title: Defensin like peptide from Panulirus argus relates structurally with beta defensin from vertebrates.
abstract: Naturally occurring antimicrobial peptides take place in the first line of host defense against pathogen as part of the humoral innate immune response. β-defensins are among the most abundant antimicrobial peptides in mammals, and thought to be solely found in vertebrates until a recent report describing the cloning and sequencing of defensin like peptides in the spiny lobster Panulirus japonicus. In the current study, we cloned and sequenced two genes from the hemocytes of the spiny lobster Panulirus argus encoding for two isoforms of defensin-like peptides, thus confirming the presence of this protein in the Panulirus genus. The 44 amino acids mature peptides showed the conservation of cysteine pattern characterizing the β-defensins, as well as known amino acids residues critical to exert their antimicrobial activity. They are also amphipathics, hydrophobics, and display an overall positive charge (+1) located at the C-terminus. The tertiary structure obtained by homology modeling indicated that likely conformations of lobster peptides are highly similar to β-defensins from vertebrates. The phylogenetic study carried out by probabilistic methods confirmed the relation with ancestral β-defensin from vertebrates. The finding of a putative defensin-like peptide in the expressed sequence tag (EST) of the lobster Homarus americanus with high homology with those of P. argus described in this study, would indicate the presence of this peptides in Palinuridae family. Taking into account all similarities between these peptides with β-defensins from vertebrates, it is conceivable to further support the finding of a new family of β-defensins in invertebrate.
authors.affiliation: Biochemistry Department, Center for Pharmaceuticals Research and Development, Ave. 26, No. 1605, CP 10 400 Habana, Cuba. vivian.montero@fq.uh.cu
authors.forename: V
authors.initials: V
authors.lastname: Montero-Alejo
authors.forename: J
authors.initials: J
authors.lastname: Acosta-Alba
authors.forename: R
authors.initials: R
authors.lastname: Perdomo-Morales
authors.forename: E
authors.initials: E
authors.lastname: Perera
authors.forename: E W
authors.initials: EW
authors.lastname: Hernández-Rodríguez
authors.forename: M P
authors.initials: MP
authors.lastname: Estrada
authors.forename: M
authors.initials: M
authors.lastname: Porto-Verdecia
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D060829:Arthropod Proteins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D001483:Base Sequence; D003001:Cloning, Molecular; D003198:Computer Simulation; D023082:Defensins / Q000737:chemistry / Q000235:genetics* / Q000378:metabolism; D020224:Expressed Sequence Tags; D006434:Hemocytes / Q000378:metabolism; D008969:Molecular Sequence Data; D008121:Nephropidae / Q000737:chemistry / Q000235:genetics; D033521:Palinuridae / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D016133:Polymerase Chain Reaction; D020033:Protein Isoforms / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D023083:beta-Defensins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism
chemical_list: D060829:Arthropod Proteins; D023082:Defensins; D020033:Protein Isoforms; D023083:beta-Defensins