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Supplementary material Table information of scorpion peptide toxins mentioned in this paper


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Supplementary material
Table S1. Information of scorpion peptide toxins mentioned in this paper*


Toxin name Species Main targets References




α-KTx

Aam-KTX Androctonus amoreuxi Kv1.2, Kv1.3 [1]

KTX (Kaliotoxin) Androctonus mauretanicus BKCa, Kv1.3 [2]

NTX (Noxiustoxin) Centruroides noxius Kv1.1,Kv1.3, Shaker [3]

Css20 Centruroides suffusus Kv1.2 and Kv1.3 [4]

HsTx1 Heterometrus spinnifer Kv1.1, Kv1.3 [5]

LpII(GaTx2) Leiurus quinquestriatus ClC-2 channels [6]

LpIII Leiurus quinquestriatus n.d [7]

ChTX (Charybdotoxin) Leiurus quinquestriatus KCa1.1, KCa3.1, Kv [8]

AgTx-2 (Agitoxin-2) Leiurus quinquestriatus Kv1.1-Kv1.3 [9]

MeuTXKα1 Mesobuthus eupeus Kv1.1,Kv1.3, Shaker This work

MeuTXKα2 Mesobuthus eupeus n.d This work

MeuTXKα3 Mesobuthus eupeus n.d This work

MeuTXKα4 Mesobuthus eupeus n.d This work

BmP01 Mesobuthus martensii Kv1.1, Kv1.3, Shaker [10], this work

BmK86 Mesobuthus martensii Kv1.3 [11]

OdK-1 Odonthobuthus doriae Kv1.2 [12]

OsK-1 Orthochirus scrobiculosus Kv1.1-Kv1.3, KCa3.1 [13]

ADWX-1 Designed Kv1.1, Kv1.3 [14]

Mokatoxin-1 Designed Kv1.2, Kv1.3 [15]




β-KTx

HgeβKTx Hadrurus gertschi Cytolytic [16]

MeuTXKβ3 Mesobuthus eupeus n.d This work

MeuTXKβ4 Mesobuthus eupeus n.d This work

MeuTXKβ5 Mesobuthus eupeus n.d This work

BmTXKβ Mesobuthus martensii Kv4.2/Kv4.3 [17]

BmTXKβ2 Mesobuthus martensii n.d [17]

TcoKIK Tityus costatus n.d [16]

TdiKIK Tityus discrepans n.d [16]

TstβKTx Tityus serrulatus Kv1.1 [16]

TtrKIK Tityus trivittatus n.d [16]




γ-KTx

ErgTx (Ergtoxin) Centruroides noxius hERG [18]

BeKm-1 Mesobuthus eupeus hERG [19]


*Data source: [1] Abbas et al., 2008. Biochem Biophys Res Commun 376, 525-530; [2] Crest et al., 1992. J Biol Chem 267, 1640-1647; [3] Sitges et al., 1986. J Neurosci 6, 1570-1574; [4] Corzo et al., 2008. Biochem Pharmacol 76, 1142-1154; [5] Lebrun et al., 1997. Biochem J 328, 321-327; [6] Thompson et al., 2009. J Biol Chem 284, 26051-26062; [7] Buisine et al., 1997. J Pept Res 49, 545-555; [8] Miller et al., 1985. Nature 313, 316-318; [9] Garcia et al., 1994. Biochemistry 33, 6834-6839; [10] Romi-Lebrun et al., 1997. Eur J Biochem 245, 457-464; [11] Mao et al., 2007. Biochem Biophys Res Commun 360, 728-734; [12] Abdel-Mottaleb et al., 2006. FEBS Lett 580, 6254-6258; [13] Mouhat, et al., 2005. Biochem J 385, 95-104; [14] Han et al., 2008. J Biol Chem 283, 19058-19065; [15] Takacs et al., 2009. Proc Natl Acad Sci USA 106, 22211-22216; [16] Diego-García et al., Cell Mol Life Sci 65, 187-200; [17] Zhu & Gao 2006. FEBS Lett 580, 6825-6836; [18] Gurrola et al., 1999. FASEB J 13, 953-962; [19] Korolkova et al., 2001. J Biol Chem 276, 9868-9876.

Table S2. Information of ion channels mentioned in this paper


Channel name Gene Description

Shaker Shaker Drosophila voltage-gated K+ channel.

Kv1.1 KCNA1 Mammalian Shaker-type K+ channel, expressed in central nerve system (CNS), heart, retina, kidney, node of Ranvier, and pancreatic islet.

Kv1.2 KCNA2 Mammalian Shaker-type K+ channel, expressed in CNS, heart, and pancreatic islet.

Kv1.3 KCNA3 Mammalian Shaker-type K+ channel, expressed in lymphocyte (prominently), macrophages, microglia, osteoclasts, platelets, CNS, and lung. Kv1.3 is a therapeutic target for T cell-mediated autoimmune diseases.

Kv1.4 KCNA4 Mammalian Shaker-type K+ channel, expressed in CNS, heart, pancreatic islet, and skeletal/smooth muscle.

Kv1.5 KCNA5 Mammalian Shaker-type K+ channel, expressed in cardiac myocytes, CNS, kidney, lung, macrophages, and skeletal muscle.

Kv1.6 KCNA6 Mammalian Shaker-type K+ channel, expressed in spinal cord and CNS.

hERG(Kv11.1) KCNH2 Human ether-a-go-go-related K+ channels, expressed in heart and CNS.

Kv4.2 KCND2 Mammalian voltage-gated K+ channel, expressed in CNS

Kv4.3 KCND3 Mammalian voltage-gated K+ channel, expressed in CNS and smooth muscle.

SKCa KCNN2-3 Small conductance Ca2+-activatd K+ channels, expressed in CNS and sensitive to apamin.



*Data source: Shieh et al., 2000. Pharmacol Rev 52, 557-594; Wulff et al., 2009. Nat Rev Drug Discov 8, 982-1001.


Table S3. The expression of K+ channel cDNAs in Xenopus oocytes


Clone Vector RE* Promoter

rKv1.1 pGEM-HE Pst I T7

rKv1.2 pAKS Sph I T7

rKv1.3 pGEM Sal I T7

hKv1.3 pCI.neo Not I T7



rKv1.4 pGEM-HE Not I T7

rKv1.5 pGEM-HE Sal I T7

rKv1.6 pGEM-HE Nde I T7

Shaker IR pGEM-HE Nhe I T7

hERG pSP64 Eco RI SP6

Note: *RE: restriction endonuclease.




Figure S1. Schematic representation of Ka/Ks of pair orthologous genes between M. martensii and M. eupeus. The number of synonymous (Ks) and nonsynonymous substitutions (Ka) per site was calculated from the signal peptide and the mature peptide coding regions, respectively, by K-Estimator 6.1 (Comeron, 1999. Bioinformatics 15, 763-764). All calculated Ka/Ks values approach one and are significantly larger than the values calculated from their own signal peptides. Higher substitution rate in nonsynonymous sites of the mature peptide-coding region than in those of the signal peptide-coding region suggests that accelerated amino acid changes have occurred in these two types of KTxs after divergence between M. eupeus and M. martensii, an evolutionary phenomenon initially observed in the β-defensin family (Morrison et al., 2003. Mol Biol Evol 20, 460-470).





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