Biochemical Journal · 2002 · 182 citations · 44 references
Life SciencesBiochemistryMicrobiologyFish BiologyIchthyologyMicrobial PhysiologyFish ImmunologyHistone ProteinsAmino Acid AnalysisAmino Acid Composition AnalysisAmino Acid Profile AnalysisAmino Acid SequencingFish BiochemistryFish Immune ResponsePeptide Mass SpectrometryReversed-phase Chromatography
Skin exudates of rainbow trout contain a potent 13.6 kDa anti-microbial protein which, from partial internal amino acid sequencing, peptide mass fingerprinting, matrix-associated laser desorption/ionization MS and amino acid analysis, seems to be histone H2A, acetylated at the N-terminus. The protein, purified to homogeneity by ion-exchange and reversed-phase chromatography, exhibits powerful anti-bacterial activity against Gram-positive bacteria, with minimal inhibitory concentrations in the submicromolar range. Kinetic analysis revealed that at a concentration of 0.3 microM all test bacteria lose viability after 30 min incubation. Weaker activity is also displayed against the yeast Saccharomyces cerevisiae. The protein is salt-sensitive and has no haemolytic activity towards trout erythrocytes at concentrations below 0.3 microM. Reconstitution of the protein in a planar lipid bilayer strongly disturbs the membrane but does not form stable ion channels, indicating that its anti-bacterial activity is probably not due to pore-forming properties. This is the first report to show that, in addition to its classical function in the cell, histone H2A has extremely strong anti-microbial properties and could therefore help contribute to protection against bacterial invasion.
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Stephen F. Altschul, Warren Gish, Webb Miller et al. · Journal of Molecular Biology · 1990 · 94.5K citations
Julie Thompson, Desmond G. Higgins, Toby J. Gibson · Nucleic Acids Research · 1994 · 64.9K citations · Full text
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Stephen F. Altschul · Journal of Molecular Biology · 1990 · 13.9K citations