Journal
GENE
Volume 514, Issue 2, Pages 99-104Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.gene.2012.11.007
Keywords
Amphibian; Skin; Venom; Antimicrobial; Innate immunity
Categories
Funding
- Chinese National Natural Science Foundation [30830021, 31070701, 31000960, 31025025, U1132601]
- Ministry of Science and Technology [2010CB529800, 2009ZX09103-1/091, 2011ZX09102-002-10]
- Yunnan Province [Y103951111]
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A 255-bp cDNA encoding an 84-amino acid residue (aa) precursor protein containing 8 half-cysteines was cloned from the skin of the frog, Ceratophrys calcarata. By sequence comparison and signal peptide prediction, the precursor was predicted to release a 63-aa mature peptide with amino acid sequence, NVTPATKPTPSK PGYCRVMDELILCPDPPLSKDLCKNDSDCPGAQKCCYRTCIMQCLPPIFRE. The mature was named ceratoxin. Ceratoxin shares significant sequence similarity with the toxin family of waprins containing the whey acidic protein-type (WAP) four-disulfide core domain found in snake venoms. Antimicrobial and trypsin-inhibitory abilities of recombinant ceratoxin were tested. Recombinant ceratoxin showed strong antimicrobial activities against wide spectrum of microorganisms including Gram-negative and Gram-positive bacteria and fungi. It had no serine protease-inhibitory activity. The current results suggested that the snake venom-like waprin with antimicrobial activities in the frog skin plays a role in innate immunity. (C) 2012 Elsevier B.V. All rights reserved.
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