A protein with antimicrobial activity in the skin of Schlegel's green tree frog Rhacophorus schlegelii (Rhacophoridae) identified as histone H2B |
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Authors: | Kawasaki Hiroaki Isaacson Todd Iwamuro Shawichi Conlon J Michael |
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Institution: | Department of Biology, Faculty of Science, Toho University, Funabashi, 274-8510, Chiba, Japan. |
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Abstract: | An extract of the skin of Schlegel's green tree frog, Rhacophorus schlegelii (Anura: Rhacophoridae), contained a protein that inhibited the growth of the Gram-negative bacterium Escherichia coli but was inactive against the Gram-positive bacterium Staphylococcus aureus. The protein was purified to near homogeneity by reverse-phase HPLC and amino acid sequence analysis of the products of an endoproteinase Glu-C digest identified the protein as histone H2B. The complete primary structure of the 125 amino acid residue Rhacophorus histone H2B was determined by nucleotide sequence analysis of a cloned cDNA encoding the protein. Mass spectrometry demonstrated that the protein isolated from the skin was not post-translationally modified. Histone fragments with antimicrobial activity were not identified in the Rhacophorus skin extract nor were cationic, alpha-helical antimicrobial peptides of the kind isolated from the skins of several other frog families. The data provide further evidence that histones play a role in the defense against microorganisms. |
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