The Role Of Ferritins In Maintaining The Redox Balance Of Musca Domestica

Iron is an indispensable metal element in organisms and plays an important role in biological processes such as DNA synthesis and cell division.However,abnormally high levels of free iron in the organism induce a Fenton reaction,which induces the production of hydroxyl radicals?·OH?by H₂O₂,which causes oxidative damage to the body.Ferritin is a protein that stores iron in living organisms and plays an important role in maintaining iron homeostasis and immune defense in the body.Changes in ferritin content can measure the extent of the body's response to external stress environments.Housefly has a short life cycle and strong resistance to disease and stress,and has become an ideal model organism for studying innate immunity of insects.The Muscle ferritin gene?MdFers?was cloned and prokaryotically expressed in the laboratory,and its tissue distribution and expression pattern of bacterial stimulation were explored.Based on the above studies,this paper explores the immune function of housefly ferritin and the role of transferrin in iron balance in vivo.The research contents are as follows:1?The expression pattern of Musca domestica MdFerH and MdFerL under oxidative stress was analyzed by Western blot.It was found that the body significantly up-regulated ferritin expression when subjected to oxidative stress.2?The expression of MdFers in Musca domestica larvae was successfully disrupted by injection of dsRNA.The results showed that knocking down the expression of MdFers caused oxidative stress in the housefly,and the body's ability to resist bacterial infection decreased significantly.3?Using the constructed MdFers prokaryotic expression system to explore the ability of housefly ferritin to fight oxidative stress,it was found that expression of housefly ferritin can effectively improve the resistance of host bacteria to H₂O₂.4?The full-length cDNA sequence of the Musca domestica transferrin gene was obtained by PCR and RACE technology?Rapid-amplification of cDNA ends?and named MdTf.The sequence contains a 1128 bp open reading frame encoding 375 amino acids and the theoretical molecular weight of the MdTf protein is 42.8 kDa.Conserved domain prediction of MdTf revealed that it has a transferrin domain and belongs to the member of the transferrin superfamily.Purified housefly transferrin was obtained by prokaryotic expression,which laid a foundation for further investigation of transferrin function.