A novel beta-defensin 1-like antimicrobial peptide (β-defensin 1TB) containing 36 amino acid residues was purified and characterized from the serum of the tree shrew, Tupaia belangeri. Its amino acid sequence was determined as DHYLCVKNEGICLYSSCPSYTKIEGTCYGGKAKCCK, by Edman degradation, mass spectrometry analysis, and cDNA cloning. Evolution analysis indicated that β-defensin 1TB showed maximal similarity to the β-defensin 1 identified from cotton-top tamarin, Saguinus oedipus. β-defensin 1TB exerted potential antimicrobial activities against wide spectrum of microorganisms including Gram-negative and -positive bacteria and fungi. It showed little hemolitic activity to human or rabbit red cells. To the best of our knowledge, this is the first report of antimicrobial peptide from Tupaiidae.
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