Abstract
Antimicrobial peptides (AMPs) derived from histone precursors form a significant class of therapeutic molecules. The study explores the comprehensive molecular characterization of core histone H2A-derived antimicrobial peptide, Etroplusin from Pearl spot, Etroplus suratensis. Etroplusin exhibited characteristic features of AMP such as net +11 charge and amphipathic alpha-helical structure. Multiple sequence alignment showed the homologous nature of etroplusin with previously reported H2A peptides. Phylogenetic analysis revealed that etroplusin is similar to Carassius auratus H2A-derived peptide and comes under the fish H2A peptide clade. Structure modelling with bioinformatics tools predicted alpha-helical structure and random coils with a proline hinge. The functional characterization of etroplusin revealed its antibacterial, antifungal, and anticancer activities. Significant upregulation of etroplusin was observed in the systemic tissues of E. suratensis on a challenge with the bacterial fish pathogen, Streptococcus agalactiae. The present study will shed light on fish innate immune responses and the importance of etroplusin, the H2A-derived peptide as a defense molecule.
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