A hepatic antimicrobial peptide, hepcidin from Indian major carp, Catla catla: molecular identification and functional characterization

Abstract

Background Increase of antibiotic resistance in pathogenic microbes necessitated novel molecules for curing infection. Antimicrobial peptides (AMPs) are the gene-encoded evolutionarily conserved small molecules with therapeutic value. AMPs are considered as an alternative drug for conventional antibiotics. Hepcidin, the cysteine-rich antimicrobial peptide, is an important component in innate immune response. In this study, we identified and characterized hepcidin gene from the fish, Catla catla (Indian major carp) and termed it as Cc-Hep. Results Open reading frame of Cc-Hep consists of 261 base pair that encodes 87 amino acids. Cc-Hep is synthesized as a prepropeptide consisting of 24 amino acid signal peptide, 36 amino acid propeptide, and 26 amino acid mature peptide. Sequence analysis revealed that Cc-Hep shared sequence similarity with hepcidin from Sorsogona tuberculata. Phylogenetic analysis indicated that Cc-Hep was grouped with HAMP2 family. Structure analysis of mature Cc-Hep identified two antiparallel beta sheets stabilized by four disulphide bonds and a random coil. The mature peptide region of Cc-Hep has a charge of + 2, isoelectric value 8.23 and molecular weight 2.73 kDa. Conclusion Functional characterization predicted antibacterial, antioxidant, and anticancer potential of Cc-Hep, which can be explored in aquaculture or human health care.

Renovation as innovation: Repurposing human antibacterial peptide LL-37 for cancer therapy

“…The cytotoxic effects of numerous AMPs on different tumor cell lines have been reported previously (Cheng et al, 2020;Lee et al, 2021;Athira et al, 2022;Jafari et al, 2022;Patil and Kunda, 2022). These AMPs contain several cationic and hydrophobic amino acids and were found to be involved in various anticancer activities.…”

B-1 derived anti-Thy-1 B cells in old aged mice develop lymphoma/leukemia with high expression of CD11b and Hamp2 that different from TCL1 transgenic mice

“…Hepcidin is an innate antimicrobial agent that is induced by most invasive bacteria and also by virus, then limits bacterial proliferation by reducing iron such as in plasma and extracellular fluids, and kills bacteria [ 38 ]. Hamp2 is more reactive as an antibacterial and antivirus activity than Hamp1 [ 39 , 40 ]. The most important function of hepcidin (also mouse both Hamp1 and Hamp2) is to regulate iron [ 41 ].…”

Antimicrobial Peptides Demonstrate Activity against Resistant Bacterial Pathogens

“…Insect AMPs (e.g., cecropin) are produced in cells and fat bodies and have demonstrated antimicrobial, anti-inflammatory activity and in some cases anticancer activity [ 18 ]. Hepcidin, a cysteine-rich AMP, has an important role in iron regulation and antimicrobial, anticancer, antiparasitic, and immunomodulatory activity [ 19 ]. As a peptide hormone, hepcidin is produced and secreted by liver hepatocytes and Kupffer’s cells [ 20 ].…”

“…Stored in the azurophilic granules of human neutrophils. Secreted by paneth cells in the small intestinal Cathelicidins Bactenecins Human cathelicidin LL-37 [9] Immunomodulatory activity, impacts quorum sensing mechanisms in P. aeruginosa biofilm formation [25], apoptosis induction, inflammasome activation, and phagocytosis [13] LL-37 inhibits Aspergillus fumigatus infection and reduces inflammation [9], LL37 analogue peptides (AC-1, AC-2, LL37-1, and D) effetive against C. albicans yeasts [3] The bactenecin ChBac3.4 appears more active against bacterial membranes and tumor cells compared to normal cells [26] LL-37 effective against various Gram-positive and Gram-negative bacteria, and AMR species [9] Hepcidins Human liver-expressed antimicrobial peptide (LEAP) Fish hepcidins HAMP1 and HAMP2 Antibacterial Iron regulatory mode of action [19] Type II acute phase protein Results in a reduction in ferroportin expression…”