Preparation, Crystallization, and Preliminary X-ray Diffraction Analysis of Recombinant House Dust Mite Allergen Der p 3 from Dermatophagoides pteronyssinus

V. I. Timofeev; Тимофеев В. И.; Yu. A. Abramchik; Абрамчик Ю. А.; N. E. Zhukhlistova; Жухлистова Н. Е.; O. O. Mikheeva; Михеева О. О.; M. B. Shevtsov; Шевцов М. Б.; E. A. Zayats; Заяц Е. А.; D. D. Lykoshin; Лыкошин Д. Д.; M. A. Kostromina; Костромина М. А.; R. S. Esipov; Есипов Р. С.; I. P. Kuranova; Куранова И. П.

doi:10.31857/S0023476122060273

Preparation, Crystallization, and Preliminary X-ray Diffraction Analysis of Recombinant House Dust Mite Allergen Der p 3 from Dermatophagoides pteronyssinus

Autores: Timofeev V.I.¹^,2, Abramchik Y.A.¹^,3, Zhukhlistova N.E.¹, Mikheeva O.O.³, Shevtsov M.B.⁴, Zayats E.A.³, Lykoshin D.D.³, Kostromina M.A.³, Esipov R.S.³, Kuranova I.P.¹^,2
Afiliações:
1. Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia
2. National Research Centre “Kurchatov Institute,”, 123098, Moscow, Russia
3. Shemyakin−Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997, Moscow, Russia
4. Moscow Institute of Physics and Technology, 141701, Dolgoprudny, Moscow oblast, Russia
Edição: Volume 68, Nº 1 (2023)
Páginas: 46-50
Seção: STRUCTURE OF MACROMOLECULAR COMPOUNDS
URL: https://clinpractice.ru/0023-4761/article/view/673539
DOI: https://doi.org/10.31857/S0023476122060273
EDN: https://elibrary.ru/DMUZXL
ID: 673539

Citar

Texto integral

Acesso aberto
Acesso é fechado

Acesso está concedido
Acesso é fechado

Somente assinantes

Resumo
Sobre autores
Bibliografia
Arquivos suplementares
Estatísticas

Resumo

The high-producing strain С3029/pGro7/pERDerp3 for the house dust mite allergen Der p 3 from Dermatophagoides pteronyssinus, expressing the recombinant protein in Escherichia coli in the soluble form, was constructed. A procedure was developed for the purification of the recombinant allergen. Crystals of the recombinant protein Der p 3 suitable for X-ray diffraction analysis were grown by the vapor-diffusion method. The X-ray diffraction data set was collected to 2.25 Å resolution at the European Synchrotron Radiation Facility (ESRF, France, ID23-1 beamline) at 100 K. The crystals belong to sp. gr. С121 and contain two enzyme molecules per asymmetric unit.

Palavras-chave

STRUCTURE OF MACROMOLECULAR COMPOUNDS

Sobre autores

V. Timofeev

Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia; National Research Centre “Kurchatov Institute,”, 123098, Moscow, Russia

Email: inna@crys.ras.ru
Россия, Москва; Россия, Москва

Yu. Abramchik

Shubnikov Institute of Crystallography of Federal Scientific Research Centre “Crystallography and Photonics,” Russian Academy of Sciences, 119333, Moscow, Russia; Shemyakin−Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, 117997, Moscow, Russia

Email: inna@crys.ras.ru
Россия, Москва; Россия, Москва

Bibliografia

Murphy K., Weaver C. // Janeway’s Immunobiology. 2017. 9th Edition. Garland Science, Taylor & Francis Group. 927 p.
Bousquet P.-J., Chinn S., Janson C. et al. // European Community Respiratory Health Survey I. Allergy. 2007. V. 62. P. 301. https://doi.org/10.1111/j.1398-9995.2006.01293.x
Gaffin J.M., Phipatanakul W. // Curr. Opin. Allergy Clin. Immunol. 2009. V. 9. P. 128. https://doi.org/10.1097/aci.0b013e32832678b0
Gaffin J.M., Spergel J.M., Boguniewicz M. et al. // Allergy Asthma Proc. 2012. V. 33. P. 282. https://doi.org/10.2500/aap.2012.33.3572
Cox L., Nelson H., Lockey R. et al. // J. Allergy Clin. Immunol. 2011. V. 127 (1 Suppl.). P. S1–55.
Thomas W.R. // J. Allergy Clin. Immunol. 2011. V. 127. P. 855. https://doi.org/10.1016/j.jaci.2010.12.1084
Pauli G., Malling H.J. // Curr. Top Microbiol. Immunol. 2011. V. 352. P. 43. https://doi.org/10.1007/82_2011_125
Gregory L.G., Lloyd C.M. // Trends Immunol. 2011. V. 32. P. 402. https://doi.org/10.1016/j.it.2011.06.006
Hales B.J., Martin A.C., Pearce L.J. et al. // J. Allergy Clin. Immunol. 2006. V. 118. P. 361. https://doi.org/10.1016/j.jaci.2006.04.001
Weghofer M., Thomas W.R., Kronqvist M. et al. // Eur. J. Clin. Invest. 2008. V. 38. P. 959. https://doi.org/10.1111/j.1365-2362.2008.02048.x
King C., Brennan S., Thompson P.J., Stewart G.A. // J. Immunol. 1998. V. 161. P. 3645.
Sun G., Stacey M.A., Schmidt M. et al. // J. Immunol. 2001. V. 167. P. 1014. https://doi.org/10.4049/jimmunol.167.2.1014
Lin Y.-P., Nelson C., Kramer H., Parekh A.B. // Mol. Cell. 2018. V. 70 (2). P. 228. https://doi.org/10.1016/j.molcel.2018.03.025
Ivanciuc O., Schein C.H., Braun W. // Bioinformatics. 2002. V. 18. № 10. P. 1358. https://doi.org/10.1093/bioinformatics/18.10.1358
Battye T.G., Kontogiannis L., Johnson O. et al. // Acta Cryst. D. 2011. V. 67. P. 271. https://doi.org/10.1107/S0907444910048675
Smith W.A., Thomas W.R. // Clin. Exp. Allergy. 1996. V. 26. P. 571.
Bouaziz A., Walgraffe D., Bouillot C. et al. // Clin. Exp. Allergy. 2015. V. 45. P. 823. https://doi.org/10.1111/cea.12452