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Updated: May 16, 2026

Harvesting Venom Toxins from Assassin Bugs and Other Heteropteran Insects
Published on: April 21, 2018
Snake venom-like waprin from the frog of Ceratophrys calcarata contains antimicrobial function
Daixi Liu1, Yuwei Wang, Lin Wei
1Life Sciences College of Nanjing Agricultural University, Nanjing 210095, Jiangsu, China.
Abstract:
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, NVTPATKPTPSKPGYCRVMDELILCPDPPLSKDLCKNDSDCPGAQKCCYRTCIMQCLPPIFRE. 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.
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