Identification of zebrafish GIGYF2 presents in egg/embryo as an antibacterial protein

Previous studies have shown that GIGYF2 plays multiple roles, but its overall biological function remains poor-defined. Here we clearly demonstrated that zebrafish (Danio rerio) GIGYF2 has GYF domain and gigyf2 mainly expressed in caudal fin, brain, eyes and testis in a tissue specific manner, and was most abundant in brain and testis. GYF domain of GIGYF2 was a peptidoglycan (PGN), lipopolysaccharide (LPS)- and lipoteichoic acid (LTA)- binding protein abundantly stored in the testis/embryos of zebrafish, acting not only as a pattern recognition receptor, but also as an effector molecule, capable of inhibiting the growth of gram-positive and -negative bacteria. Furthermore, we reveal that the residues of GIGYF2 positioned at 582–601 and 848–865 were indispensable for GIGYF2 antibacterial activity. Additionally, site-directed mutation could improve antibacterial activities. Collectively, our results indicate that zebrafish GYF domain of GIGYF2 recognize bacterial characteristic molecules PGN, LPS and LTA, and directly kill bacteria as an antibacterial effector. This work also provides another angle for understanding the biological roles of GIGYF2. •GIGYF2 is a newly identified bacteria-binding protein present abundantly in the egg/embryos of zebrafish.•GIGYF2 is a newly identified PGN-, LPS- and LTA-binding protein present abundantly in the eggs/embryos of zebrafish.•GYF domain acts as a pattern recognition receptor and functions as an antibacterial effector molecule killing the bacteria.•Site-directed mutation could improve antibacterial activity of peptidesbeing applied to resist aquatic bacterial diseases.