Identification of FerLCH, isolation of ferritin and functional analysis related to interaction with pathogens in Eri-silkworm, Samia cynthia ricini.
Samia cynthia ricini
ferritin
light-chain subunit
pathogens interaction
Journal
Archives of insect biochemistry and physiology
ISSN: 1520-6327
Titre abrégé: Arch Insect Biochem Physiol
Pays: United States
ID NLM: 8501752
Informations de publication
Date de publication:
May 2020
May 2020
Historique:
received:
03
12
2019
revised:
12
01
2020
accepted:
13
01
2020
pubmed:
25
1
2020
medline:
11
7
2020
entrez:
25
1
2020
Statut:
ppublish
Résumé
Ferritin is a ubiquitous and conserved iron storage protein that plays a significant role in host detoxification, iron storage, and immune response. Although ferritin has been studied in many species, little is known about its role in the Eri-silkworm (Samia cynthia ricini). In this study, the ferritin light-chain subunit gene, named ScFerLCH, was identified from S. c. ricini. The full-length gene, ScFerLCH, was 1,155 bp and encoded a protein consisting of 231 amino acids with a deduced molecular weight of 26.38 kDa. Higher ScFerLCH expression levels were found in the midgut, silk gland, and fat body by quantitative reverse-transcription polymerase chain reaction and western blot analysis. Injection of Staphylococcus aureus and Pseudomonas aeruginosa could induce upregulation of ScFerLCH in the hemolymph, fat body, and midgut, indicating that ScFerLCH may contribute to the host defense against invading pathogens. In addition, the native ferritin protein was isolated from S. c. ricini by native polyacrylamide gel electrophoresis and its two subunits, ferritin heavy-chain subunit (ScFerHCH) and ferritin light-chain subunit (ScFerLCH), were identified by mass spectrometry. Specifically, we found that recombinant ferritin subunits could self-assemble into a protein complex in vitro; moreover, both recombinant subunits and the protein complex were found to bind different bacteria, including Escherichia coli, P. aeruginosa, S. aureus, and Bacillus subtilis. However, bactericidal tests showed that the protein complex could not inhibit the growth of bacteria directly. Taken together, our results suggest that ScFerritin might play an important role in mediating molecular interaction with pathogens.
Substances chimiques
Insect Proteins
0
Ferritins
9007-73-2
Iron
E1UOL152H7
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
e21659Subventions
Organisme : National Natural Science Foundation of China
ID : 31973002
Organisme : International Cooperation Project of Anhui Province
ID : 1804b06020345
Informations de copyright
© 2020 Wiley Periodicals, Inc.
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