β-Defensins from common goby (Pomatoschistus microps) and silver trevally (Pseudocaranx georgianus): Molecular characterization and phylogenetic analysis.
K L Dhanya Lenin, Rajeswary Vasu Iyer, Athira Raveendran, M V Anju, Rosamma Philip, Swapna P Antony
Author Information
K L Dhanya Lenin: Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Rajeswary Vasu Iyer: Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Athira Raveendran: Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
M V Anju: Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Rosamma Philip: Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India.
Swapna P Antony: Department of Marine Biology, Microbiology and Biochemistry, School of Marine Sciences, Cochin University of Science and Technology, Fine Arts Avenue, Kochi, Kerala, 682016, India. swapnapantony@gmail.com. ORCID
Antimicrobial peptides (AMPs) are biologically active molecules involved in host defense present in a variety of organisms. They are an integral component of innate immunity, forming a front line of defense against potential pathogens, including antibiotic-resistant ones. Fishes are proven to be a prospective source of AMPs as they are constantly being challenged by a variety of pathogens and the AMPs are reported to play an inevitable role in fish immunity. Among them, β-defensins form one of the most studied multifunctional peptides with early evolutionary history and recently being considered as host defense peptides. The present study highlights the first-ever report on β-defensin AMP sequences from common goby (Pomatoschistus microps) and silver trevally (Pseudocaranx georgianus). A 192 bp cDNA fragment with an open reading frame encoding 63 amino acids (aa) comprising a 20 aa signal peptide region at the N-terminal was obtained from the mRNA of gill tissue of both P. microps and P. georgianus by RT-PCR. These peptide sequences when characterized in silico at the molecular level revealed a 43 aa cationic mature peptide with the signature intra-molecular disulphide bonded cysteine residue pattern ascertaining its β-defensin identity, further confirmed by phylogenetic analysis. The data collected will pave the way for further research on varied facets of the peptide-like, tissue level expressions, antimicrobial activities on commonly encountered pathogens, and its feasibility as a therapeutant in the aquaculture scenario.
Katzenback B (2015) Antimicrobial peptides as mediators of innate immunity in teleosts. Biology 4:607–639. https://doi.org/10.3390/biology4040607
[DOI: 10.3390/biology4040607]
Silphaduang U, Noga EJ (2001) Peptide antibiotics in mast cells of fish. Nature 414:268–269. https://doi.org/10.1038/35104690
[DOI: 10.1038/35104690]
Casadei E, Wang T, Zou J, Vecino JLG, Wadsworth S, Secombes CJ (2009) Characterization of three novel β-defensin antimicrobial peptides in rainbow trout (Oncorhynchus mykiss). Mol Immunol 46:3358–3366. https://doi.org/10.1016/j.molimm.2009.07.018
[DOI: 10.1016/j.molimm.2009.07.018]
Aoki W, Ueda M (2013) Characterization of antimicrobial peptides toward the development of novel antibiotics. Pharmaceuticals 6:1055–1081. https://doi.org/10.3390/ph6081055
[DOI: 10.3390/ph6081055]
Kang HK, Kim C, Seo CH, Park Y (2017) The therapeutic applications of antimicrobial peptides (AMPs): a patent review. J Microbiol 55:1–12. https://doi.org/10.1007/s12275-017-6452-1
[DOI: 10.1007/s12275-017-6452-1]
Wu Q, Patočka J, Kuča K (2018) Insect antimicrobial peptides, a mini review. Toxins 10:461. https://doi.org/10.3390/toxins10110461
[DOI: 10.3390/toxins10110461]
Ruangsri J, Kitani Y, Kiron V, Lokesh J, Brinchmann MF, Karlsen BO, Fernandes JM (2013) A novel beta-defensin antimicrobial peptide in Atlantic cod with stimulatory effect on phagocytic activity. PLoS ONE 8:e62302. https://doi.org/10.1371/journal.pone.0062302
[DOI: 10.1371/journal.pone.0062302]
Selsted ME, Ouellette AJ (2005) Mammalian defensins in the antimicrobial immune response. Nature Immunol 6:551–557. https://doi.org/10.1038/ni1206
[DOI: 10.1038/ni1206]
Zou J, Mercier C, Koussounadis A, Secombes C (2007) Discovery of multiple beta-defensin like homologues in teleost fish. Mol Immunol 44:638–647. https://doi.org/10.1016/j.molimm.2006.01.012
[DOI: 10.1016/j.molimm.2006.01.012]
Tu J, Li D, Li Q, Zhang L, Zhu Q, Gaur U, Fan X, Xu H, Yao Y, Yang ZX (2015) Molecular evolutionary analysis of β-defensin peptides in vertebrates. Evol Bioinform. https://doi.org/10.4137/EBO.S25580
[DOI: 10.4137/EBO.S25580]
Zhao JG, Zhou L, Jin JY, Zhao Z, Lan J, Zhang YB, Zhang QY, Gui JF (2009) Antimicrobial activity-specific to Gram-negative bacteria and immune modulation-mediated NF-κB and Sp1 of a medaka β-defensin. Dev Comp Immunol 33:624–637. https://doi.org/10.1016/j.dci.2008.11.006
[DOI: 10.1016/j.dci.2008.11.006]
Jin JY, Zhou L, Wang Y, Li Z, Zhao JG, Zhang QY, Gui JF (2010) Antibacterial and antiviral roles of a fish β-defensin expressed both in pituitary and testis. PLoS ONE 5:e12883. https://doi.org/10.1371/journal.pone.0012883
[DOI: 10.1371/journal.pone.0012883]
Cuesta A, Meseguer J, Esteban MA (2011) Molecular and functional characterization of the gilthead seabream β-defensin demonstrate its chemotactic and antimicrobial activity. Mol Immunol 48:1432–1438. https://doi.org/10.1016/j.molimm.2011.03.022
[DOI: 10.1016/j.molimm.2011.03.022]
Liang T, Wang DD, Zhang GR, Wei KJ, Wang WM, Zou GW (2013) Molecular cloning and expression analysis of two β-defensin genes in the blunt snout bream (Megalobrama amblycephala). Comp Biochem Physiol B Biochem Mol Biol 166:91–98. https://doi.org/10.1016/j.cbpb.2013.07.006
[DOI: 10.1016/j.cbpb.2013.07.006]
Harte A, Tian G, Xu Q, Secombes CJ, Wang T (2020) Five subfamilies of β-defensin genes are present in salmonids: evolutionary insights and expression analysis in Atlantic salmon Salmo salar. Dev Comp Immunol 104:103560. https://doi.org/10.1016/j.dci.2019.103560
[DOI: 10.1016/j.dci.2019.103560]
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
[DOI: 10.1016/j.molimm.2007.06.358]
Nam BH, Moon JY, Kim YO, Kong HJ, Kim WJ, Lee SJ, Kim KK (2010) Multiple β-defensin isoforms identified in early developmental stages of the teleost Paralichthys olivaceus. Fish Shellfish Immunol 28:267–274. https://doi.org/10.1016/j.fsi.2009.11.004
[DOI: 10.1016/j.fsi.2009.11.004]
Dong JJ, Wu F, Ye X, Sun CF, Tian YY, Lu MX, Chen ZH (2015) β-Defensin in Nile tilapia (Oreochromis niloticus): sequence, tissue expression, and anti-bacterial activity of synthetic peptides. Gene 566:23–31. https://doi.org/10.1016/j.gene.2015.04.025
[DOI: 10.1016/j.gene.2015.04.025]
Wang G, Li J, Zou P, Xie H, Huang B, Nie P, Chang M (2012) Expression pattern, promoter activity and bactericidal property of β-defensin from the mandarin fish Siniperca chuatsi. Fish Shellfish Immunol 33:522–531. https://doi.org/10.1016/j.fsi.2012.06.003
[DOI: 10.1016/j.fsi.2012.06.003]
Anooja VV, Anju MV, Athira PP, Archana K, Radhakrishnan CK, Philip R (2020) Structural, functional and phylogenetic analysis of a beta defensin gene from the Whipfin silverbiddy, Gerres filamentosus (Cuvier, 1829). Gene Rep 21:100805. https://doi.org/10.1016/j.genrep.2020.100805
[DOI: 10.1016/j.genrep.2020.100805]
Semple CA, Gautier P, Taylor K, Dorin JR (2006) The changing of the guard: molecular diversity and rapid evolution of β-defensins. Mol Divers 10:575–584. https://doi.org/10.1007/s11030-006-9031-7
[DOI: 10.1007/s11030-006-9031-7]
Peng K, Wang JH, Sheng JQ, Zeng LG, Hong YJ (2012) Molecular characterization and immune analysis of a defensin from freshwater pearl mussel, Hyriopsis schlegelii. Aquaculture 334:45–50. https://doi.org/10.1016/j.aquaculture.2011.12.039
[DOI: 10.1016/j.aquaculture.2011.12.039]
Chaturvedi P, Dhanik M, Pande A (2015) Molecular characterization and in silico analysis of defensin from Tor putitora (Hamilton). Probiotics Antimicrob Proteins 7:207–215. https://doi.org/10.1007/s12602-015-9197-3
[DOI: 10.1007/s12602-015-9197-3]
Montero-Alejo V, Acosta-Alba J, Perdomo-Morales R, Perera E, Hernández-Rodríguez EW, Estrada MP, Porto-Verdecia M (2012) Defensin like peptide from Panulirus argus relates structurally with beta defensin from vertebrates. Fish Shellfish Immunol 33:872–879. https://doi.org/10.1016/j.fsi.2012.07.013
[DOI: 10.1016/j.fsi.2012.07.013]
Bahar A, Ren D (2013) Antimicrobial peptides. Pharmaceuticals 6:1543–1575. https://doi.org/10.3390/ph6121543
[DOI: 10.3390/ph6121543]
Mótyán JA, Tóth F, Tőzsér J (2013) Research applications of proteolytic enzymes in molecular biology. Biomolecules 3:923–942. https://doi.org/10.3390/biom3040923
[DOI: 10.3390/biom3040923]
Grants
No.PL.(UGC)1/SPG/SMNRI/2017-18/Cochin University of Science and Technology