Abstract
Hepcidin, a cysteine-rich antimicrobial peptide, with multiple disulfide bonds plays an important role in the defense mechanism and iron metabolism of organisms. In this study, we characterized a hepcidin from a fish under IUCN Red List i.e., tuberculated flathead, Sorsogona tuberculata. The hepcidin consists of an open reading frame of 261 base pairs encoding 86 amino acids with a signal peptide of 24 amino acids, a prodomain of 36 amino acids and a biologically active mature peptide of 26 amino acids. A conserved RX (K/R) R motif and eight conserved cysteine residues were observed. Mature peptide of St-hep is found to have a molecular weight of 2.73 kDa and the predicted three dimensional structure was similar to hepcidins from other animals, which can attain a β-hairpin-like structure with two antiparallel β-sheets. The Ramachandran plot showed 100 % of the residues in favourable and allowed regions, which confirmed the accuracy of the model. Functional characterization of St-hep was carried out using various bioinformatic resource portals. The results suggested that St-hep possesses antibacterial, antiviral, antifungal, anticancer, and immunomodulatory properties indicating its importance as a defense molecule that can be explored for therapeutic applications in aquaculture.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
Data availability
Not applicable.
Code availability
Not applicable.
Abbreviations
- St-hep:
-
Sorsogona tuberculata-hepcidin
- FORV:
-
Fishery Oceanographic Research Vessel
- CO1:
-
Cytochrome Oxidase 1
- AMP:
-
Antimicrobial peptide
- RT-PCR:
-
Reverse transcription Polymerase chain reaction
- IPTG:
-
Isopropyl β-D-1 thiogalactopyranoside
- X-Gal:
-
5-Bromo-4-chloro-3-indoyl-β-D-galactopyranoside
- BLAST:
-
Basic Local Alignment Search Tool
- SVM:
-
Support Vector Machine
- TH:
-
Tilapia hepcidin
References
Agrawal P, Bhalla S, Chaudhary K, Kumar R, Sharma M, Raghava GP (2018) In silico approach for prediction of antifungal peptides. Front Microbiol 9:323. https://doi.org/10.3389/fmicb.2018.00323
Álvarez CA, Santana PA, Guzmán F, Marshall S, Mercado L (2013) Detection of the hepcidin prepropeptide and mature peptide in liver of rainbow trout. Dev Comp Immunol 41:77–81. https://doi.org/10.1016/j.dci.2013.04.002
Álvarez CA, Guzmán F, Cárdenas C, Marshall SH, Mercado L (2014) Antimicrobial activity of trout hepcidin. Fish Shellfish Immunol 41:93–101. https://doi.org/10.1016/j.fsi.2014.04.013
Bo J, Cai L, Xu JH, Wang KJ, Au DW (2011) The marine medaka Oryzias melastigma– a potential marine fish model for innate immune study. Mar Pollut Bull 63: 267–276. https://doi.org/10.1016/j.marpolbul.2011.05.014
Bustillo ME, Fischer AL, LaBouyer MA, Klaips JA, Webb AC, Elmore DE (2014) Modular analysis of hipposin, a histone-derived antimicrobial peptide consisting of membrane translocating and membrane permeabilizing fragments. Biochim Biophys Acta Biomembr 1838:2228–2233. https://doi.org/10.1016/j.bbamem.2014.04.010
Byadgi O, Massimo M, Dirks RP, Pallavicini A, Bron JE, Ireland JH, Volpatti D, Galeotti M, Beraldo P (2021) Innate immune-gene expression during experimental amyloodiniosis in European seabass (Dicentrarchus labrax). Vet Immunol Immunopathol 234:110217. https://doi.org/10.1016/j.vetimm.2021.110217
Cai L, Cai JJ, Liu HP, Fan DQ, Peng H, Wang KJ (2012) Recombinant medaka (Oryzias melastigmus) pro-hepcidin: Multifunctional characterization. Comp Biochem Physiol B: Biochem Mol Biol 161:140–147. https://doi.org/10.1016/j.cbpb.2011.10.006
Capparelli R, De Chiara F, Nocerino N, Montella RC, Iannaccone M, Fulgione A, Romanelli A, Avitabile C, Blaiotta G, Capuano F (2012) New perspectives for natural antimicrobial peptides: application as antinflammatory drugs in a murine model. BMC Immunol 13:61. https://doi.org/10.1186/1471-2172-13-61
Chaithanya ER, Philip R, Sathyan N, Kumar PA, Antony SP, Sanjeevan VN, Singh IB (2013) A novel isoform of the hepatic antimicrobial peptide, hepcidin (Hepc-CB1), from a deep-sea fish, the spinyjaw greeneye Chlorophthalmus bicornis (Norman, 1939): molecular characterisation and phylogeny. Probiotics Antimicro Prot 5:1–7. https://doi.org/10.1007/s12602-012-9120-0
Chang WT, Pan CY, Rajanbabu V, Cheng CW, Chen JY (2011) Tilapia (Oreochromis mossambicus) antimicrobial peptide, hepcidin 1–5, shows antitumor activity in cancer cells. Peptides 32:342–352. https://doi.org/10.1016/j.peptides.2010.11.003
Chen SL, Xu MY, Ji XS, Yu GC, Liu Y (2005) Cloning, characterization, and expression analysis of hepcidin gene from red sea bream (Chrysophrys major). Antimicrob Agents Chemother 49:1608–1612. https://doi.org/10.1128/AAC.49.4.1608-1612.2005
Chen JY, Lin WJ, Lin TL (2009) A fish antimicrobial peptide, tilapia hepcidin TH2-3, shows potent antitumor activity against human fibrosarcoma cells. Peptides 30: 1636–1642. https://doi.org/10.1016/j.peptides.2009.06.009
Chen J, Nie L, Chen J (2018) Mudskipper (Boleophthalmus pectinirostris) hepcidin-1 and hepcidin-2 present different gene expression profile and antibacterial activity and possess distinct protective effect against Edwardsiella tarda infection. Probiotics Antimicrob Proteins 10:176–185. https://doi.org/10.1007/s12602-017-9352-0
Chen T, Zhou J, Qu Z, Zou Q, Liu X, Su J, Fu X, Yuan G (2020) Administration of dietary recombinant hepcidin on grass carp (Ctenopharyngodon idella) against Flavobacterium columnare infection under cage aquaculture conditions. Fish Shellfish Immunol 99:27–34. https://doi.org/10.1016/j.fsi.2020.01.042
Cole AM, Weis P, Diamond G (1997) Isolation and characterization of pleurocidin, an antimicrobial peptide in the skin secretions of winter flounder. J Biol Chem 272:12008–12013. https://doi.org/10.1074/jbc.272.18.12008
Conchillo-Solé O, de Groot NS, Avilés FX, Vendrell J, Daura X, Ventura S (2007) AGGRESCAN: a server for the prediction and evaluation of "hot spots" of aggregation in polypeptides. BMC Bioinformatics 8:65. https://doi.org/10.1186/1471-2105-8-65
Cuesta A, Meseguer J, Esteban MA (2008) The antimicrobial peptide hepcidin exerts an important role in the innate immunity against bacteria in the bony fish Gilthead Sea bream. Mol Immunol 45:2333–2342. https://doi.org/10.1016/j.molimm.2007.11.007
Douglas SE, Gallant JW, Liebscher RS, DacanayA, Tsoi SC (2003) Identification and expression analysis of hepcidin-like antimicrobial peptides in bony fish. Dev Comp Immunol 27:589–601. https://doi.org/10.1016/S0145-305X(03)00036-3
Falco A, Chico V, Marroqui L, Perez L, Coll JM, Estepa A (2008) Expression and antiviral activity of a β-defensin-like peptide identified in the rainbow trout (Oncorhynchus mykiss) EST sequences. Mol Immunol 45: 757–765. https://doi.org/10.1016/j.molimm.2007.06.358
Fan Y, Liu B, Chen F, Song Z, Han B, Meng Y, Hou J, Cao P, Chang Y, Tan K (2021) Hepcidin upregulation in lung cancer: A potential therapeutic target associated with immune infiltration. Front Immunol 12:1080. https://doi.org/10.3389/fimmu.2021.612144
Gautam A, Chaudhary K, Kumar R, Sharma A, Kapoor P, Tyagi A, Raghava GP (2013) In silico approaches for designing highly effective cell penetrating peptides. J Transl Med 11:74. https://doi.org/10.1186/1479-5876-11-74
Gong LC, Wang H, Deng L (2014) Molecular characterization, phylogeny and expression of a hepcidin gene in the blotched snakehead Channa maculata. Dev Comp Immunol 44:1–11. https://doi.org/10.1016/j.dci.2013.11.007
Hilton KB, Lambert LA (2008) Molecular evolution and characterization of hepcidin gene products in vertebrates. Gene 415:40–48. https://doi.org/10.1016/j.gene.2008.02.016
Hirono I, Hwang JY, Ono Y, Kurobe T, Ohira T, Nozaki R, Aoki T (2005) Two different types of hepcidins from the Japanese flounder Paralichthys olivaceus. FEBS J 272:5257–5264. https://doi.org/10.1111/j.1742-4658.2005.04922.x
Hocquellet A, le Senechal C, Garbay B (2012) Importance of the disulfide bridges in the antibacterial activity of human hepcidin Peptides 36: 303–307. https://doi.org/10.1016/j.peptides.2012.06.001
Huang T, Gu W, Wang B, Zhang Y, Cui L, Yao Z, Zhao C, Xu G (2019) Identification and expression of the hepcidin gene from brown trout (Salmo trutta) and functional analysis of its synthetic peptide. Fish Shellfish Immunol 87:243–253. https://doi.org/10.1016/j.fsi.2019.01.020
Hunter HN, Fulton DB, Ganz T, Vogel HJ (2002) The solution structure of human hepcidin, a peptide hormone with antimicrobial activity that is involved in iron uptake and hereditary hemochromatosis. J Biol Chem 277:37597–37603. https://doi.org/10.1074/jbc.M205305200
Joseph S, Karnik S, Nilawe P, Jayaraman VK, Idicula-Thomas S (2012) ClassAMP: a prediction tool for classification of antimicrobial peptides. TCBB 9:1535–1538. https://doi.org/10.1109/TCBB.2012.89
Kelley LA, Mezulis S, Yates CM, Wass MN, Sternberg MJ (2015) The Phyre2 web portal for protein modeling, prediction and analysis. Nat Protoc 10:845. https://doi.org/10.1038/nprot.2015.053
Kolaskar AS, Tongaonkar PC (1990) A semi-empirical method for prediction of antigenic determinants on protein antigens. FEBS Lett 276:172–174. https://doi.org/10.1016/0014-5793(90)80535-Q
Krause A, Neitz S, Mägert HJ, Schulz A, Forssmann WG, Schulz-Knappe P, Adermann K (2000) LEAP-1, a novel highly disulfide‐bonded human peptide, exhibits antimicrobial activity. FEBS Lett 480:147–150. https://doi.org/10.1016/S0014-5793(00)01920-7
Krause A, Sillard R, Kleemeier B, Klüver E, Maronde E, Conejo-García JR, Forssmann WG, Schulz‐Knappe P, Nehls MC, Wattler F, Wattler S (2003) Isolation and biochemical characterization of LEAP‐2, a novel blood peptide expressed in the liver. Protein Sci 12:143–152. https://doi.org/10.1110/ps.0213603
Kumar M, Gromiha MM, Raghava GP (2007) Identification of DNA-binding proteins using support vector machines and evolutionary profiles. BMC Bioinform 8: 463. https://doi.org/10.1186/1471-2105-8-463
Kyte J, Doolittle RF (1982) A simple method for displaying the hydropathic character of a protein. J Mol Biol 157:105–132. https://doi.org/10.1016/0022-2836(82)90515-0
Lai Y, Gallo RL (2009) AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense. Trends Immunol 30:131–141. https://doi.org/10.1016/j.it.2008.12.003
Lata S, Mishra NK, Raghava GP (2010) AntiBP2: improved version of antibacterial peptide prediction. BMC Bioinform 11:S19. https://doi.org/10.1186/1471-2105-11-S1-S19
Lauth X, Babon JJ, Stannard JA, Singh S, Nizet V, Carlberg JM, Ostland VE, Pennington MW, Norton RS, Westerman ME (2005) Bass hepcidin synthesis, solution structure, antimicrobial activities and synergism, and in vivo hepatic response to bacterial infections. J Biol Chem 280:9272–9282. https://doi.org/10.1074/jbc.M411154200
Li Z, Hong WS, Qiu HT, Zhang YT, Yang MS, You XX, Chen SX (2016) Cloning and expression of two hepcidin genes in the mudskipper (Boleophthalmus pectinirostris) provides insights into their roles in male reproductive immunity. Fish Shellfish Immunol 56:239–247. https://doi.org/10.1016/j.fsi.2016.07.025
Lin JHY, Lin HT, Lopez C, Chen TY, Chen MS, Yang HL (2008) A comparison of the expression of immunity‐related rag 1 and ikaros genes with histogenesis of the thymus in Epinephelus malabaricus (Bloch & Schneider). Aquac Res 39:252–262. https://doi.org/10.1111/j1365-2109.2007.01871.x
Liu QN, Xin ZZ, Zhang DZ, Jiang SH, Chai XY, Wang ZF, Li CF, Zhou CL, Tang BP (2017) cDNA cloning and expression analysis of a hepcidin gene from yellow catfish Pelteobagrus fulvidraco (Siluriformes: Bagridae). Fish Shellfish Immunol 60:247–254. https://doi.org/10.1128/AAC.49.4.1608-1612.2005
Liu ZM, Chen J, Lv YP, Hu ZH, Dai QM, Fan XL (2018) Molecular characterization of a hepcidin homologue in starry flounder (Platichthys stellatus) and its synergistic interaction with antibiotics. Fish Shellfish Immunol 83:45–51. https://doi.org/10.1016/j.fsi.2018.09.019
Luo SW, Luo ZY, Yan T, Luo KK, Feng PH, Liu SJ (2020) Antibacterial and immunoregulatory activity of a novel hepcidin homologue in diploid hybrid fish (Carassius auratus cuvieri♀× Carassius auratus red var♂). Fish Shellfish Immunol 98: 551–563. https://doi.org/10.1016/j.fsi.2020.01.038
Ma Y, Lee CJ, Kim SS, Kim DN, Nam BH, Kim YO, An CM, Park JS (2020) Role of hepcidins from black rockfish (Sebastes schlegelii) in iron-metabolic function and bacterial defense. J Mar Sci Eng 8:493. https://doi.org/10.3390/jmse8070493
Mahrous KF, Abd El-Kader HA, Mabrouk DM, Aboelenin MM, Osman NM, Khalil WK, Hassanane MS (2020) Molecular characterization and expression analysis of hepc1 and hepc2 in three tilapia species collected from Lake Manzala. Bull Natl Res Cent 44:1–13. https://doi.org/10.1186/s42269-020-00309-9
Mahrous KF, Mabrouk DM, Aboelenin MM, Abd El HA (2021) Identification and characterization of antimicrobial peptide genes in Clarias gariepinus and Chelon ramada. Jordan J Biol Sci 14
Nagpal G, Chaudhary K, Agrawal P, Raghava GP (2018) Computer-aided prediction of antigen presenting cell modulators for designing peptide-based vaccine adjuvants. J Trans Med 16:181. https://doi.org/10.1186/s12967-018-1560-1
Nair A, Sruthy KS, Chaithanya ER, Sajeevan TP, Singh IB, Philip R (2017) Molecular Characterisation of a Novel Isoform of Hepatic Antimicrobial Peptide, Hepcidin (Le-Hepc), from Leiognathus equulus and analysis of its functional properties In Silico. Probiotics Antimicrob Proteins 9:473–482. https://doi.org/10.1007/s12602-017-9294-6
Nakayama K (1997) Furin: a mammalian subtilisin/ Kex2p-like endoprotease involved in processing of a wide variety of precursor proteins. Biochem J 327:625–635. https://doi.org/10.1042/bj3270625
Neves JV, Caldas C, Vieira I, Ramos MF, Rodrigues PN (2015) Multiple hepcidins in a teleost fish, Dicentrarchus labrax: different hepcidins for different roles. J Immunol 195:2696–2709. https://doi.org/10.4049/jimmunol.1501153
Pan CY, Chow TY, Yu CY, Yu CY, Chen JC, Chen JY (2010) Antimicrobial peptides of an anti-lipopolysaccharide factor, epinecidin-1, and hepcidin reduce the lethality of Riemerella anatipestifer sepsis in ducks. Peptides 31:806–815. https://doi.org/10.1016/j.peptides.2010.01.013
Pan CY, Lee SC, Rajanbabu V, Lin CH, Chen JY (2012) Insights into the antibacterial and immunomodulatory functions of tilapia hepcidin (TH) 2–3 against Vibrio vulnificus infection in mice. Dev Comp Immunol 36:166–173. https://doi.org/10.1016/j.dci.2011.06.013
Park CH, Valore EV, Waring AJ, Ganz T (2001) Hepcidin, a urinary antimicrobial peptide synthesized in the liver. J Biol Chem 276:7806–7810. https://doi.org/10.1074/jbc.M008922200
Pereiro P, Figueras A, Novoa B (2012) A novel hepcidin-like in turbot (Scophthalmus maximus L.) highly expressed after pathogen challenge but not after iron overload. Fish Shellfish Immunol 32: 879–889. https://doi.org/10.1016/j.fsi.2012.02.016
Pigeon C, Ilyin G, Courselaud B, Leroyer P, Turlin B, Brissot P, Loréal O (2001) A new mouse liver-specific gene, encoding a protein homologous to human antimicrobial peptide hepcidin, is over expressed during iron overload. J Biol Chem 276:7811–7819. https://doi.org/10.1074/jbc.M008923200
Porollo AA, Adamczak R, Meller J (2004) POLYVIEW: a flexible visualization tool for structural and functional annotations of proteins. Bioinformatics 20:2460–2462. https://doi.org/10.1093/bioinformatics/bth248
Powers JPS, Hancock RE (2003) The relationship between peptide structure and antibacterial activity. Peptides 24:1681–1691. https://doi.org/10.1016/j.peptides.2003.08.023
Rajanbabu V, Pan CY, Lee SC, Lin WJ, Lin CC, Li CL, Chen JY (2010) Tilapia Hepcidin 2–3 Peptide Modulates Lipopolysaccharide-induced Cytokines and Inhibits Tumor Necrosis Factor-α through Cyclooxygenase-2 and Phosphodiesterase 4D. J Biol Chem 285 40:30577–30586. https://doi.org/10.1074/jbc.M110.137935
Ramaprasad ASE, Singh S, Venkatesan S (2015) AntiAngioPred: a server for prediction of anti-angiogenic peptides. PLoS One 10:e0136990. https://doi.org/10.1371/journal.pone.0136990
Ravichandran S, Kumaravel K, Rameshkumar G, Ajithkumar TT (2010) Antimicrobial peptides from the marine fishes. Res J Immunol 3:146–156. https://doi.org/10.3923/rji.2010.146.156
Ren HL, Wang KJ, Zhou HL, Yang M (2006) Cloning and organisation analysis of a hepcidin-like gene and cDNA from Japan sea bass, Lateolabrax japonicus. Fish Shellfish Immunol 21:221–227. https://doi.org/10.1016/j.fsi.2005.10.011
Robertson LS (2009) Expression in fish of hepcidin, a putative antimicrobial peptide and iron regulatory hormone. In: Proceedings of The Third Bilateral Conference between the United States and Russia: Aquatic Animal Health: Sheperdstown, WV 284–292
Rodrigues PN, Vázquez-Dorado S, Neves JV, Wilson JM (2006) Dual function of fish hepcidin: response to experimental iron overload and bacterial infection in sea bass (Dicentrarchus labrax). Dev Comp Immunol 30: 1156–1167. https://doi.org/10.1016/j.dci.2006.02.005
Rong M, He B, McAllister WT, Durbin RK (1998) Promoter specificity determinants of T7 RNA polymerase. Proc Natl Acad Sci 95:515–519. https://doi.org/10.1073/pnas.95.2.515
Sarode GS, Gupta K, Maniyar N, Sarode SC, Panta P, Patil S (2019) Use of tilapia hepcidin in oral cancer therapeutics: a proposal. J Contemp Dent Pract 20:403–404. https://doi.org/10.5005/jp-journals-10024-2529
Scocchi M, Pallavicini A, Salgaro R, Bociek K, Gennaro R (2009) The salmonid cathelicidins: a gene family with highly varied C-terminal antimicrobial domains. Comp Biochem Physiol B: Biochem Mol Biol, 152: 376–381. https://doi.org/10.1016/j.cbpb.2009.01.003
Shi J, Camus AC (2006) Hepcidins in amphibians and fishes: antimicrobial peptides or iron-regulatory hormones? Dev Comp Immunol 30:746–755. https://doi.org/10.1016/j.dci.2005.10.009
Shike H, Lauth X, Westerman ME, Ostland VE, Carlberg JM, Van Olst JC, Shimizu C, Bulet P, Burns JC (2002) Bass hepcidin is a novel antimicrobial peptide induced by bacterial challenge. Eur J Biochem 269:2232–2237. https://doi.org/10.1046/j.1432-1033.2002.02881.x
Stark M, Liu LP, Deber CM (2002) Cationic hydrophobic peptides with antimicrobial activity. Antimicrob Agents Chemother 46:3585–3590. https://doi.org/10.1128/AAC.46.11.3585-3590.2002
Sumon TA, Hussain MA, Hasan M, Rashid A, Abualreesh MH, Jang WJ, Sharifuzzaman SM, Brown CL, Lee EW, Hasan MT (2021) Antiviral peptides from aquatic organisms: Functionality and potential inhibitory effect on SARS-CoV-2. Aquaculture 541:736783. https://doi.org/10.1016/j.aquaculture.2021.736783
Thakur N, Qureshi A, Kumar M (2012) AVPpred: collection and prediction of highly effective antiviral peptides. Nucleic Acids Res 40(W1):W199–W204. https://doi.org/10.1093/nar/gks450
Ting CH, Pan CY, Chen YC, Lin YC, Chen TY, Rajanbabu V, Chen JY (2019) Impact of Tilapia hepcidin 2–3 dietary supplementation on the gut microbiota profile and immunomodulation in the grouper (Epinephelus lanceolatus). Sci Rep 9:1–17. https://doi.org/10.1038/s41598-019-55509-9
Tyagi A, Kapoor P, Kumar R, Chaudhary K, Gautam A, Raghava GPS (2013) silico models for designing and discovering novel anticancer peptides. Sci Rep 3:2984. https://doi.org/10.1038/srep02984
Waghu FH, Barai RS, Gurung P, Idicula-Thomas S (2016) CAMPR3: a database on sequences, structures and signatures of antimicrobial peptides. Nucleic Acids Res 44 (D1): D1094–D1097. https://doi.org/10.1093/nar/gkv1051
Wang KJ, Cai JJ, Cai L, Qu HD, Yang M, Zhang M (2009) Cloning and expression of a hepcidin gene from a marine fish (Pseudosciaena crocea) and the antimicrobial activity of its synthetic peptide. Peptides 30:638–646. https://doi.org/10.1016/j.peptides.2008.12.014
Wang D, Li S, Zhao J, Liu H, Lu T, Yin J (2016) Genomic organization, expression and antimicrobial activity of a hepcidin from taimen (Hucho taimen, Pallas). Fish Shellfish Immunol 56:303–309. https://doi.org/10.1016/j.fsi.2016.07.027
Ward RD, Zemlak TS, Innes BH, Last PR, Hebert PD (2005) DNA barcoding Australia’s fish species. Philos Trans R Soc B Biol Sci 360:1847–1857. https://doi.org/10.1098/rstb.2005.1716
Xiao X, Wang P, Lin WZ, Jia JH, Chou KC (2013) iAMP-2L: a two-level multi-label classifier for identifying antimicrobial peptides and their functional types. Anal Biochem 436:168–177. https://doi.org/10.1016/j.ab.2013.01.019
Xu Q, Cheng CHC, Hu P, Ye H, Chen Z, Cao L, Chen L, Shen Y, Chen L (2008) Adaptive evolution of hepcidin genes in antarctic notothenioid fishes. Mol Biol Evol 25:1099–1112. https://doi.org/10.1093/molbev/msn056
Xu G, Huang T, Gu W, Zhang Y, Yao Z, Zhao C, Wang B (2018) Characterization, expression, and functional analysis of the hepcidin gene from Brachymystax lenok. Dev Comp Immunol 89:131–140. https://doi.org/10.1016/j.dci.2018.08.013
Yang M, Wang KJ, Chen JH, Qu HD, Li SJ (2007) Genomic organization and tissue-specific expression analysis of hepcidin-like genes from black porgy (Acanthopagrus schlegelii B.). Fish Shellfish Immunol 23:1060–1071. https://doi.org/10.1016/j.fsi.2007.04.011
Zheng L, Li Y, Wang J, Pan Y, Chen J, Zheng W, Lin L (2020) Antibacterial and antiparasitic activities analysis of a hepcidin-like antimicrobial peptide from Larimichthys crocea. Acta Oceanol Sin 39:129–139. https://doi.org/10.1007/s13131-020-1580-6
Zhou JG, Wei JG, Xu D, Cui HC, Yan Y, Ou-Yang ZL, Huang XH, Huang YH, Qin QW (2011) Molecular cloning and characterization of two novel hepcidins from orange-spotted grouper, Epinephelus coioides. Fish Shellfish Immunol 30:559–568. https://doi.org/10.1016/j.fsi.2010.11.021
Acknowledgements
The authors are grateful to the Director, Centre for Marine Living Resources and Ecology (CMLRE), and Ministry of Earth Sciences (MoES), Government of India for the research grant (MoES/10-MLR/01/2012) and scientific support for the work. Authors also thank Director, National Centre for Aquatic and Animal Health (NCAAH), for scientific/ technical support of the work. The first author gratefully acknowledges DST (Department of Science and Technology), Government of India for the award of INSPIRE fellowship and the corresponding author to University grants Commission, Government of India for the BSR Faculty Grant (F.18 − 1/2011 (BSR) 2019).
Author information
Authors and Affiliations
Contributions
AMV carried out the experiment of the present work with support from APP, AVV, AK, and NS. The manuscript was written by AMV. RP supervised the work and corrected the manuscript.
Corresponding author
Ethics declarations
Conflicts of interest/Competing interests
The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.
Ethics approval
This article does not contain any studies with human participants or animalsperformed by any of the authors
Consent to participate
Not applicable.
Consent for publication
Not applicable.
Additional information
Publisher’s Note
Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.
Rights and permissions
About this article
Cite this article
Veedu, A.M., Prahaladhan, A.P., Vadakkeveettil, A.V. et al. An Antimicrobial peptide hepcidin, St-hep from tuberculated flathead, Sorsogona tuberculata (Cuvier, 1829): Molecular and functional characterization. Biologia 76, 3477–3488 (2021). https://doi.org/10.1007/s11756-021-00867-x
Received:
Accepted:
Published:
Issue Date:
DOI: https://doi.org/10.1007/s11756-021-00867-x