']
@entity20481 :: (27405,Species) :: ['Marsupenaeus japonicus']
