1. Molecular Characterization and Functional Analysis of a Ferritin Heavy Chain Subunit from the Eri-Silkworm, Samia cynthia ricini
- Author
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Zhen Li, Jia-Ping Xu, Li Bing, Hai-Zhong Yu, Dong-Qiong Fei, Li-ang Yang, Azharuddin Muhammad, Yan Ma, Shang-Zhi Zhang, and Jie Wang
- Subjects
0106 biological sciences ,0301 basic medicine ,Models, Molecular ,Protein Conformation ,01 natural sciences ,immune response ,lcsh:Chemistry ,Iron-Binding Proteins ,Hemolymph ,Cloning, Molecular ,lcsh:QH301-705.5 ,Spectroscopy ,Phylogeny ,chemistry.chemical_classification ,iron binding capacity ,General Medicine ,Computer Science Applications ,Amino acid ,Real-time polymerase chain reaction ,Biochemistry ,Protein subunit ,ferritin ,Samia cynthia ricini ,anti-oxidation activity ,Biology ,Catalysis ,Article ,Inorganic Chemistry ,Immunomodulation ,03 medical and health sciences ,Structure-Activity Relationship ,Bombyx mori ,Consensus Sequence ,Animals ,Protein Interaction Domains and Motifs ,Amino Acid Sequence ,Physical and Theoretical Chemistry ,Molecular Biology ,Innate immune system ,Base Sequence ,Organic Chemistry ,fungi ,Midgut ,Sequence Analysis, DNA ,biology.organism_classification ,Bombyx ,Ferritin ,010602 entomology ,Protein Subunits ,030104 developmental biology ,chemistry ,lcsh:Biology (General) ,lcsh:QD1-999 ,Ferritins ,biology.protein - Abstract
Ferritins are conserved iron-binding proteins that are primarily involved in iron storage, detoxification and the immune response. Despite the importance of ferritin in organisms, little is known about their roles in the eri-silkworm (Samia cynthia ricini). We previously identified a ferritin heavy chain subunit named ScFerHCH in the S. c. ricini transcriptome database. The full-length S. c. ricini ferritin heavy chain subunit (ScFerHCH) was 1863 bp and encoded a protein of 231 amino acids with a deduced molecular weight of 25.89 kDa. Phylogenetic analysis revealed that ScFerHCH shared a high amino acid identity with the Bombyx mori and Danaus plexippus heavy chain subunits. Higher ScFerHCH expression levels were found in the silk gland, fat body and midgut of S. c. ricini by reverse transcription quantitative polymerase chain reaction (RT-qPCR) and Western blotting. Injection of Staphylococcus aureus and Pseudomonas aeruginosa was associated with an upregulation of ScFerHCH in the midgut, fat body and hemolymph, indicating that ScFerHCH may contribute to the host’s defense against invading pathogens. In addition, the anti-oxidation activity and iron-binding capacity of recombinant ScFerHCH protein were examined. Taken together, our results suggest that the ferritin heavy chain subunit from eri-silkworm may play critical roles not only in innate immune defense, but also in organismic iron homeostasis.
- Published
- 2017