A novel ferritin gene from Procambarus clarkii involved in the immune defense against Aeromonas hydrophila infection and inhibits WSSV replication

Yang, Hui; Liu, Zhe; Jiang, Qun; JunJie, Xu; An, Zhenhua; Zhang, Yingying; Xiong, Dongmei; Wang, Lixin

doi:10.1016/j.fsi.2018.12.022

Cited by 18 publications

(5 citation statements)

References 48 publications

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“…The relative expression level of ferritin heavy chain subunit from Papilio xuthus sharply increased in response to bacterial (Escherichia coli and Staphylococcus aureus) challenge [27]. The infection rate and proliferation rate of white spot syndrome virus in ferritin-silenced Procambarus clarkii were significantly increased [28]. In the present study, the relative expression of ferritin changed significantly under low temperature stress, and both HrFer1 and HrFer2 were significantly downregulated.…”

Section: Discussionsupporting

confidence: 45%

The molecular and functional characterization of ferritins in the hard tick Hyalomma rufipes

Gao

Zheng²,

Wang³

et al. 2022

Parasites Vectors

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Background The protein ferritin, which plays an important role in the maintenance of iron homeostasis, is indispensable for iron detoxification, resistance to oxidative stress and innate immunity. Ticks, which are obligate blood-sucking ectoparasites, have to deal with a large amount of iron when they take a blood meal. Methods Sequence analysis was undertaken using bioinformatics. A recombinant (r) expression vector, rferritin, was constructed for a prokaryotic expression system. A quantitative polymerase chain reaction platform was used to detect the spatial and temporal expression patterns of target genes and their responses to a low temperature environment. Knockdown of the ferritin genes through RNA interference was used to analyze their effects on physiological parameters of ticks. Results Two ferritin genes, HrFer1 and HrFer2, were cloned from the tick Hyalomma rufipes. Their open reading frames are 519 base pairs (bp) and 573 bp in length, and number of coding amino acids 170 and 190, respectively. The phylogenetic tree showed that HrFer1 and HrFer2 have a close evolutionary relationship with the H subunit of ferritin. In vitro experiments showed that rHrFer1 and rHrFer2 had concentration-dependent iron chelating activity. The relative expression of the two ferritin genes was higher in the ovary and midgut of H. rufipes. RNA interference results demonstrated that HrFer1 and HrFer2 expression had a significant effect on engorged body weight, number of eggs laid, and mortality of H. rufipes, and that HrFer2 also had a significant effect on feeding duration. Furthermore, the relative expression of ferritin decreased significantly in a low temperature environment, suggesting that HrFer1 and HrFer2 play a regulatory role in the cold stress response of H. rufipes. Conclusions The results of the present study improve our understanding of the involvement of ferritins in tick blood-feeding. Graphical Abstract

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Section: Discussionsupporting

confidence: 45%

The molecular and functional characterization of ferritins in the hard tick Hyalomma rufipes

Gao

Zheng²,

Wang³

et al. 2022

Parasites Vectors

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“…In addition, Ferritin is also involved in the innate defense against viruses. The WSSV copy number in ferritin -silenced shrimp was much higher than that in the control group ( 24 ). Unfortunately, previous reports have indicated that Ferritin can serve as a bacterial growth inhibitor, whereas no direct killing effect was characterized.…”

Section: Discussionmentioning

confidence: 80%

A novel antimicrobial peptide screened by a Bacillus subtilis expression system, derived from Larimichthys crocea Ferritin H, exerting bactericidal and parasiticidal activities

et al. 2023

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Antimicrobial peptides (AMPs) may be the most promising substitute for antibiotics due to their effective antimicrobial activities and multiple function mechanisms against pathogenic microorganisms. In this study, a novel AMP containing 51 amino acids, named Lc1687, was screened from the large yellow croaker (Larimichthys crocea) via a B. subtilis system. Bioinformatics and circular dichroism (CD) analyses showed that Lc1687 is a novel anionic amphiphilic α-helical peptide, which was derived from the C-terminal of a Ferritin heavy subunit. The recombinant Lc1687 (named rLc1687) purified from Escherichia coli exhibited strong activities against Gram-positive (Gram+) bacterium Staphylococcus aureus, Gram-negative (Gram-) bacteria Vibrio vulnificus, V. parahaemolyticus, and Scuticociliatida. Scanning electron microscope (SEM) and transmission electron microscopy (TEM) revealed the possible function mechanisms of this peptide, which is to target and disrupt the bacterial cell membranes, including pore-forming, loss of fimbriae, and cytoplasm overflow, whereas gel retardation assay revealed that peptide Lc1687 cannot bind bacterial DNA. The peptide stability analysis showed that rLc1687 acts as a stable antimicrobial agent against Gram+ and Gram- bacteria at temperatures ranging from 25 to 100°C, pH 3-12, and UV radiation time ranging from 15 to 60 min. A hemolytic activity assay confirmed that this peptide may serve as a potential source for clinical medicine development. Taken together, Lc1687 is a novel AMP as it is a firstly confirmed Ferritin fragment with antimicrobial activity. It is also a promising agent for the development of peptide-based antibacterial and anti-parasitic therapy.

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“…For example, HCV inhibits apolipoprotein B100 expression by upregulating host FerHCH, changes that are beneficial to viral replication [ 13 ]. After Procambarus clarkii is attacked by the white spot syndrome virus, ferritin mRNA and protein expression increase significantly in blood cells and the hepato-pancreas [ 33 ]. Therefore, we consider that BmNPV could induce BmFerHCH expression.…”

Section: Discussionmentioning

confidence: 99%

Nuclear Factor Kappa B Promotes Ferritin Heavy Chain Expression in Bombyx mori in Response to B. mori Nucleopolyhedrovirus Infection

Zhu

Liu

Wang

et al. 2022

IJMS

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Ferritin heavy chain (FerHCH) is a major component of ferritin and plays an important role in maintaining iron homeostasis and redox equilibrium. Our previous studies have demonstrated that the Bombyx mori ferritin heavy chain homolog (BmFerHCH) could respond to B. mori nucleopolyhedrovirus (BmNPV) infection. However, the mechanism by which BmNPV regulates the expression of BmFerHCH remains unclear. In this study, BmFerHCH increased after BmNPV infection and BmNPV infection enhanced nuclear factor kappa B (NF-κB) activity in BmN cells. An NF-κB inhibitor (PDTC) reduced the expression of the virus-induced BmFerHCH in BmN cells, and overexpression of BmRelish (NF-κB) increased the expression of virus-induced BmFerHCH in BmN cells. Furthermore, BmNPV infection enhanced BmFerHCH promoter activity. The potential NF-κB cis-regulatory elements (CREs) in the BmFerHCH promoter were screened by using the JASPAR CORE database, and two effective NF-κB CREs were identified using a dual luciferase reporting system and electrophoretic mobility shift assay (EMSA). BmRelish (NF-κB) bound to NF-κB CREs and promoted the transcription of BmFerHCH. Taken together, BmNPV promotes activation of BmRelish (NF-κB), and activated BmRelish (NF-κB) binds to NF-κB CREs of BmFerHCH promoter to enhance BmFerHCH expression. Our study provides a foundation for future research on the function of BmFerHCH in BmNPV infection.

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A novel ferritin gene from Procambarus clarkii involved in the immune defense against Aeromonas hydrophila infection and inhibits WSSV replication

Cited by 18 publications

References 48 publications

The molecular and functional characterization of ferritins in the hard tick Hyalomma rufipes

The molecular and functional characterization of ferritins in the hard tick Hyalomma rufipes

A novel antimicrobial peptide screened by a Bacillus subtilis expression system, derived from Larimichthys crocea Ferritin H, exerting bactericidal and parasiticidal activities

Nuclear Factor Kappa B Promotes Ferritin Heavy Chain Expression in Bombyx mori in Response to B. mori Nucleopolyhedrovirus Infection

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