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

Авторлар: 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
Мекемелер:
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
Шығарылым: Том 68, № 1 (2023)
Беттер: 46-50
Бөлім: STRUCTURE OF MACROMOLECULAR COMPOUNDS
URL: https://journals.rcsi.science/0023-4761/article/view/137361
DOI: https://doi.org/10.31857/S0023476122060273
EDN: https://elibrary.ru/DMUZXL
ID: 137361

Дәйексөз келтіру

Толық мәтін

Ашық рұқсат
Рұқсат жабық

Рұқсат берілді
Рұқсат жабық

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Аннотация

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.

Негізгі сөздер

STRUCTURE OF MACROMOLECULAR COMPOUNDS

Авторлар туралы

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

Әдебиет тізімі

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