Ferritin, an evolutionarily conserved
iron-binding protein, plays important roles in
iron storage and detoxification and in host immune response to invading stimulus as well. In the present study, we identified three
ferritin subunit analog cDNAs from Chinese giant salamander (Andrias davidianus). All the three
ferritin subunit cDNAs had a putative
iron responsive
element in the 5'-untranslated region. Two deduced
ferritin subunits (designated as cgsFerH and cgsFerM) had the highest identity of 90% to H type subunit of vertebrate
ferritins, while another deduced
ferritin subunit (designated as cgsFerL) had the highest identity of 84% to L type subunit of vertebrate
ferritins. The Chinese giant salamander
ferritin (cgsFer) was widely expressed in various tissues, with highest expression for cgsFerH and cgsFerL in liver and highest expression for cgsFerM in spleen.
Infection of Chinese giant salamander with A. davidianus ranavirus showed significant induction of cgsFer expression. Both
lipopolysaccharide and
iron challenge drastically augmented cgsFer expression in the splenocytes and hepatocytes from Chinese giant salamander. In addition, recombinant cgsFers bound to ferrous
iron in a dose-dependent manner, with significant
ferroxidase activity. Furthermore, the recombinant cgsFer inhibited the growth of the pathogen Vibrio anguillarum. These results indicated that cgsFer was potential candidate of immune molecules involved in
acute phase response to invading microbial pathogens in Chinese giant salamander possibly through its regulatory roles in
iron homeostasis.