Panusin represents a new family of β-defensin-like peptides in invertebrates.
Beta_defensin have been solely found in vertebrates until β-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 α/β 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 β-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 β-defensins from vertebrates.
Biochemistry Department, Center for Pharmaceuticals Research and Development, Havana, Cuba. Electronic address: vivian.montero@fq.uh.cu.
Vivian
V
Montero-Alejo
Departamento de Medicina Molecular y Bioprocesos, Instituto de Biotecnología, Universidad Nacional Autónoma de México, Mexico.
Gerardo
G
Corzo
Biochemistry Department, Center for Pharmaceuticals Research and Development, Havana, Cuba.
Javier
J
Porro-Suardíaz
Biochemistry Department, Center for Pharmaceuticals Research and Development, Havana, Cuba.
Zenia
Z
Pardo-Ruiz
Department of Fish Physiology and Biotechnology, Institute of Aquaculture Torre de la Sal (IATS-CSIC), Castellón, Spain.
Erick
E
Perera
Center for Marine Research, University of Havana, Havana, Cuba.
Leandro
L
Rodríguez-Viera
Department for Basic and Biomedical Sciences, Medicine Faculty, Artemisa, Cuba; Laboratory of Computational and Theoretical Chemistry, University of Havana, Havana, Cuba.
Gabriela
G
Sánchez-Díaz
Department for Basic and Biomedical Sciences, Medicine Faculty, Artemisa, Cuba; Laboratory of Computational and Theoretical Chemistry, University of Havana, Havana, Cuba.
Erix Wiliam
EW
Hernández-Rodríguez
Center for Protein Studies, Faculty of Biology, University of Havana, Havana, Cuba.
Carlos
C
Álvarez
Toxicology and Pharmacology, University of Leuven (KU Leuven), Leuven, Belgium.
Steve
S
Peigneur
Toxicology and Pharmacology, University of Leuven (KU Leuven), Leuven, Belgium.
Jan
J
Tytgat
Biochemistry Department, Center for Pharmaceuticals Research and Development, Havana, Cuba. Electronic address: rolando.perdomo@infomed.sld.cu.
Rolando
R
Perdomo-Morales
D000818:Animals; D000890:Anti-Infective Agents / Q000378:metabolism*; D060829:Arthropod Proteins / Q000235:genetics / Q000378:metabolism*; D005075:Biological Evolution; D019281:Dimerization; D006434:Hemocytes / Q000276:immunology*; D007448:Invertebrates; D033521:Palinuridae / Q000276:immunology*; D010802:Phylogeny; D011487:Protein Conformation; D040681:Structural Homology, Protein; D023083:beta-Defensins / Q000235:genetics / Q000378:metabolism*
D000890:Anti-Infective Agents; D060829:Arthropod Proteins; D023083:beta-Defensins
Antimicrobial activity; Defensins; Invertebrate; Membrane binding; Protein purification; Secondary structure