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001-es BibID:	BIBFORM113131
035-os BibID:	(cikkazonosító)121 (scopus)85160315499 (wos)000994418900002
Első szerző:	Ashwood, Lauren M.
Cím:	Genomic, functional and structural analyses elucidate evolutionary innovation within the sea anemone 8 toxin family / Ashwood Lauren M., Elnahriry Khaled A., Stewart Zachary K., Shafee Thomas, Naseem Muhammad Umair, Szanto Tibor G., van der Burg Chloé A., Smith Hayden L., Surm Joachim M., Undheim Eivind A. B., Madio Bruno, Hamilton Brett R., Guo Shaodong, Wai Dorothy C. C., Coyne Victoria L., Phillips Matthew J., Dudley Kevin J., Hurwood David A., Panyi Gyorgy, King Glenn F., Pavasovic Ana, Norton Raymond S., Prentis Peter J.
Dátum:	2023
ISSN:	1741-7007
Megjegyzések:	Background The ShK toxin from Stichodactyla helianthus has established the therapeutic potential of sea anemone venom peptides, but many lineage-specific toxin families in Actiniarians remain uncharacterised. One such peptide family, sea anemone 8 (SA8), is present in all five sea anemone superfamilies. We explored the genomic arrangement and evolution of the SA8 gene family in Actinia tenebrosa and Telmatactis stephensoni, characterised the expression patterns of SA8 sequences, and examined the structure and function of SA8 from the venom of T. stephensoni. Results We identified ten SA8-family genes in two clusters and six SA8-family genes in five clusters for T. stephen- soni and A. tenebrosa, respectively. Nine SA8 T. stephensoni genes were found in a single cluster, and an SA8 peptide encoded by an inverted SA8 gene from this cluster was recruited to venom. We show that SA8 genes in both spe- cies are expressed in a tissue-specific manner and the inverted SA8 gene has a unique tissue distribution. While the functional activity of the SA8 putative toxin encoded by the inverted gene was inconclusive, its tissue localisation is similar to toxins used for predator deterrence. We demonstrate that, although mature SA8 putative toxins have similar cysteine spacing to ShK, SA8 peptides are distinct from ShK peptides based on structure and disulfide connectivity. Conclusions Our results provide the first demonstration that SA8 is a unique gene family in Actiniarians, evolving through a variety of structural changes including tandem and proximal gene duplication and an inversion event that together allowed SA8 to be recruited into the venom of T. stephensoni.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk
Megjelenés:	BMC Biology. - 21 : 1 (2023), p. 1-25. -
További szerzők:	Elnahriry, Khaled A. Stewart, Zachary K. Shafee, Thomas Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Szántó Gábor Tibor (1980-) (vegyész) van der Burg, Chloé A. Smith, Hayden L. Surm, Joachim M. Undheim, Eivind A. B. Madio, Bruno Hamilton, Brett R. Guo, Shaodong Wai, Dorothy C. C. Coyne, Victoria L. Phillips, Matthew J. Dudley, Kevin J. Hurwood, David A. Panyi György (1966-) (biofizikus) King, Glenn F. Pavasovic, Ana Norton, Raymond S. Prentis, Peter
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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001-es BibID:	BIBFORM114859
035-os BibID:	(cikkazonosító)140952 (scopus)85170288156
Első szerző:	Elnahriry, Khaled A.
Cím:	Structural and functional characterisation of Tst2, a novel TRPV1 inhibitory peptide from the Australian sea anemone Telmatactis stephensoni / Elnahriry Khaled A., Wai Dorothy C. C., Ashwood Lauren M., Naseem Muhammad Umair, Szanto Tibor G., Guo Shaodong, Panyi Gyorgy, Prentis Peter J., Norton Raymond S.
Dátum:	2024
ISSN:	1570-9639
Megjegyzések:	Sea anemone venoms are complex mixtures of biologically active compounds, including disulfide-rich peptides, some of which have found applications as research tools, and others as therapeutic leads. Our recent transcriptomic and proteomic studies of the Australian sea anemone Telmatactis stephensoni identified a transcript for a peptide designated Tst2. Tst2 is a 38-residue peptide showing sequence similarity to peptide toxins known to interact with a range of ion channels (NaV, TRPV1, KV and CaV). Recombinant Tst2 (rTst2, which contains an additional Gly at the N-terminus) was produced by periplasmic expression in Escherichia coli, enabling the production of both unlabelled and uniformly 13C,15N?labelled peptide for functional assays and structural studies. The LC-MS profile of the recombinant Tst2 showed a pure peak with molecular mass 6 Da less than that of the reduced form of the peptide, indicating the successful formation of three disulfide bonds from its six cysteine residues. The solution structure of rTst2 was determined using multidimensional NMR spectroscopy and revealed that rTst2 adopts an inhibitor cystine knot (ICK) structure. rTst2 was screened using various functional assays, including patch?clamp electrophysiological and cytotoxicity assays. rTst2 was inactive against voltagegated sodium channels (NaV) and the human voltage-gated proton (hHv1) channel. rTst2 also did not possess cytotoxic activity when assessed against Drosophila melanogaster flies. However, the recombinant peptide at 100 nM showed >50% inhibition of the transient receptor potential subfamily V member 1 (TRPV1) and slight (~10%) inhibition of transient receptor potential subfamily A member 1 (TRPA1). Tst2 is thus a novel ICK inhibitor of the TRPV1 channel.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Sea anemone Disulfide-rich peptides Recombinant expression NMR spectroscopy ICK scaffold TRPV1 channel
Megjelenés:	Biochimica et Biophysica Acta (BBA). Proteins and Proteomics. - 1872 : 1 (2024), p. 1-13. -
További szerzők:	Wai, Dorothy C. C. Ashwood, Lauren M. Naseem, Muhammad Umair (1993-) (biofizikus, molekuláris biológus) Szántó Gábor Tibor (1980-) (vegyész) Guo, Shaodong Panyi György (1966-) (biofizikus) Prentis, Peter Norton, Raymond S.
Pályázati támogatás:	K143071 OTKA Stipendium Hungaricum Scholarship from the Tempus Public Foundation Egyéb
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