Identification and expression of the hepcidin gene from brown trout (Salmo trutta) and functional analysis of its synthetic peptide

Huang, Tianqing; Gu, Wei; Wang, Bingqian; Zhang, Yuyong; Cui, Lili; Yao, Zuochun; Zhao, Cheng; Xu, Gefeng

doi:10.1016/j.fsi.2019.01.020

Cited by 31 publications

(20 citation statements)

References 41 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

“…Brown trout hepcidin (Hepc) together with a scrambled version of this peptide was tested for its antibacterial activities in a disc diffusion assay [ 30 ]. Both peptides were able to inhibit the growth of four Gram-negative Acinetobacter baumannii ( A. baumannii ), A. salmonicida , Aeromonas hydrophila ( A. hydrophila ), and Pseudomonas aeruginosa ( P. aeruginosa ), as well as two Gram-positive bacteria S. aureus and Enterococcus faecium ( E. faecium ), at a concentration of 2 mg/mL [ 30 ]. The scrambled peptide showed significantly less inhibition activity against all bacteria tested compared with the synthetic mature peptide, indicating that the sequence order is an important factor determining the antibacterial potency of this peptide [ 30 ].…”

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

“…Both peptides were able to inhibit the growth of four Gram-negative Acinetobacter baumannii ( A. baumannii ), A. salmonicida , Aeromonas hydrophila ( A. hydrophila ), and Pseudomonas aeruginosa ( P. aeruginosa ), as well as two Gram-positive bacteria S. aureus and Enterococcus faecium ( E. faecium ), at a concentration of 2 mg/mL [ 30 ]. The scrambled peptide showed significantly less inhibition activity against all bacteria tested compared with the synthetic mature peptide, indicating that the sequence order is an important factor determining the antibacterial potency of this peptide [ 30 ]. In a similar assay, Hepc from Siberian taimen ( Hucho taimen ) was able to inhibit the growth of Gram-negative E. coli and S. aureus , and Gram-positive Micrococcus lsyodeikticus ( M. lysodeikticus ) [ 31 ].…”

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

“…Moreover, Z-stack confocal microscopy in combination with a Sytox membrane permeabilization assay revealed a translocation of oxidized rainbow trout Hepc into P. salmonis cells without disrupting the bacterial membrane, indicating that direct membrane disruption is likely not the mechanism of action for this AMP [ 32 ]. In contrast, another study including brown trout Hepc suggests that this peptide does indeed act through a membrane permeabilization mechanism [ 30 ]. To more clearly elucidate the role of Hepc in the immune response of a salmonid species, the effect of P. salmonis infection on hepcidin ( hepc ) expression in the RTS-11 cell line was compared against a control containing heat-inactivated P. salmonis [ 32 ].…”

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

“…This effect was deemed to be specific to Cath2 and not owing to the high concentration of peptide alone, as two other synthetic peptides derived from trout Il-17a and Il-22 were not found to delay sporulation of S. parasitica at a concentration of 100 µM [ 36 ]. Synthetic brown trout Hepc and a scrambled version of the same peptide were tested against the haploid yeast Candida glabrata ( C. glabrata ) in a disc diffusion assay [ 30 ]. Both peptides were able to inhibit the growth of C. glabrata , however, the inhibition area around disc containing the predicted Hepc was significantly larger than around the scrambled peptide at a concentration of 2 mg/mL [ 30 ].…”

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

See 4 more Smart Citations

Antimicrobial Peptides of Salmonid Fish: From Form to Function

Brunner

Varga

Dixon

2020

Biology

View full text Add to dashboard Cite

Antimicrobial peptides (AMPs) are small, usually cationic, and amphiphilic molecules that play a crucial role in molecular and cellular host defense against pathogens, tissue damage, and infection. AMPs are present in all metazoans and several have been discovered in teleosts. Some teleosts, such as salmonids, have undergone whole genome duplication events and retained a diverse AMP repertoire. Salmonid AMPs have also been shown to possess diverse and potent antibacterial, antiviral, and antiparasitic activity and are induced by a variety of factors, including dietary components and specific molecules also known as pathogen-associated molecular patterns (PAMPs), which may activate downstream signals to initiate transcription of AMP genes. Moreover, a multitude of cell lines have been established from various salmonid species, making it possible to study host-pathogen interactions in vitro, and several of these cell lines have been shown to express various AMPs. In this review, the structure, function, transcriptional regulation, and immunomodulatory role of salmonid AMPs are highlighted in health and disease. It is important to characterize and understand how salmonid AMPs function as this may lead to a better understanding of host-pathogen interactions with implications for aquaculture and medicine.

show abstract

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

Section: Function Of Salmonid Ampsmentioning

confidence: 99%

See 3 more Smart Citations

Antimicrobial Peptides of Salmonid Fish: From Form to Function

Brunner

Varga

Dixon

2020

Biology

View full text Add to dashboard Cite

show abstract

Participation of Hepcidins in the Inflammatory Response Triggered by λ-Carrageenin in Gilthead Seabream (Sparus aurata)

Campos-Sánchez,

Serna-Duque,

Alburquerque

et al. 2024

Mar Biotechnol

View full text Add to dashboard Cite

The role of hepcidins, antimicrobial peptides involved in iron metabolism, immunity, and inflammation, is studied. First, gilthead seabream (Sparus aurata L.) head-kidney leucocytes (HKLs) were incubated with λ-carrageenin to study the expression of hepcidin and iron metabolism-related genes. While the expression of most of the genes studied was upregulated, the expression of ferroportin gene (slc40a) was downregulated. In the second part of the study, seabream specimens were injected intramuscularly with λ-carrageenin or buffer (control). The expression of the same genes was evaluated in the head kidney, liver, and skin at different time points after injection. The expression of Hamp1m, ferritin b, and ferroportin genes (hamp1, fthb, and slc40a) was upregulated in the head kidney of fish from the λ-carrageenin-injected group, while the expression of Hamp2C and Hamp2E genes (hamp2.3 and hamp2.7) was downregulated. In the liver, the expression of hamp1, ferritin a (ftha), slc40a, Hamp2J, and Hamp2D (hamp2.5/6) genes was downregulated in the λ-carrageenin-injected group. In the skin, the expression of hamp1 and (Hamp2A Hamp2C) hamp2.1/3/4 genes was upregulated in the λ-carrageenin-injected group. A bioinformatic analysis was performed to predict the presence of transcription factor binding sites in the promoter region of hepcidins. The primary sequence of hepcidin was conserved among the different mature peptides, although changes in specific amino acid residues were identified. These changes affected the charge, hydrophobicity, and probability of hepcidins being antimicrobial peptides. This study sheds light on the poorly understood roles of hepcidins in fish. The results provide insight into the regulatory mechanisms of inflammation in fish and could contribute to the development of new strategies for treat inflammation in farm animals. Graphical Abstract

show abstract