TY - JOUR
T1 - Insecticidal peptides from the theraposid spider Brachypelma albiceps
T2 - An NMR-based model of Ba2
AU - Corzo, Gerardo
AU - Bernard, Cedric
AU - Clement, Herlinda
AU - Villegas, Elba
AU - Bosmans, Frank
AU - Tytgat, Jan
AU - Possani, Lourival D.
AU - Darbon, Herve
AU - Alagón, Alejandro
N1 - Funding Information:
We are grateful to Benjamin Chagot for fruitful discussion on NMR data analysis. The confirmation of the amino acid sequence of Ba1 and 2 by Dr. Fernando Zamudio and the mass spectrometry determination conducted by Dr. Cesar Batista are greatly acknowledged. We would also like to thank Martin S. Williamson, IACR-Rothamsted, UK for the Para and tipE clone; A.L. Goldin, Univ. of California, Irvine, USA for Na v 1.2; R.G. Kallen, Univ. of Pennsylvania, Philadelphia, USA for Na v 1.5 and S.H. Heinemann, Friedrich-Schiller-Universität Jena, Germany for the β 1 subunit. This work was supported in part by a grant from MEXUS P-191 and CONACyT 49773/24968 to G.C. J.T. was supported by the following grants: G.0330.06 (FWO-Vlaanderen), OT-05-64 (KULeuven) and P6/31 (Interuniversity Attraction Poles Programme-Belgian State-Belgian Science Policy).
PY - 2009/8
Y1 - 2009/8
N2 - Soluble venom and purified fractions of the theraposid spider Brachypelma albiceps were screened for insecticidal peptides based on toxicity to crickets. Two insecticidal peptides, named Ba1 and Ba2, were obtained after the soluble venom was separated by high performance liquid chromatography and cation exchange chromatography. The two insecticidal peptides contain 39 amino acid residues and three disulfide bonds, and based on their amino acid sequence, they are highly identical to the insecticidal peptides from the theraposid spiders Aphonopelma sp. from the USA and Haplopelma huwenum from China indicating a relationship among these genera. Although Ba1 and Ba2 were not able to modify currents in insect and vertebrate cloned voltage-gated sodium ion channels, they have noteworthy insecticidal activities compared to classical arachnid insecticidal toxins indicating that they might target unknown receptors in insect species. The most abundant insecticidal peptide Ba2 was submitted to NMR spectroscopy to determine its 3-D structure; a remarkable characteristic of Ba2 is a cluster of basic residues, which might be important for receptor recognition.
AB - Soluble venom and purified fractions of the theraposid spider Brachypelma albiceps were screened for insecticidal peptides based on toxicity to crickets. Two insecticidal peptides, named Ba1 and Ba2, were obtained after the soluble venom was separated by high performance liquid chromatography and cation exchange chromatography. The two insecticidal peptides contain 39 amino acid residues and three disulfide bonds, and based on their amino acid sequence, they are highly identical to the insecticidal peptides from the theraposid spiders Aphonopelma sp. from the USA and Haplopelma huwenum from China indicating a relationship among these genera. Although Ba1 and Ba2 were not able to modify currents in insect and vertebrate cloned voltage-gated sodium ion channels, they have noteworthy insecticidal activities compared to classical arachnid insecticidal toxins indicating that they might target unknown receptors in insect species. The most abundant insecticidal peptide Ba2 was submitted to NMR spectroscopy to determine its 3-D structure; a remarkable characteristic of Ba2 is a cluster of basic residues, which might be important for receptor recognition.
KW - Insecticidal peptide
KW - NMR structure
KW - Spider venom
KW - Theraposid
UR - https://www.scopus.com/pages/publications/67349224086
UR - https://www.scopus.com/pages/publications/67349224086#tab=citedBy
U2 - 10.1016/j.bbapap.2009.04.004
DO - 10.1016/j.bbapap.2009.04.004
M3 - Article
C2 - 19374957
AN - SCOPUS:67349224086
SN - 1570-9639
VL - 1794
SP - 1190
EP - 1196
JO - Biochimica et Biophysica Acta - Proteins and Proteomics
JF - Biochimica et Biophysica Acta - Proteins and Proteomics
IS - 8
ER -