Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus

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In response to epidermal injury, Pavasilurus asotus, a catfish, secreted a strong antimicrobial peptide into the epithelial mucosal layer. The molecular mass of the antimicrobial peptide, named parasin I, was 2000.4 Die, as determined by matrix-associated laser desorption ionization mass spectrometry. The complete amino acid sequence of parasin I, which was determined by automated Edman degradation, was Lys-Gly-Arg-Gly-Lys-Gln-Gly-Gly-Lys-Val-Arg-Ala-Lys-Ala-Lys-Thr-Arg-Ser-Ser. Eighteen of the 19 residues ia parasin I sere identical to the N-terminal of buforin I, ct 39-residue antimicrobial peptide derived from the N-terminal of toad histone H2A [Kim et al, (1996) Biochem. Biophys. Res. Commun. 229, 381-387], which implies that parasin I was cleaved off from the N-terminal of catfish histone H2A, Parasin I showed strong antimicrobial activity, about 12-100 times more potent than magainin 2, against a wide spectrum of microorganisms, without any hemolytic activity, Circular dichroism spectra of parasin I indicated a structural content of 11% alpha-helix, 33% beta-sheet, and 56% random coils. The beta-sheet axial projection diagram of parasin I showed an amphipathic structure. Our results indicate that the catfish may produce parasin I from its histone H2A by a specific protease upon injury to protect against invasion by microorganisms. (C) 1998 Federation of European Biochemical Societies.
Publisher
ELSEVIER SCIENCE BV
Issue Date
1998-10
Language
English
Article Type
Article
Keywords

XENOPUS-LAEVIS; SKIN; DEFENSINS; CELLS; CDNA; ANTIBIOTICS; LACTOFERRIN; SECRETION; MELITTIN; FRAGMENT

Citation

FEBS LETTERS, v.437, no.3, pp.258 - 262

ISSN
0014-5793
URI
http://hdl.handle.net/10203/77611
Appears in Collection
BS-Journal Papers(저널논문)
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