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Panusin represents a new family of β-defensin-like peptides in invertebrates
Montero-Alejo, V.; Corzo, G.; Porro-Suardiaz, J.; Pardo-Ruiz, Z.; Perera, E.; Rodriguez-Viera, L.; Sanchez-Diaz, G.; Alvarez, C.; Peigneur, S.; Tytgat, J.; Perdomo-Morales, R. (2017). Panusin represents a new family of β-defensin-like peptides in invertebrates. Dev. Comp. Immunol. 67: 310-321.
In: Developmental and Comparative Immunology. Elsevier: New York,. ISSN 0145-305X; e-ISSN 0145-305X, more
Peer reviewed article  

Available in  Authors 

Author keywords
    Invertebrate; Antimicrobial activity; Secondary structure; Proteinpurification; Membrane binding; Defensins

Authors  Top 
  • Montero-Alejo, V.
  • Corzo, G.
  • Porro-Suardiaz, J.
  • Pardo-Ruiz, Z.
  • Perera, E.
  • Rodriguez-Viera, L.
  • Sanchez-Diaz, G.
  • Alvarez, C.
  • Peigneur, S., more
  • Tytgat, J., more
  • Perdomo-Morales, R.

    Beta_defensin have been solely found in vertebrates until beta-defensin-like peptides were described as transcript isoforms in two species of Panulirus genus. They were considered as putative antimicrobials since their biological activity have not been demonstrated. Here we purified and characterized a defensin-like peptide from the hemocytes of spiny lobster P. argus, hereafter named panusin. Structurally, panusin presents a cysteine-stabilized alpha/beta motif, and is prone to form homodimers. Biological activity of panusin showed broad-spectrum antimicrobial activity, characterized for being strikingly salt-resistant. Panusin did not showed hemolytic activity but was demonstrated its binding capacity to different lipid membrane models, indicating amphipathicity of beta-sheet core as driving force for its antimicrobial activity. Panusin is considered a new kind of arthropod defensin which share structural and biological features with beta-defensin from vertebrates. The presence of beta-defensin like peptides in crustacean might suggest the emergence of the evolutionary relationship of beta-defensins from vertebrates.

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