β-Defensins from common goby (Pomatoschistusmicrops) and silver trevally (Pseudocaranxgeorgianus): Molecular characterization and phylogenetic analysis

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 p...

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Bibliographic Details
Published in:Molecular biology reports 2021-05, Vol.48 (5), p.4943-4951
Main Authors: Dhanya Lenin, K. L., Iyer, Rajeswary Vasu, Raveendran, Athira, Anju, M. V., Philip, Rosamma, Antony, Swapna P.
Format: Article
Language:English
Subjects:
Animal Anatomy
Animal Biochemistry
Antibiotic resistance
Antimicrobial agents
Antimicrobial peptides
Biological activity
Biomedical and Life Sciences
Defensins
Fish immunity
Histology
Innate immunity
Life Sciences
Morphology
mRNA
Pathogens
Peptides
Phylogenetics
Phylogeny
Polymerase chain reaction
Short Communication
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Summary: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.
ISSN:0301-4851
1573-4978
DOI:10.1007/s11033-021-06435-5