Evidence map›Paper›PMID 42163299›Full record

ArticleBMC veterinary research2026

Immunological response of goldfish (Carassius auratus) to recombinant pro-hepcidin and its antibacterial activity against Aeromonas hydrophila.

Maryam Gheisari, Fatemeh Peyravii Ghadikolaii, Rahem Khoshbakht, Poulin Shohreh, Hami Kaboosi

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Article in BMC veterinary research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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2 · The registry

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3 · Its place in the literature

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4 · The record

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5 · Who and what money

Authors and funding

5 authors.

Maryam GheisariDepartment of Biology, QaS.C., Islamic Azad University, Qaemshahr, Iran.
Fatemeh Peyravii GhadikolaiiDepartment of Biology, QaS.C., Islamic Azad University, Qaemshahr, Iran. peyravii57@iau.ac.ir.
Rahem KhoshbakhtDepartment of Pathobiology, Faculty of Veterinary Medicine, Amol University of Special Modern Technologies, Amol, Iran. khoshbakht.r@gmail.com.
Poulin ShohrehDepartment of Clinical Sciences, Faculty of Veterinary Medicine, Amol University of Special Modern Technologies, Amol, Iran.
Hami KaboosiDepartment of Microbiology, Am.C., Islamic Azad University, Amol, Iran.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundHepcidin is a key antimicrobial peptide involved in innate immunity in fish. The present study aimed to produce recombinant pro-hepcidin from goldfish (Carassius auratus) (rpro-CuHep) and to evaluate its antibacterial activity as well as its effects on immune responses and resistance against Aeromonas hydrophila infection in goldfish.

resultsThe full-length goldfish pro-hepcidin gene was synthesized using codon optimization for Escherichia coli BL21 Rosetta and cloned into the pET28a + expression vector. Successful transformation was confirmed by Colony PCR, yielding a 287-bp fragment. Recombinant protein expression was induced with 1 mM IPTG at 37 °C for 8 h. The rpro-CuHep peptide was purified using affinity chromatography and identified as an approximately 10-kDa protein by SDS-PAGE and Western blot analysis. Antibacterial assays demonstrated that rpro-CuHep exhibited notable inhibitory activity against A. hydrophila and Streptococcus iniae. In vivo challenge experiments showed that goldfish treated with rpro-CuHep had significantly lower mortality rates following A. hydrophila infection compared to the control group. Furthermore, immune parameters including total protein, lysozyme activity, alternative complement activity (ACH50), and total immunoglobulin levels were significantly elevated in rpro-CuHep-treated fish (p < 0.05). Gene expression analysis revealed significant upregulation of interleukin-6 (IL-6) and interleukin-10 (IL-10) (p < 0.05), whereas no significant change was observed in interleukin-8 (IL-8) expression (p > 0.05).

conclusionsThe results demonstrate that rpro-CuHep possesses strong antibacterial activity and can significantly enhance immune responses and disease resistance in goldfish. These findings suggest that recombinant pro-hepcidin has potential as an effective immunostimulant and antibacterial agent for controlling bacterial infections such as A. hydrophila in aquaculture.

Indexed as

Aeromonas hydrophilaAnti-Bacterial AgentsFish DiseasesGoldfishGram-Negative Bacterial InfectionsHepcidinsAnimalsFish ProteinsImmunity, InnateRecombinant ProteinsAnti-Bacterial AgentsFish ProteinsHepcidinsRecombinant ProteinsAntibiotics resistanceBacterial diseaseGoldfishHepcidin

Identifiers

PMID42163299
PMCPMC13471415

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.