Amino Acids

, Volume 46, Issue 11, pp 2561–2571 | Cite as

Vipericidins: a novel family of cathelicidin-related peptides from the venom gland of South American pit vipers

  • C. B. Falcao
  • B. G. de La Torre
  • C. Pérez-Peinado
  • A. E. Barron
  • D. AndreuEmail author
  • G. Rádis-BaptistaEmail author
Original Article


Cathelicidins are phylogenetically ancient, pleiotropic host defense peptides—also called antimicrobial peptides (AMPs)—expressed in numerous life forms for innate immunity. Since even the jawless hagfish expresses cathelicidins, these genetically encoded host defense peptides are at least 400 million years old. More recently, cathelicidins with varying antipathogenic activities and cytotoxicities were discovered in the venoms of poisonous snakes; for these creatures, cathelicidins may also serve as weapons against prey and predators, as well as for innate immunity. We report herein the expression of orthologous cathelicidin genes in the venoms of four different South American pit vipers (Bothrops atrox, Bothrops lutzi, Crotalus durissus terrificus, and Lachesis muta rhombeata)—distant relatives of Asian cobras and kraits, previously shown to express cathelicidins—and an elapid, Pseudonaja textilis. We identified six novel, genetically encoded peptides: four from pit vipers, collectively named vipericidins, and two from the elapid. These new venom-derived cathelicidins exhibited potent killing activity against a number of bacterial strains (S. pyogenes, A. baumannii, E. faecalis, S. aureus, E. coli, K. pneumoniae, and P. aeruginosa), mostly with relatively less potent hemolysis, indicating their possible usefulness as lead structures for the development of new anti-infective agents. It is worth noting that these South American snake venom peptides are comparable in cytotoxicity (e.g., hemolysis) to human cathelicidin LL-37, and much lower than other membrane-active peptides such as mastoparan 7 and melittin from bee venom. Overall, the excellent bactericidal profile of vipericidins suggests they are a promising template for the development of broad-spectrum peptide antibiotics.


Venom peptides Antimicrobial peptides Reptilian CRAMPs Vipericidins Peptide synthesis Therapeutic peptide 



Research at Federal University of Ceará supported by the Brazilian National Council for Scientific and Technological Development (CNPq), by the Ministry of Science and Technology, and by the Coordination for the Improvement of Higher Education Personnel (CAPES). Research at Pompeu Fabra University supported by the Spanish Ministry of Science and Innovation (SAF 2011-24899) and by Generalitat de Catalunya (SGR2009-00492). Mobility support from the European Commission, Marie Curie Actions—International Research Staff Exchange Scheme (no. 247513, MEMPEPACROSS), is gratefully acknowledged.

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

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Supplementary material 1 (TIFF 373 kb)
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Supplementary material 2 (DOC 105 kb)
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Supplementary material 3 (DOC 35 kb)
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Supplementary material 4 (DOC 35 kb)


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Copyright information

© Springer-Verlag Wien 2014

Authors and Affiliations

  • C. B. Falcao
    • 1
    • 2
  • B. G. de La Torre
    • 1
  • C. Pérez-Peinado
    • 1
  • A. E. Barron
    • 3
  • D. Andreu
    • 1
    Email author
  • G. Rádis-Baptista
    • 1
    • 2
    Email author
  1. 1.Department of Experimental and Health SciencesPompeu Fabra UniversityBarcelonaSpain
  2. 2.Laboratory of Biochemistry and Biotechnoloy, Institute for Marine SciencesFederal University of CearáFortalezaBrazil
  3. 3.Department of BioengineeringStanford UniversityStanfordUSA

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