Consensus Integrase of a New HIV-1 Genetic Variant CRF63_02A1

Agapkina, Y.Y.; Pustovarova, M.A.; Korolev, S.P.; Zyryanova, D.P.; Ivlev, V.V.; Totmenin, A.V.; Gashnikova, N.M.; Gottikh, M.B.

Информация о цитировании статьи получена из Web of Science
Статья опубликована в журнале из перечня ВАК
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 сентября 2019 г.

Авторы: Agapkina Y.Y., Pustovarova M.A., Korolev S.P., Zyryanova D.P., Ivlev V.V., Totmenin A.V., Gashnikova N.M., Gottikh M.B.
Журнал: Acta Naturae (англоязычная версия)
Том: 11
Номер: 1(40)
Год издания: 2019
Издательство: Park Media Ltd
Местоположение издательства: Moscow, Russia (Federation)
Первая страница: 14
Последняя страница: 22
Аннотация: The high genetic variability of the human immunodeficiency virus (HIV-1) leads to a constant emergence of new genetic variants, including the recombinant virus CRF63_02A1, which is widespread in the Siberian Federal District of Russia. We studied HIV-1 CRF63_02A1 integrase (IN_CRF) catalyzing the incorporation of viral DNA into the genome of an infected cell. The consensus sequence was designed, recombinant integrase was obtained, and its DNA-binding and catalytic activities were characterized. The stability of the IN_CRF complex with the DNA substrate did not differ from the complex stability for subtype A and B integrases; however, the rate of complex formation was significantly higher. The rates and efficiencies of 3’-processing and strand transfer reactions catalyzed by IN_CRF were found to be higher, too. Apparently, all these distinctive features of IN_CRF may result from specific amino acid substitutions in its N-terminal domain, which plays an important role in enzyme multimerization and binding to the DNA substrate. It was also found that the drug resistance mutations Q148K/G140S and G118R/E138K significantly reduce the catalytic activity of IN_CRF and its sensitivity to the strand transfer inhibitor raltegravir. Reduction in sensitivity to raltegravir was found to be much stronger in the case of double-mutation Q148K/G140S.https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6475865/
Добавил в систему: Агапкина Юлия Юрьевна

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Consensus Integrase of a New HIV-1 Genetic Variant CRF63_02A1статья

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