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.

40S ribosomal protein S18 is a novel maternal peptidoglycan-binding protein that protects embryos of zebrafish from bacterial infections.

Previous studies have shown that ribosomal proteins play important roles in ribosome assembly and protein translation, but other biological functions remain ill-defined. Here it is clearly demonstrated that RPS18 is a newly identified PGN-binding protein which is present abundantly in the eggs/embryos of zebrafish. Recombinant RPS18 not only identifies the bacterial signature molecule PGN, LPS, and LTA, and binds the bacteria as a pattern recognition receptor, but also kills the Gram-positive and Gram-negative bacteria as an antibacterial effector molecule. What is important is that, we reveal that microinjection of rRPS18 into early embryos significantly improved the resistance of the embryos against pathogenic Aeromonas hydrophila challenge, and co-injection of anti-RPS18 antibody could markedly reduced this improved bacterial resistance. In summary, these results indicate that RPS18 is a maternal immune factor that can protect the early embryos of zebrafish against pathogenic attacks. This work also provides another angle for understanding the biological functions of ribosomal proteins.