caa a22 4500 606230262 CHVBK 20210128101213.0 cr unu---uuuuu 210128e20150801xx s 000 0 eng 10.1007/s10695-015-0060-y doi (NATIONALLICENCE)springer-10.1007/s10695-015-0060-y Ferritin M of Paralichthys olivaceus possesses antimicrobial and antioxidative properties [Elektronische Daten] [Jing-jing Wang, Li Sun] Ferritin is an evolutionarily conserved protein that plays a vital role in maintaining iron homeostasis. In this study, we identified a ferritin M (PoFerM) from Japanese flounder (Paralichthys olivaceus) and analyzed its biological property. PoFerM is composed of 176 amino acid residues and contains the conserved ferroxidase diiron center and the ferrihydrite nucleation center typical of M ferritins. Expression of PoFerM occurred in multiple tissues and was most abundant in blood. Bacterial infection upregulated PoFerM expression in head kidney, spleen, and liver in a time-dependent manner. Recombinant PoFerM (rPoFerM) purified from Escherichia coli exhibited iron-chelating activity and inhibited bacterial growth, whereas rPoFerMM, the mutant protein that bears alanine substitution at two conserved residues of the ferroxidase center and the ferrihydrite nucleation center, failed to do so. Oxidative protection analysis showed that rPoFerM, but not rPoFerMM, was able to alleviate the deleterious effect of H2O2-induced free radicals on plasmid DNA and primary flounder cells. Together these results indicate that PoFerM is an iron chelator with antimicrobial and antioxidative properties, all which depend on the conserved ferroxidase center and the ferrihydrite nucleation site. Springer Science+Business Media Dordrecht, 2015 Antimicrobial nationallicence Antioxidative nationallicence Ferritin nationallicence Iron binding nationallicence Paralichthys olivaceus nationallicence Wang Jing-jing Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Road, 266071, Qingdao, People's Republic of China aut Sun Li Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Road, 266071, Qingdao, People's Republic of China aut Fish Physiology and Biochemistry Springer Netherlands 41/4(2015-08-01), 951-959 0920-1742 41:4<951 2015 41 10695 https://doi.org/10.1007/s10695-015-0060-y text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 research-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s10695-015-0060-y text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Wang Jing-jing Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Road, 266071, Qingdao, People's Republic of China aut NATIONALLICENCE 700 1- Sun Li Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences, 7 Nanhai Road, 266071, Qingdao, People's Republic of China aut NATIONALLICENCE 773 0- Fish Physiology and Biochemistry Springer Netherlands 41/4(2015-08-01), 951-959 0920-1742 41:4<951 2015 41 10695