| تعداد نشریات | 286 |
| تعداد نشریات سازمان | 84 |
| تعداد شماره‌ها | 3,028 |
| تعداد مقالات | 33,882 |
| تعداد مشاهده مقاله | 45,253,393 |
| تعداد دریافت فایل اصل مقاله | 60,281,285 |
Molecular Characterization of a Three-disulfide Bridges Beta-like Neurotoxin from Androctonus crassicauda Scorpion Venom | ||
| Archives of Razi Institute | ||
| مقاله 6، دوره 74، شماره 2، شهریور 2019، صفحه 135-142 اصل مقاله (451.3 K) | ||
| نوع مقاله: Original Articles | ||
| شناسه دیجیتال (DOI): 10.22092/ari.2018.105829.1028 | ||
| نویسنده | ||
| A. Jolodar* | ||
| Department of Basic Sciences, Biochemistry and Molecular Biology Section, Faculty of Veterinary Medicine, Shahid Chamran University of Ahvaz, Ahvaz, Iran | ||
| چکیده | ||
| Scorpion venom is the richest source of peptide toxins with high levels of specific interactions with different ion-channel membrane proteins. The present study involved the amplification and sequencing of a 310-bp cDNA fragment encoding a beta-like neurotoxin active on sodium ion-channel from the venom glands of scorpion Androctonus crassicauda belonging to the Buthidae family using reverse transcription polymerase chain reaction (RT-PCR) technique. The amplified complementary DNA (cDNA) fragment had a coding sequence of 240 bp. The deduced precursor open-reading frame was composed of 80 amino acid residues contain a signal peptide of 22 amino acid residues, followed by a mature toxin of 58 amino acids. It had a molecular mass of 6.84 kDa and isoelectric point of 4.58. The sequence similarity search revealed several matches with the scorpion toxin-like domain of toxin-3 superfamily with a homology range of 35- 75%. Multiple alignments and secondary structure prediction demonstrated that the toxin peptide deduced from the amplified cDNA was related to the long-chain neurotoxins in size but stabilized by three disulfide bridges instead of four. The level of difference implies that the corresponding genes have originated from a common ancestor. This level of difference may also confirm an evolutionary link between the ‘short-chain’ and ‘long-chain’ toxins. The analysis showed one major segment within this neurotoxin with maximal hydrophilicity which was predicted to be antigenic by inducing an antibody response. | ||
| کلیدواژه‌ها | ||
| Androctonus crassicauda؛ Beta-neurotoxin؛ Disulfide bridges | ||
| مراجع | ||
|
Altschul, S.F., Gish, W., Miller, W., Myers, E.W., Lipman, D.J., 1990. Basic local alignment search tool. J MolBiol 215, 403-410.
Bougis, P.E., Rochat, H., Smith, L.A., 1989. Precursors of Androctonus australis scorpion neurotoxins. Structures of precursors, processing outcomes, and expression of a functional recombinant toxin II. J Biol Chem 264, 19259-19265.
Carbone, E., Wanke, E., Prestipino, G., Possani, L.D., Maelicke, A., 1982. Selective blockage of voltage-dependent K+ channels by a novel scorpion toxin. Nature 296, 90-91.
DeBin, J.A., Maggio, J.E., Strichartz, G.R., 1993. Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion. Am J Physiol 264, C361-369.
Farajzadeh-Sheikh, A., Jolodar, A., Ghaemmaghami, S., 2013. Sequence characterization of cDNA sequence of encoding of an antimicrobial Peptide with no disulfide bridge from the Iranian mesobuthus eupeus venomous glands. Iran Red Crescent Med J 15, 36-41.
Finn, R.D., Tate, J., Mistry, J., Coggill, P.C., Sammut, S.J., Hotz, H.R., et al., 2008. The Pfam protein families database. Nucleic Acids Res 36, D281-288.
Jouirou, B., Mouhat, S., Andreotti, N., De Waard, M., Sabatier, J.M., 2004. Toxin determinants required for interaction with voltage-gated K+ channels. Toxicon 43, 909-914.
Jover, E., Couraud, F., Rochat, H., 1980. Two types of scorpion neurotoxins characterized by their binding to two separate receptor sites on rat brain synaptosomes. Biochem BiophResCom 95, 1607-1614.
Kelley, L.A., Sternberg, M.J., 2009. Protein structure prediction on the Web: a case study using the Phyre server. Nat Protoc 4, 363-371.
Kobayashi, Y., Takashima, H., Tamaoki, H., Kyogoku, Y., Lambert, P., Kuroda, H., et al., 1991. The cystine-stabilized alpha-helix: a common structural motif of ion-channel blocking neurotoxic peptides. Biopolymers 31, 1213-1220.
Kolaskar, A.S., Tongaonkar, P.C., 1990. A semi-empirical method for prediction of antigenic determinants on protein antigens. FEBS Lett 276, 172-174.
Kopeyan, C., Martinez, G., Rochat, H., 1979. Amino acid sequence of neurotoxin III of the scorpion Androctonus austrialis Hector. Eur J Biochem 94, 609-615.
Lebrun, B., Romi-Lebrun, R., Martin-Eauclaire, M.F., Yasuda, A., Ishiguro, M., Oyama, Y., et al., 1997. A four-disulphide-bridged toxin, with high affinity towards voltage-gated K+ channels, isolated from Heterometrus spinnifer (Scorpionidae) venom. Biochem J 328 ( Pt 1), 321-327.
Loret, E.P., Mansuelle, P., Rochat, H., Granier, C., 1990. Neurotoxins active on insects: amino acid sequences, chemical modifications, and secondary structure estimation by circular dichroism of toxins from the scorpion Androctonus australis Hector. Biochemistry 29, 1492-1501.
Martin-Eauclaire, M.F., Ceard, B., Bosmans, F., Rosso, J.P., Tytgat, J., Bougis, P.E., 2005. New "Birtoxin analogs" from Androctonus australis venom. Biochem Biophys Res Commun 333, 524-530.
Nakagawa, Y., Lee, Y.M., Lehmberg, E., Herrmann, R., Herrmann, R., Moskowitz, H., et al., 1997. Anti-insect toxin 5 (AaIT5) from Androctonus australis. Eur J Biochem 246, 496-501.
Rochat, C., Sampieri, F., Rochat, H., Miranda, F., Lissitzky, S., 1972. Iodination of neurotoxins I and II of the scorpion Androctonus australis Hector. Biochimie 54, 445-449.
Srinivasan, K.N., Gopalakrishnakone, P., Tan, P.T., Chew, K.C., Cheng, B., Kini, R.M., et al., 2002. SCORPION, a molecular database of scorpion toxins. Toxicon 40, 23-31.
Thompson, J.D., Higgins, D.G., Gibson, T.J., 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 22, 4673-4680.
Valdivia, H.H., Possani, L.D., 1998. Peptide Toxins as Probes of Ryanodine Receptor Structure and Function. Trends CardiovasMed 8, 111-118.
von Heijne, G., 1986. A new method for predicting signal sequence cleavage sites. Nucleic Acids Res 14, 4683-4690.
Zeng, X.C., Corzo, G., Hahin, R., 2005. Scorpion venom peptides without disulfide bridges. IUBMB Life 57, 13-21.
Zeng, X.C., Luo, F., Li, W.X., 2006. Molecular dissection of venom from Chinese scorpion Mesobuthus martensii: identification and characterization of four novel disulfide-bridged venom peptides. Peptides 27, 1745-1754.
Zeng, X.C., Wang, S.X., Zhu, Y., Zhu, S.Y., Li, W.X., 2004. Identification and functional characterization of novel scorpion venom peptides with no disulfide bridge from Buthus martensii Karsch. Peptides 25, 143-150.
Zhu, S., Gao, B., 2006. Molecular characterization of a new scorpion venom lipolysis activating peptide: Evidence for disulfide bridge-mediated functional switch of peptides. FEBS Lett 580, 6825-6836.
Zlotkin, E., Martinez, G., Rochat, H., Miranda, F., 1975. A protein toxic to crustacea from the venom of the scorpion Androctonus australis. Insect Biochemistry 5, 243-250.
Zlotkin, E., Rochat, H., Kopeyan, Miranda, F., Lissitzky, S., 1971. Purification and properties of the insect toxin from the venom of the scorpion Androctonus australis Hector. Biochimie 53, 1073-1078. | ||
|
آمار تعداد مشاهده مقاله: 1,776 تعداد دریافت فایل اصل مقاله: 1,959 |
||