Isolation and characterization of Psalmopeotoxin I and II: two novel antimalarial peptides from the venom of the tarantula Psalmopoeus cambridgei
| Autor: | Marie-Louise Célérier, David M. Ojcius, Carole Guillaume, Jean-Michel Camadro, Romain Parent, Christiane Delarbre, Jean-Jacques Montagne, Soo Jin Choi, Jordi Molgó, Mohamed Amiche, Christiane Deregnaucourt, Catherine Guette, Aude Phelipot |
|---|---|
| Přispěvatelé: | Laboratoire d'Ingénierie des Protéines et Contrôle Métabolique, Centre National de la Recherche Scientifique (CNRS), Laboratoire de chimie et biochimie des substances naturelles, Muséum national d'Histoire naturelle (MNHN)-Centre National de la Recherche Scientifique (CNRS), Molécules de Communication et Adaptation des Micro-Organismes (MCAM), Muséum national d'Histoire naturelle (MNHN)-Institut National de la Santé et de la Recherche Médicale (INSERM)-Centre National de la Recherche Scientifique (CNRS), Laboratoire d'Immunologie Cellulaire, Laboratoire Ecologie et évolution, Centre National de la Recherche Scientifique (CNRS)-Université Pierre et Marie Curie - Paris 6 (UPMC)-École normale supérieure - Paris (ENS Paris), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL), Laboratoire de Bioactivation des Peptides, Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS), Laboratoire de neurobiologie cellulaire et moléculaire (NBCM), Institut de Neurobiologie Alfred Fessard (INAF), École normale supérieure - Paris (ENS-PSL), Université Paris sciences et lettres (PSL)-Université Paris sciences et lettres (PSL)-Université Pierre et Marie Curie - Paris 6 (UPMC)-Centre National de la Recherche Scientifique (CNRS) |
| Jazyk: | angličtina |
| Rok vydání: | 2004 |
| Předmět: |
Male
MESH: Sequence Homology Amino Acid Psalmopoeus cambridgei Neuromuscular transmission Spider Venoms Peptide Venom MESH: Amino Acid Sequence MESH: Base Sequence Biochemistry Structural Biology MESH: Animals Conserved Sequence MESH: Plasmodium falciparum chemistry.chemical_classification 0303 health sciences MESH: Conserved Sequence biology 030302 biochemistry & molecular biology Rana esculenta Spiders MESH: Spider Venoms 3. Good health MESH: Rana esculenta [SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC] Signal peptide Molecular Sequence Data Plasmodium falciparum Biophysics Neuromuscular Junction MESH: Sequence Alignment MESH: Spiders 03 medical and health sciences Antimalarials Genetics Animals Amino Acid Sequence Molecular Biology 030304 developmental biology MESH: Molecular Sequence Data Base Sequence Sequence Homology Amino Acid Tarantula venom Cell Biology biology.organism_classification Molecular biology MESH: Antimalarials In vitro MESH: Male Malaria ICK peptide chemistry MESH: Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Spectrometry Mass Matrix-Assisted Laser Desorption-Ionization Inhibitor cystine knot MESH: Neuromuscular Junction Sequence Alignment |
| Zdroj: | FEBS Letters FEBS Letters, Wiley, 2004, 572 (1-3), pp.109-117. ⟨10.1016/j.febslet.2004.07.019⟩ FEBS Letters, 2004, 572 (1-3), pp.109-117. ⟨10.1016/j.febslet.2004.07.019⟩ |
| ISSN: | 0014-5793 1873-3468 |
| DOI: | 10.1016/j.febslet.2004.07.019⟩ |
| Popis: | Two novel peptides that inhibit the intra-erythrocyte stage of Plasmodium falciparum in vitro were identified in the venom of the Trinidad chevron tarantula, Psalmopoeus cambridgei. Psalmopeotoxin I (PcFK1) is a 33-residue peptide and Psalmopeotoxin II (PcFK2) has 28-amino acid residues; both have three disulfide bridges and belong to the Inhibitor Cystine Knot superfamily. The cDNAs encoding both peptides were cloned, and nucleotide sequence analysis showed that the peptides are synthesized with typical signal peptides and pro-sequences that are cleaved at a basic doublet before secretion of the mature peptides. The IC(5O) of PcFK1 for inhibiting P. falciparum growth was 1.59+/-1.15 microM and that of PcFK2 was 1.15+/-0.95 microM. PcFK1 was adsorbed strongly to uninfected erythrocytes, but PcFK2 was not. Neither peptide has significant hemolytic activity at 10 microM. Electrophysiological recordings in isolated frog and mouse neuromuscular preparations revealed that the peptides (at up to 9.3 microM) do not affect neuromuscular transmission or quantal transmitter release. PcFK1 and PcFK2 do not affect the growth or viability of human epithelial cells, nor do they have any antifungal or antibacterial activity at 20 microM. Thus, PcFK1 and PcFK2 seem to interact specifically with infected erythrocytes. They could therefore be promising tools for antimalaria research and be the basis for the rational development of antimalarial drugs. |
| Databáze: | OpenAIRE |
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