References
- Hubner CA, Jentsch TJ. Ion channel diseases. Hum Mol Genet. 2002;11:2435–2445.
- Yogeeswari P, Ragavendran JV, Thirumurugan R, et al. Ion channels as important targets for antiepileptic drug design. Curr Drug Targets. 2004;5:589–602.
- Tfelt-Hansen J, Winkel BG, Grunnet M, et al. Inherited cardiac diseases caused by mutations in the Nav1.5 sodium channel. J Cardiovasc Electrophysiol. 2010;21:107–115.
- Cannon SC, Bean BP. Sodium channels gone wild: resurgent current from neuronal and muscle channelopathies. J Clin Invest. 2010;120:80–83.
- Cregg R, Momin A, Rugiero F, et al. Pain channelopathies. J Physiol. 2010;588:1897–1904.
- Toledo-Aral JJ, Moss BL, He Z-J, et al. Identification of PN1, a predominant voltage-dependent sodium channel expressed principally in peripheral neurons. Proc Natl Acad Sci U S A. 1997;94:1527–1532.
- Alexandrou AJ, Brown AR, Chapman ML, et al. Subtype-selective small molecule inhibitors reveal a fundamental role for Nav1.7 in nociceptor electrogenesis, axonal conduction and presynaptic release. PloS One. 2016;11:e0152405.
- Yang Y, Wang Y, Li S, et al. Mutations in SCN9A, encoding a sodium channel alpha subunit, in patients with primary erythermalgia. J Med Genet. 2004;41:171–174.
- Fertleman CR, Baker MD, Parker KA, et al. SCN9A mutations in paroxysmal extreme pain disorder: allelic variants underlie distinct channel defects and phenotypes. Neuron. 2006;52:767–774.
- Legroux-Crespel E, Sassolas B, Guillet G, et al. [Treatment of familial erythermalgia with the association of lidocaine and mexiletine]. Annales de dermatologie et de venereologie. 2003;130:429–433.
- Li QS, Cheng P, Favis R, et al. SCN9A variants may be implicated in neuropathic pain associated with diabetic peripheral neuropathy and pain severity. Clin J Pain. 2015;31:976–982.
- Reimann F, Cox JJ, Belfer I, et al. Pain perception is altered by a nucleotide polymorphism in SCN9A. Proc Natl Acad Sci U S A. 2010;107:5148–5153.
- Estacion M, Harty TP, Choi JS, et al. A sodium channel gene SCN9A polymorphism that increases nociceptor excitability. Ann Neurol. 2009;66:862–866.
- Vargas-Alarcon G, Alvarez-Leon E, Fragoso J-M, et al. A SCN9A gene-encoded dorsal root ganglia sodium channel polymorphism associated with severe fibromyalgia. BMC Musculoskelet Disord. 2012;13:23.
- Cox JJ, Reimann F, Nicholas AK, et al. An SCN9A channelopathy causes congenital inability to experience pain. Nature. 2006;444:894–898.
- Goldberg YP, MacFarlane J, MacDonald ML, et al. Loss-of-function mutations in the Nav1.7 gene underlie congenital indifference to pain in multiple human populations. Clin Genet. 2007;71:311–319.
- Sun J, Li L, Yang L, et al. Novel SCN9A missense mutations contribute to congenital insensitivity to pain: unexpected correlation between electrophysiological characterization and clinical phenotype. Mol Pain. 2020;16:1744806920923881.
- He W, Young GT, Zhang B, et al. Functional confirmation that the R1488* variant in SCN9A results in complete loss-of-function of Nav1.7. BMC Med Genet. 2018;19:124.
- Cox JJ, Sheynin J, Shorer Z, et al. Congenital insensitivity to pain: novel SCN9A missense and in-frame deletion mutations. Hum Mutat. 2010;31:E1670–1686.
- Kurban M, Wajid M, Shimomura Y, et al. A nonsense mutation in the SCN9A gene in congenital insensitivity to pain. Dermatology. 2010;221:179–183.
- Nilsen KB, Nicholas AK, Woods CG, et al. Two novel SCN9A mutations causing insensitivity to pain. Pain. 2009;143:155–158.
- Shorer Z, Wajsbrot E, Liran TH, et al. A novel mutation in SCN9A in a child with congenital insensitivity to pain. Pediatr Neurol. 2014;50:73–76.
- Wheeler DW, Lee MC, Harrison EK, et al. Case Report: neuropathic pain in a patient with congenital insensitivity to pain. F1000Res. 2014;3:135.
- Ahmad S, Dahllund L, Eriksson AB, et al. A stop codon mutation in SCN9A causes lack of pain sensation. Hum Mol Genet. 2007;16:2114–2121.
- Bogdanova-Mihaylova P, Alexander MD, Murphy RP, et al. SCN9A-associated congenital insensitivity to pain and anosmia in an Irish patient. J Peripher Nerv Syst: JPNS. 2015;20:86–87.
- Marchi M, Provitera V, Nolano M, et al. A novel SCN9A splicing mutation in a compound heterozygous girl with congenital insensitivity to pain, hyposmia and hypogeusia. J Peripher Nerv Syst: JPNS. 2018;23:202–206.
- Staud R, Price DD, Janicke D, et al. Two novel mutations of SCN9A (Nav1.7) are associated with partial congenital insensitivity to pain. Eur J Pain. 2011;15:223–230.
- Weiss J, Pyrski M, Jacobi E, et al. Loss-of-function mutations in sodium channel Nav1.7 cause anosmia. Nature. 2011;472:186–190.
- Bartholomew F, Lazar J, Marqueling A, et al. Channelopathy: a novel mutation in the SCN9A gene causes insensitivity to pain and autonomic dysregulation. Br J Dermatol. 2014;171:1268–1270.
- Yuan J, Matsuura E, Higuchi Y, et al. Hereditary sensory and autonomic neuropathy type IID caused by an SCN9A mutation. Neurology. 2013;80:1641–1649.
- Gingras J, Smith S, Matson DJ, et al. Global Nav1.7 knockout mice recapitulate the phenotype of human congenital indifference to pain. PloS One. 2014;9:e105895.
- Nassar MA, Stirling LC, Forlani G, et al. Nociceptor-specific gene deletion reveals a major role for Nav1.7 (PN1) in acute and inflammatory pain. Proc Natl Acad Sci U S A. 2004;101:12706–12711.
- Minett MS, Nassar MA, Clark AK, et al. Distinct Nav1.7-dependent pain sensations require different sets of sensory and sympathetic neurons. Nat Commun. 2012;3:791.
- Mulcahy JV, Pajouhesh H, Beckley JT, et al. Challenges and Opportunities for Therapeutics Targeting the Voltage-Gated Sodium Channel Isoform NaV1.7. J Med Chem. 2019;62:8695–8710.
- Lee JH, Park C-K, Chen G, et al. A monoclonal antibody that targets a NaV1.7 channel voltage sensor for pain and itch relief. Cell. 2014;157:1393–1404.
- Robinson SD, Undheim EAB, Ueberheide B, et al. Venom peptides as therapeutics: advances, challenges and the future of venom-peptide discovery. Expert Rev Proteomics. 2017;14:931–939.
- Dongol Y, Cardoso FC, Lewis RJ. Spider knottin pharmacology at voltage-gated sodium channels and their potential to modulate pain pathways. Toxins (Basel). 2019;11. DOI:https://doi.org/10.3390/toxins11110626.
- Langenegger N, Nentwig W, Kuhn-Nentwig L. Spider venom: components, modes of action, and novel strategies in transcriptomic and proteomic analyses. Toxins (Basel). 2019;11. DOI:https://doi.org/10.3390/toxins11100611.
- Wu T, Wang M, Wu W, et al. Spider venom peptides as potential drug candidates due to their anticancer and antinociceptive activities. J Venom Anim Toxins Incl Trop Dis. 2019;25:e146318.
- Goncalves TC, Benoit E, Partiseti M, et al. The NaV1.7 channel subtype as an antinociceptive target for spider toxins in adult dorsal root ganglia neurons. Front Pharmacol. 2018;9:1000.
- Saez NJ, Senff S, Jensen JE, et al. Spider-venom peptides as therapeutics. Toxins (Basel). 2010;2:2851–2871.
- Klint JK, Senff S, Rupasinghe DB, et al. Spider-venom peptides that target voltage-gated sodium channels: pharmacological tools and potential therapeutic leads. Toxicon: Offl J Int Soc Toxinol. 2012;60:478–491.
- Cardoso FC, Lewis RJ. Structure-function and therapeutic potential of spider venom-derived cysteine knot peptides targeting sodium channels. Front Pharmacol. 2019;10:366.
- Peng K, Shu Q, Liu Z, et al. Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena. J Biol Chem. 2002;277:47564–47571.
- Bosmans F, Rash L, Zhu S, et al. Four novel tarantula toxins as selective modulators of voltage-gated sodium channel subtypes. Mol Pharmacol. 2006;69:419–429.
- Deuis JR, Dekan Z, Wingerd JS, et al. Pharmacological characterisation of the highly NaV1.7 selective spider venom peptide Pn3a. Sci Rep. 2017;7:40883.
- Middleton RE, Warren VA, Kraus RL, et al. Two tarantula peptides inhibit activation of multiple sodium channels. Biochemistry. 2002;41:14734–14747.
- NCBI:txid29017, NCBI Taxonomy Browser, 1 Dec. 2020, <https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi>
- Xiao Y, Bingham J-P, Zhu W, et al. Tarantula huwentoxin-IV inhibits neuronal sodium channels by binding to receptor site 4 and trapping the domain ii voltage sensor in the closed configuration. J Biol Chem. 2008;283:27300–27313.
- Revell JD, Lund P-E, Linley JE, et al. Potency optimization of Huwentoxin-IV on hNav1.7: a neurotoxin TTX-S sodium-channel antagonist from the venom of the Chinese bird-eating spider Selenocosmia huwena. Peptides. 2013;44:40–46.
- Minassian NA, Gibbs A, Shih AY, et al. Analysis of the structural and molecular basis of voltage-sensitive sodium channel inhibition by the spider toxin huwentoxin-IV (mu-TRTX-Hh2a. J Biol Chem. 2013;288:22707–22720.
- Rahnama S, Deuis JR, Cardoso FC, et al. The structure, dynamics and selectivity profile of a NaV1.7 potency-optimised huwentoxin-IV variant. PloS One. 2017;12:e0173551.
- Neff RA, Flinspach M, Gibbs A, et al. Comprehensive engineering of the tarantula venom peptide huwentoxin-IV to inhibit the human voltage-gated sodium channel hNav1.7. J Biol Chem. 2020;295:1315–1327.
- Deng M, Luo X, Jiang L, et al. Synthesis and biological characterization of synthetic analogs of Huwentoxin-IV (Mu-theraphotoxin-Hh2a), a neuronal tetrodotoxin-sensitive sodium channel inhibitor. Toxicon: Offl J Int Soc Toxinol. 2013;71:57–65.
- Agwa AJ, Lawrence N, Deplazes E, et al. Spider peptide toxin HwTx-IV engineered to bind to lipid membranes has an increased inhibitory potency at human voltage-gated sodium channel hNaV1.7. Biochim Biophys Acta. 2017;1859:835–844.
- Xu H, Li T, Rohou A, et al. Structural Basis of Nav1.7 Inhibition by a Gating-Modifier Spider Toxin. Cell. 2019;176:1238–1239.
- Agwa AJ, Tran P, Mueller A, et al. Manipulation of a spider peptide toxin alters its affinity for lipid bilayers and potency and selectivity for voltage-gated sodium channel subtype 1.7. J Biol Chem. 2020;295:5067–5080.
- Shen H, Liu D, Wu K, et al. Structures of human Nav1.7 channel in complex with auxiliary subunits and animal toxins. Science. 2019;363:1303–1308.
- Tzakoniati F, Xu H, Li T, et al. Development of photocrosslinking probes based on huwentoxin-IV to map the site of interaction on Nav1.7. Cell Chem Biol. 2020;27:306–313 e304. .
- Gao S, Valinsky WC, On NC, et al. Employing NaChBac for cryo-EM analysis of toxin action on voltage-gated Na(+) channels in nanodisc. Proc Natl Acad Sci U S A. 2020;117:14187–14193.
- Murray JK, Biswas K, Holder JR, et al. Sustained inhibition of the NaV1.7 sodium channel by engineered dimers of the domain II binding peptide GpTx-1. Bioorg Med Chem Lett. 2015;25:4866–4871.
- Murray JK, Ligutti J, Liu D, et al. Engineering potent and selective analogues of GpTx-1, a tarantula venom peptide antagonist of the Na(V)1.7 sodium channel. J Med Chem. 2015;58:2299–2314.
- Murray JK, Long J, Zou A, et al. Single Residue Substitutions That Confer Voltage-Gated Sodium Ion Channel Subtype Selectivity in the NaV1.7 Inhibitory Peptide GpTx-1. J Med Chem. 2016;59:2704–2717.
- Biswas K, Nixey TE, Murray JK, et al. Engineering antibody reactivity for efficient derivatization to generate NaV1.7 Inhibitory GpTx-1 peptide-antibody conjugates. ACS Chem Biol. 2017;12:2427–2435.
- Deuis JR, Wingerd J, Winter Z, et al. Analgesic Effects of GpTx-1, PF-04856264 and CNV1014802 in a Mouse Model of NaV1.7-Mediated Pain. Toxins (Basel). 2016;8. DOI:https://doi.org/10.3390/toxins8030078.
- Chen C, Xu B, Shi X, et al. GpTx-1 and [Ala(5), Phe(6), Leu(26), Arg(28)]GpTx-1, two peptide NaV 1.7 inhibitors: analgesic and tolerance properties at the spinal level. Br J Pharmacol. 2018;175:3911–3927.
- Shcherbatko A, Rossi A, Foletti D, et al. Engineering Highly Potent and Selective Microproteins against Nav1.7 Sodium Channel for Treatment of Pain. J Biol Chem. 2016;291:13974–13986.
- Jalali A, Bosmans F, Amininasab M, et al. OD1, the first toxin isolated from the venom of the scorpion Odonthobuthus doriae active on voltage-gated Na+ channels. FEBS Lett. 2005;579:4181–4186.
- Mueller A, Starobova H, Morgan M, et al. Antiallodynic effects of the selective NaV1.7 inhibitor Pn3a in a mouse model of acute postsurgical pain: evidence for analgesic synergy with opioids and baclofen. Pain. 2019;160:1766–1780.
- Mueller A, Dekan Z, Kaas Q, et al. Mapping the Molecular Surface of the Analgesic NaV1.7-Selective Peptide Pn3a Reveals Residues Essential for Membrane and Channel Interactions. ACS Pharmacol Transl Sci. 2020;3:535–546.
- Schmalhofer WA, Calhoun J, Burrows R, et al. ProTx-II, a selective inhibitor of NaV1.7 sodium channels, blocks action potential propagation in nociceptors. Mol Pharmacol. 2008;74:1476–1484.
- Xiao Y, Blumenthal K, Jackson JO 2nd, et al. The tarantula toxins ProTx-II and huwentoxin-IV differentially interact with human Nav1.7 voltage sensors to inhibit channel activation and inactivation. Mol Pharmacol. 2010;78:1124–1134.
- Hackel D, Krug SM, Sauer R-S, et al. Transient opening of the perineurial barrier for analgesic drug delivery. Proc Natl Acad Sci U S A. 2012;109:E2018–2027.
- Black JA, Frezel N, Dib-Hajj SD, et al. Expression of Nav1.7 in DRG neurons extends from peripheral terminals in the skin to central preterminal branches and terminals in the dorsal horn. Mol Pain. 2012;8:82.
- Flinspach M, Xu Q, Piekarz AD, et al. Insensitivity to pain induced by a potent selective closed-state Nav1.7 inhibitor. Sci Rep. 2017;7:39662.
- Park JH, Carlin KP, Wu G, et al. Studies examining the relationship between the chemical structure of protoxin II and its activity on voltage gated sodium channels. J Med Chem. 2014;57:6623–6631.
- Flinspach M, Neff R, Liu Y, et al. Protoxin-II variants and methods of use. US20150099705. 2015.
- Flinspach M, Fellows R, Xu Q, et al. Protoxin-II Variants and Methods of Use. 2016.
- Chagot B, Escoubas P, Villegas E, et al. Solution structure of Phrixotoxin 1, a specific peptide inhibitor of Kv4 potassium channels from the venom of the theraphosid spider Phrixotrichus auratus. Protein Sci. 2004;13:1197–1208.
- Moyer BD, Murray JK, Ligutti J, et al. Pharmacological characterization of potent and selective NaV1.7 inhibitors engineered from Chilobrachys jingzhao tarantula venom peptide JzTx-V. PloS One. 2018;13:e0196791.
- Murray JK, Qian Y-X, Liu B, et al. Pharmaceutical optimization of peptide toxins for ion channel targets: potent, selective, and long-lived antagonists of Kv1.3. J Med Chem. 2015;58:6784–6802.
- Wu B, Murray JK, Andrews KL, et al. Discovery of tarantula venom-derived NaV1.7-Inhibitory JzTx-V Peptide 5-Br-Trp24 Analogue AM-6120 with Systemic Block of Histamine-Induced Pruritis. J Med Chem. 2018;61:9500–9512.
- Edwards W, Fung-Leung W-P, Huang C, et al. Targeting the ion channel Kv1.3 with scorpion venom peptides engineered for potency, selectivity, and half-life. J Biol Chem. 2014;289:22704–22714.
- Murray JK, Wu B, Tegley CM, et al. Engineering NaV1.7 Inhibitory JzTx-V Peptides with a potency and basicity profile suitable for antibody conjugation to enhance pharmacokinetics. ACS Chem Biol. 2019;14:806–818.