Cloning and characterization of cDNAs that code for Na+ -channel-blocking toxins of the scorpion Centruroides noxius Hoffmann

Becerril, Baltazar; Vázquez, Arturo Pérez; García, Carlos Bosch; Corona, Miguel; Bolívar, Francisco; Possani, Lourival D.

doi:10.1016/0378-1119(93)90559-l

Cited by 40 publications

(24 citation statements)

References 19 publications

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“…This is consistent with the C-terminal amidation of urotoxin. According to the known processes that occur during expression of scorpion toxins (Becerril et al, 1993), the last residue of the peptide (glycine) is eliminated during the process of maturation, and the amino group of the glycine is used for amidation of the previous residue (resulting in this case in valinamide). Thus, we conclude that the complete amino acid sequence of mature urotoxin is GDIKCSGTRQCWGPCKKQTTCTNSKC-MNGKCKCYGCV*(G), where * means that valine (V) is amidated.…”

Section: Sequence Elucidationmentioning

confidence: 99%

Structure, Molecular Modeling, and Function of the Novel Potassium Channel Blocker Urotoxin Isolated from the Venom of the Australian Scorpion Urodacus yaschenkoi

et al. 2014

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This communication reports the structural and functional characterization of urotoxin, the first K 1 channel toxin isolated from the venom of the Australian scorpion Urodacus yaschenkoi. It is a basic peptide consisting of 37 amino acids with an amidated C-terminal residue. Urotoxin contains eight cysteines forming four disulfide bridges with sequence similarities resembling the a-potassium channel toxin 6 (a-KTx-6) subfamily of peptides; it was assigned the systematic number of a-KTx-6.21. Urotoxin is a potent blocker of human voltage-gated potassium channel (K v )1.2 channels, with an IC 50 of 160 pM, whereas its affinity for other channels tested was in the nanomolar range (hK v 1

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Section: Sequence Elucidationmentioning

confidence: 99%

Structure, Molecular Modeling, and Function of the Novel Potassium Channel Blocker Urotoxin Isolated from the Venom of the Australian Scorpion Urodacus yaschenkoi

et al. 2014

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“…The genomic organization of BmKKs deduced from these positive clones was highly similar to that of the other K + channel scorpion toxins: the gene consists of two exons disrupted by a single intron of 79 bp and this intron was located between the first and the second base of Ala codon at the end of signal peptide coding region (24). The A + T content of the intron was about 81% and was significantly higher than that of exons (59%) and was similar with that of 5'UTR and 3'UTR(81%), which had possibly been shown to play a great role in the process of splicing.…”

Section: Multicopy Of Bmkks Gene In Scorpion Chromosomementioning

confidence: 78%

“…PolyA + mRNA was purified using a polyA Tract mRNA Isolation System (Promega, USA) according to the manufacturer's specification. The total genomic DNA of Buthus martensii Karsch was extracted using proteinase incubation method as described (24).…”

Section: Methodsmentioning

confidence: 99%

Adaptive Evolution after Gene Duplication in α-KT × 14 Subfamily from Buthus martensii Karsch

Cao

Mao

et al. 2005

IUBMB Life (International Union of Biochemistry and Molecular B

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A series of isoforms of a-KT 6 14 (short chain potassium channel scorpion toxins) were isolated from the venom of Buthus martensii Karsch by RACE and screening cDNA library methods. These isoforms adding BmKK 1 -3 and BmSKTx 1 -2 together shared high homology (more than 97%) with each other. The result of genomic sequence analysis showed that a length 79bp intron is inserted Ala codes between the first and the second base at the 17th amino acid of signal peptide.

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“…The PCR product was cloned into the pGEM-T Easy T Overhang Vector System (Promega), and several positive clones were analyzed by nucleic acid sequencing (Sambrook et al, 1989). The total genomic DNA was isolated from scorpion and cloned by the method described previously (Becerril et al, 1993).…”

Section: Cdna and Genomic Cloningmentioning

confidence: 99%

Purification, characterization and functional expression of a new peptide with an analgesic effect from Chinese scorpion Buthus martensii Karsch (BmK AGP‐SYPU1)

Wang

Cui

et al. 2010

Biomedical Chromatography

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In this study, a new peptide named BmK AGP-SYPU1 with an analgesic effect was purified from the venom of Chinese scorpion Buthus martensi Karsch (BmK) through a four-step chromatographic process. The mouse twisting test was used to identify the target peptides in every separation step. The purified BmK AGP-SYPU1 was further qualified by RP-HPLC and HPCE. The molecular mass determined by the MALDI-4800-TOF/TOF MS for BmK AGP-SYPU1 was 7544 Da. Its primary structure of the N-terminal was obtained using Edman degradation. The gene sequence of BmK AGP-SYPU1 was cloned from the cDNA pool and genomic of scorpion glands, respectively, and then expressed in Escherichia coli. The sequence determination showed that BmK AGP-SYPU1 was composed of 66 amino acid residues with a new primary structure. The metal chelating affinity column and cation exchange chromatography were used to purify the recombinant BmK AGP-SYPU1. Consequently, the native and recombinant BmK AGP-SYPU1 showed similar analgesic effects on mice as assayed using a mouse twisting model. These results suggested that BmK AGP-SYPU1 is a new analgesic component found in the Chinese scorpion Buthus martensi Karsch.

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Cloning and characterization of cDNAs that code for Na+ -channel-blocking toxins of the scorpion Centruroides noxius Hoffmann

Cited by 40 publications

References 19 publications

Structure, Molecular Modeling, and Function of the Novel Potassium Channel Blocker Urotoxin Isolated from the Venom of the Australian Scorpion Urodacus yaschenkoi

Structure, Molecular Modeling, and Function of the Novel Potassium Channel Blocker Urotoxin Isolated from the Venom of the Australian Scorpion Urodacus yaschenkoi

Adaptive Evolution after Gene Duplication in α-KT × 14 Subfamily from Buthus martensii Karsch

Purification, characterization and functional expression of a new peptide with an analgesic effect from Chinese scorpion Buthus martensii Karsch (BmK AGP‐SYPU1)

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