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001-es BibID:	BIBFORM102212
035-os BibID:	(cikkazonosító)115023 (WoS)000793623600002 (Scopus)85127510848
Első szerző:	Csóti Ágota (biológus)
Cím:	sVmKTx, a transcriptome analysis-based synthetic peptide analogue of Vm24, inhibits Kv1.3 channels of human T cells with improved selectivity / Csoti Agota, del Carmen Nájera Meza Rosby, Bogár Ferenc, Tajti Gabor, Szanto Tibor G., Varga Zoltan, Gurrola Georgina B., Tóth Gábor K., Possani Lourival D., Panyi Gyorgy
Dátum:	2022
ISSN:	0006-2952
Megjegyzések:	Kv1.3 K+ channels play a central role in the regulation of T cell activation and Ca2+ signaling under physiological and pathophysiological conditions. Peptide toxins targeting Kv1.3 have a significant therapeutic potential in the treatment of autoimmune diseases; thus, the discovery of new toxins is highly motivated. Based on the transcriptome analysis of the venom gland of V. mexicanus smithi a novel synthetic peptide, sVmKTx was generated, containing 36 amino acid residues. sVmKTx shows high sequence similarity to Vm24, a previously characterized peptide from the same species, but contains a Glu at position 32 as opposed to Lys32 in Vm24. Vm24 inhibits Kv1.3 with high affinity (Kd = 2.9 pM). However, it has limited selectivity (~1,500-fold) for Kv1.3 over hKv1.2, hKCa3.1, and mKv1.1. sVmKTx displays reduced Kv1.3 affinity (Kd = 770 pM) but increased selectivity for Kv1.3 over hKv1.2 (~9,000-fold) as compared to Vm24, other channels tested in the panel (hKCa3.1, hKv1.1, hKv1.4, hKv1.5, rKv2.1, hKv11.1, hKCa1.1, hNav1.5) were practically insensitive to the toxin at 2.5 ?M. Molecular dynamics simulations showed that introduction of a Glu instead of Lys at position 32 led to a decreased structural fluctuation of the N-terminal segment of sVmKTx, which may explain its increased selectivity for Kv1.3. sVmKTx at 100 nM concentration decreased the expression level of the Ca2+ -dependent T cell activation marker, CD40 ligand. The high affinity block of Kv1.3 and increased selectivity over the natural peptide makes sVmKTx a potential candidate for Kv1.3 blockade-mediated treatment of autoimmune diseases.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Kv1.3 Toxin-channel interaction T-cell activation Patch-clamp Ion channel selectivity Scorpion toxin
Megjelenés:	Biochemical Pharmacology. - 199 (2022), p. 1-14. -
További szerzők:	del Carmen Nájera Meza, Rosby Bogár Ferenc Tajti Gábor (1988-) (gyógyszerész, biofizikus, sejtbiológus) Szántó Gábor Tibor (1980-) (vegyész) Varga Zoltán (1969-) (biofizikus, szakfordító) Gurrola-Briones, Georgina Tóth Gábor K. Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Pályázati támogatás:	143071 OTKA K119417 OTKA K132906 OTKA EFOP-3.6.2-16-2017-00006 EFOP GINOP-2.3.2-15-2016-00044 GINOP PRONACE303045 from National Conseil of Science and Technology of Mexico Egyéb Ministry of Human Capacities, Hungary grant, TKP-2020 Egyéb
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001-es BibID:	BIBFORM083629
035-os BibID:	(WoS)000518872600011 (Scopus)85078049471 (PMID)31870846
Első szerző:	Jin, Jiayi
Cím:	Weaponisation 'on the fly' : convergent recruitment of knottin and defensin peptide scaffolds into the venom of predatory assassin flies / Jiayi Jin, Akello J. Agwa, G. Tibor Szanto, Agota Csóti, Gyorgy Panyi, Christina I. Schroeder, Andrew A. Walker, Glenn F. King
Dátum:	2020
ISSN:	0965-1748
Megjegyzések:	Many arthropod venom peptides have potential as bioinsecticides, drug leads, and pharmacological tools due to their specific neuromodulatory functions. Assassin flies (Asilidae) are a family of predaceous dipterans that produce a unique and complex peptide-rich venom for killing insect prey and deterring predators. However, very little is known about the structure and function of their venom peptides. We therefore used an E. coli periplasmic expression system to express four disulfide-rich peptides that we previously reported to exist in venom of the giant assassin fly Dolopus genitalis. After purification, each recombinant peptide eluted from a C18 column at a position closely matching its natural counterpart, strongly suggesting adoption of the native tertiary fold. Injection of purified recombinant peptides into blowflies (Lucilia cuprina) and crickets (Acheta domestica) revealed that two of the four recombinant peptides, named rDg3b and rDg12, inhibited escape behaviour in a manner that was rapid in onset (<1 min) and reversible. Homonuclear NMR solution structures revealed that rDg3b and rDg12 adopt cystine-stabilised α/ß defensin and inhibitor cystine knot folds, respectively. Although the closest known homologues of rDg3b at the level of primary structure are dipteran antimicrobial peptides such as sapecin and lucifensin, a DALI search showed that the tertiary structure of rDg3b most closely resembles the KV11.1-specific α-potassium channel toxin CnErg1 from venom of the scorpion Centruroides noxius. This is mainly due to the deletion of a large, unstructured loop between the first and second cysteine residues present in Dg3b homologues from non-asiloid, but not existing in asiloid, species. Patch-clamp electrophysiology experiments revealed that rDg3b shifts the voltage-dependence of KV11.1 channel activation to more depolarised potentials, but has no effect on KV1.3, KV2.1, KV10.1, KCa1.1, or the Drosophila Shaker channel. Although rDg12 shares the inhibitor cystine knot structure of many gating modifier toxins, rDg12 did not affect any of these KV channel subtypes. Our results demonstrate that multiple disulfide-rich peptide scaffolds have been convergently recruited into asilid and other animal venoms, and they provide insight into the molecular evolution accompanying their weaponisation.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Diptera Dolopus genitalis Ion channel K(V)11.1 (hERG) Toxin
Megjelenés:	Insect Biochemistry and Molecular Biology. - 118 (2020), p. 1-12. -
További szerzők:	Agwa, Akello J. Szántó Gábor Tibor (1980-) (vegyész) Csóti Ágota (1989-) (biológus) Panyi György (1966-) (biofizikus) Schroeder, Christina I. Walker, Andrew A. King, Glenn F.
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001-es BibID:	BIBFORM103992
035-os BibID:	(cikkazonosító)10533 (scopus)85138397388 (wos)000857594300001
Első szerző:	Mészáros Beáta (molekuláris biológus, mikrobiológus)
Cím:	The hEag1 K+ Channel Inhibitor Astemizole Stimulates Ca2+ Deposition in SaOS-2 and MG-63 Osteosarcoma Cultures / Mészáros Beáta, Csoti Agota, Szanto Tibor G., Telek Andrea, Kovács Katalin, Toth Agnes, Volkó Julianna, Panyi Gyorgy
Dátum:	2022
ISSN:	1422-0067
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	International Journal Of Molecular Sciences. - 23 : 18 (2022), p. 1-19. -
További szerzők:	Csóti Ágota (1989-) (biológus) Szántó Gábor Tibor (1980-) (vegyész) Telek Andrea (1977-) (élettanász) Kovács Katalin (1978-) (biokémikus) Tóth Ágnes (1983-) (biofizikus) Volkó Julianna (1983-) (biotechnológus) Panyi György (1966-) (biofizikus)
Pályázati támogatás:	EFOP- 3.6.2- 16-2017-00006 EFOP GINOP-2.3.2-15-2016-00044 GINOP K143071 OTKA
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001-es BibID:	BIBFORM091018
Első szerző:	Tajti Gábor (gyógyszerész, biofizikus, sejtbiológus)
Cím:	Immunomagnetic separation is a suitable method for electrophysiology and ion channel pharmacology studies on T cells / Gabor Tajti, Tibor Gabor Szanto, Agota Csoti, Greta Racz, César Evaristo, Peter Hajdu, Gyorgy Panyi
Dátum:	2021
ISSN:	1933-6950 1933-6969
Megjegyzések:	Ion channels play pivotal role in the physiological and pathological function of immune cells. As immune cells represent a functionally diverse population, subtype-specific functional studies, such as single-cell electrophysiology require proper subset identification and separation. Magneticactivated cell sorting (MACS) techniques provide an alternative to fluorescence-activated cell sorting (FACS), however, the potential impact of MACS-related beads on the biophysical and pharmacological properties of the ion channels were not studied yet. We studied the aforementioned properties of the voltage-gated Kv1.3 K+ channel in activated CD4+ T-cells as well as the membrane capacitance using whole-cell patch-clamp following immunomagnetic positive separation, using the REAlease? kit. This kit allows three experimental configurations: bead-bound configuration, bead-free configuration following the removal of magnetic beads, and the labelfree configuration following removal of CD4 recognizing antibody fragments. As controls, we used FACS separation as well as immunomagnetic negative selection. The membrane capacitance and of the biophysical parameters of Kv1.3 gating, voltage-dependence of steady-state activation and inactivation kinetics of the current were not affected by the presence of MACS-related compounds on the cell surface. We found subtle differences in the activation kinetics of the Kv1.3 current that could not be explained by the presence of MACS-related compounds. Neither the equilibrium block of Kv1.3 by TEA+ or charybdotoxin (ChTx) nor the kinetics of ChTx block are affected by the presence of the magnetics beads on the cell surface. Based on our results MACS is a suitable method to separate cells for studying ion channels in non-excitable cells, such as T-lymphocytes.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Kv1.3 cd4+ T-cell magneticactivated cell sorting macs immunomagnetic separation fluorescenceactivated cell sorting facs
Megjelenés:	Channels. - 15 : 1 (2021), p. 53-66. -
További szerzők:	Szántó Gábor Tibor (1980-) (vegyész) Csóti Ágota (1989-) (biológus) Rácz Gréta Evaristo, César Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus)
Pályázati támogatás:	OTKA K119417 Egyéb EFOP-3.6.2-16-2017-00006 EFOP GINOP-2.3.2-15-2016-00015 GINOP NKFIH K128525 Egyéb Bolyai Research Fellowship Egyéb
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