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Isolation and characterisation of oncorhyncin II, a histone H1-derived antimicrobial peptide from skin secretions of rainbow trout, Oncorhynchus mykiss

Research output: Contribution to journalArticle

Author(s)

JMO Fernandes, G Molle, Graham Duncan Kemp, Valerie Jane Smith

School/Research organisations

Abstract

A potent antimicrobial peptide, tentatively named oncorhyncin II, was isolated from an acid extract of rainbow trout skin secretions. Amino acid sequencing showed that the first 17 residues of oncorhyncin II are identical to residues 138-154 of histone H1 from rainbow trout. Matrix-assisted laser desorption ionization mass spectrometry revealed that the purified peptide has a molecular mass of 7195.3 Da. Taken together, these data indicate that oncorhyncin II is a 69-residue C-terminal fragment of histone H1, probably phosphorylated at two residues. Oncorhyncin II has minimal inhibitory concentrations in the submicromolar range against Gram-(+) as well as Gram-(-) bacteria and it does not display significant haemolytic activity towards trout erythrocytes. The purified peptide was found to induce a marked destabilisation of planar lipid bilayers without the formation of stable ion channels. Oncorhyncin II is possibly a cleavage product of histone H1 with a potentially important role in mucosal defence of rainbow trout. (C) 2003 Elsevier Ltd. All rights reserved.

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Details

Original languageEnglish
Pages (from-to)127-138
Number of pages12
JournalDevelopmental and Comparative Immunology
Volume28
Issue number2
DOIs
Publication statusPublished - Feb 2004

    Research areas

  • mucosal immunity, antimicrobial peptide, trout, teleost, mucus, histone, ANTIBACTERIAL PEPTIDES, HOST-DEFENSE, FISH, MECHANISM, PROTEINS, SEQUENCE, BINDING, H1, PHOSPHORYLATION, VERTEBRATES

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