A New Peptide from the Venom of the Madagascar Cat-Eyed Snake Madagascarophis colubrinus Blocks Nicotinic Acetylcholine Receptor
- Autores: Kryukova E.1, Ivanov D.2, Kopylova N.1, Starkov V.1, Andreeva T.1, Ivanov I.1, Tsetlin V.1, Utkin Y.1
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Afiliações:
- Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences
- FKOO “Labkorp”
- Edição: Volume 49, Nº 3 (2023)
- Páginas: 296-305
- Seção: Articles
- URL: https://journals.rcsi.science/0132-3423/article/view/139153
- DOI: https://doi.org/10.31857/S0132342323030156
- EDN: https://elibrary.ru/PDSQUE
- ID: 139153
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Resumo
In screening the venoms of various snake species, we found that the venom of the Madagascar cat-eyed snake Madagascarophis colubrinus competes with α-bungarotoxin for binding to the nicotinic acetylcholine receptor from Torpedo californica. Using liquid chromatography, a peptide, called macoluxin and inhibiting the binding of the toxin to the receptor, was isolated from the venom. The amino acid sequence of this 23-amino acid peptide was determined by automatic Edman degradation. Comparison with amino acid sequences of known proteins showed that the macoluxin sequence is homologous to the α-helical region of the sequence of snake venom metalloproteinases. The peptide was synthesized by solid-phase peptide synthesis, and the study of its biological activity showed that it inhibits the binding of α-bungarotoxin to the Torpedo receptor with an IC50 of 47 μM. Macoluxin also reversibly inhibited acetylcholine-induced currents in the muscle-type nicotinic acetylcholine receptor. This is the first data on the presence in the venom of rear fanged snakes of a peptide that can inhibit the nicotinic acetylcholine receptor.
Palavras-chave
Sobre autores
E. Kryukova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences
Email: utkin@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10
D. Ivanov
FKOO “Labkorp”
Email: utkin@ibch.ru
Russia, 107045, Moscow, ul. Trubnaya 12
N. Kopylova
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences
Email: utkin@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10
V. Starkov
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences
Email: utkin@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10
T. Andreeva
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences
Email: utkin@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10
I. Ivanov
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences
Email: utkin@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10
V. Tsetlin
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences
Email: utkin@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10
Yu. Utkin
Shemyakin–Ovchinnikov Institute of Bioorganic Chemistry Russian Academy of Sciences
Autor responsável pela correspondência
Email: utkin@ibch.ru
Russia, 117997, Moscow, ul. Miklukho-Maklaya 16/10
Bibliografia
- Madagascarophis colubrinus (Schlegel, 1837) // The Reptile Database, 2022. https://reptile-database.reptarium.cz/species?genus= Madagascarophis&species=colubrinus&search_param= %28%28genus%3D%27madagascarophis%27%29%29
- Domergue C.A. // Bull. Mus. Natn. Hist. Nat., Paris. 1987. V. 9. P. 455–489.
- Domergue C.A. // Bull. Acad. Malgache. 1962. V. 40. P. 97–98.
- Dashevsky D., Debono J., Rokyta D., Nouwens A., Josh P., Fry B.G. // J. Mol. Evol. 2018. V. 86. P. 531–545. https://doi.org/10.1007/s00239-018-9864-6
- Heyborne W.H., Mackessy S.P. // Biochimie. 2013. V. 95. P. 1923–1932. https://doi.org/10.1016/j.biochi.2013.06.025
- Calvete J.J., Bonilla F., Granados-Martínez S., Sanz L., Lomonte B., Sasa M. // J. Proteomics. 2020. V. 225. P. 103 882. https://doi.org/10.1016/j.jprot.2020.103882
- Xie B., Dashevsky D., Rokyta D., Ghezellou P., Fathinia B., Shi Q., Richardson M.K., Fry B.G. // BMC Biol. 2022. V. 20. P. 4. https://doi.org/10.1186/s12915-021-01208-9
- Koua D., Ebou A., Habbouche Z., Ballouard J.M., Caron S., Bonnet X., Dutertre S. // Toxicon X. 2022. V. 15. P. 100 130. https://doi.org/10.1016/j.toxcx.2022.100130
- Vulfius C.A., Kasheverov I.E., Starkov V.G., Osipov A.V., Andreeva T.V., Filkin S.Y., Gorbacheva E.V., Astashev M.E., Tsetlin V.I., Utkin Y.N. // PLoS One. 2014. V. 9. P. e115428. https://doi.org/10.1371/journal.pone.0115428
- Vulfius C.A., Kasheverov I.E., Kryukova E.V., Spirova E.N., Shelukhina I.V., Starkov V.G., Andreeva T.V., Faure G., Zouridakis M., Tsetlin V.I., Utkin Y.N. // PLoS One. 2017. V. 12. P. e0186206. https://doi.org/10.1371/journal.pone.0186206
- Utkin Y.N., Weise C., Kasheverov I.E., Andreeva T.V., Kryukova E.V., Zhmak M.N., Starkov V.G., Hoang N.A., Bertrand D., Ramerstorfer J., Sieghart W., Thompson A.J., Lummis S.C., Tsetlin V.I. // J. Biol. Chem. 2012. V. 287. P. 27079–27086. https://doi.org/10.1074/jbc.M112.363051
- Vulfius C.A., Spirova E.N., Serebryakova M.V., Shelukhina I.V., Kudryavtsev D.S., Kryukova E.V., Starkov V.G., Kopylova N.V., Zhmak M.N., Ivanov I.A., Kudryashova K.S., Andreeva T.V., Tsetlin V.I., Utkin Y.N. // Toxicon. 2016. V. 121. P. 70–76. https://doi.org/10.1016/j.toxicon.2016.08.020
- Kryukova E.V., Vulfius C.A., Ziganshin R.H., Andreeva T.V., Starkov V.G., Tsetlin V.I., Utkin Y.N. // J. Venom Res. 2020. V. 10. P. 23–29.
- Dutertre S., Nicke A., Tsetlin V.I. // Neuropharmacology. 2017. V. 127. P. 196–223. https://doi.org/10.1016/j.neuropharm.2017.06.011
- Kudryavtsev D.S., Shelukhina I.V., Son L.V., Ojomoko L.O., Kryukova E.V., Lyukmanova E.N., Zhmak M.N., Dolgikh D.A., Ivanov I.A., Kasheverov I.E., Starkov V.G., Ramerstorfer J., Sieghart W., Tsetlin V.I., Utkin Y.N. // J. Biol. Chem. 2015. V. 290. P. 22747–22758. https://doi.org/10.1074/jbc.M115.648824
- Shelukhina I., Spirova E., Kudryavtsev D., Ojomoko L., Werner M., Methfessel C., Hollmann M., Tsetlin V. // PLoS One. 2017. V. 12. P. e0181936. https://doi.org/10.1371/journal.pone.0181936
- Altschul S.F., Madden T.L., Schäffer A.A., Zhang J., Zhang Z., Miller W., Lipman D.J. // Nucleic Acids Res. 1997. V. 25. P. 3389–3402. https://doi.org/10.1093/nar/25.17.3389
- Guan H.H., Goh K.S., Davamani F., Wu P.L., Huang Y.W., Jeyakanthan J., Wu W.G., Chen C.J. // J. Struct. Biol. 2010. V. 169. P. 294–303. https://doi.org/10.1016/j.jsb.2009.11.009
- Brust A., Sunagar K., Undheim E.A., Vetter I., Yang D.C., Casewell N.R., Jackson T.N., Koludarov I., Alewood P.F., Hodgson W.C., Lewis R.J., King G.F., Antunes A., Hendrikx I., Fry B.G. // Mol. Cell. Proteomics. 2013. V. 12. P. 651–663. https://doi.org/10.1074/mcp.M112.023135
- Nicolau C.A., Carvalho P.C., Junqueira-de-Azevedo I.L., Teixeira-Ferreira A., Junqueira M., Perales J., Neves-Ferreira A.G., Valente R.H. // J. Proteomics. 2017. V. 151. P. 214–231. https://doi.org/10.1016/j.jprot.2016.06.029
- Jin A.H., Cristofori-Armstrong B., Rash L.D., Román-González S.A., Espinosa R.A., Lewis R.J., Alewood P.F., Vetter I. // Biochem. Pharmacol. 2019. V. 164. P. 342–348. https://doi.org/10.1016/j.bcp.2019.04.025
- Shelukhina I.V., Zhmak M.N., Lobanov A.V., Ivanov I.A., Garifulina A.I., Kravchenko I.N., Rasskazova E.A., Salmova M.A., Tukhovskaya E.A., Rykov V.A., Slashcheva G.A., Egorova N.S., Muzyka I.S., Tsetlin V.I., Utkin Y.N. // Toxins (Basel). 2018. V. 10. P. 34. https://doi.org/10.3390/toxins10010034
- Lebedev D.S., Kryukova E.V., Ivanov I.A., Egorova N.S., Timofeev N.D., Spirova E.N., Tufanova E.Y., Siniavin A.E., Kudryavtsev D.S., Kasheverov I.E., Zouridakis M., Katsarava R., Zavradashvili N., Iagorshvili I., Tzartos S.J., Tsetlin V.I. // Mol. Pharmacol. 2019. V. 96. P. 664–673. https://doi.org/10.1124/mol.119.117713
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