Abhisin: a potential antimicrobial peptide derived from histone H2A of disk abalone (Haliotis discus discus)

Antimicrobial peptides (AMPs) play an important role in the immune defense against pathogenic microorganisms. In this study, a histone H2A full-length cDNA was cloned from disk abalone Haliotis discus discus. We identified a 40-amino acid AMP designated as abhisin from the N-terminus of the abalone histone H2A sequence. Abhisin shows the characteristic features of AMPs including net positive charge (+13), higher hydrophobic residues (27%) and 2.82 kcal/mol protein binding potential. Abhisin shares 80% amino acid identity with the buforin I peptide that is derived from Asian toad histone H2A. We synthesized the synthetic peptide of abhisin, and characterized its antimicrobial activities. Our results showed the growth inhibition of Gram positive (G+) Listeria monocytogenes, Gram negative (G-) Vibrio ichthyoenteri bacteria, and fungi (yeast) Pityrosporum ovale by abhisin treatment at 250 microg/mL. However, stronger activity was displayed against the G+ than G- bacteria. Additionally, scanning electron microscope (SEM) observation results confirmed that P. ovale cells were damaged by abhisin treatment. Interestingly, abhisin treatment (50 microg/mL) decreased the viability of THP-1 leukemia cancer cells approximately by 25% but there was no effect on the normal vero cells, suggesting that abhisin has cytotoxicity against cancer cells but not normal cells. Quantitative real time RT-PCR results revealed that histone H2A transcription was significantly induced at 3 h post-infection with bacteria in abalone gills and digestive tract. These results suggest that abhisin is a potential antimicrobial agent, and its precursor histone H2A may be involved in the innate immune defense system in abalone.