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XL-MS for novel HIV-1 integrase partners detectionстатья Тезисы
Статья опубликована в высокорейтинговом журнале
Статья опубликована в журнале из списка Web of Science и/или ScopusДата последнего поиска статьи во внешних источниках: 1 декабря 2021 г.
- Авторы: Anna Rozina, Anisenko Andrey, Galkin Simon, Gottikh Marina
- Журнал: Protein Science
- Том: 30
- Номер: S1
- Год издания: 2021
- Издательство: Cold Spring Harbor Laboratory Press
- Местоположение издательства: United States
- Первая страница: 59
- Последняя страница: 59
- Аннотация: RNA viruses, in pursuit of genome miniaturization, tend to employ cellular proteins to facilitate their replication. HIV-1, one of the most studied retrovirus, is not an exception. Search for HIV-1 cellular partners and their examination is a prevailing area of research. One of the probable applications is a development of anti-HIV drugs that hamper cell-virus protein-protein interactions. One of HIV-1 proteins, integrase, is a key virus enzyme since it catalyzes HIV integration. To carry out its functions,integrase, seemingly, employs a great number of cellular factors. Despite years of extensive research, there are pro- cesses where cellular cofactors employed have not been determined yet or where their interplay is not fully understood, including integrase degradation, its inter- actome during PIC nuclear import, its role in post- integrational repair machinery recruitment and many others. Expanding our understanding of the integrase interactome would potentially open up new opportunities for drug development. Our work aims at capturing tran- sient partners of HIV-1 integrase that would enhance our understanding of the molecular pathways involved in the integrase functioning. To do that, we employed XL-MS technique in HA-integrase plasmid transfected cells. We have conducted four repeats of the experiment and as a result have detected 18 potential previously undescribed partners, as well as several well-known partners. Among the former, we observed several proteins involved in HIV-1 replication but not known as the integrase part- ners. Also, we have found a previously undescribed in HIV-1 integrase context E3-ubiquitin ligase, a protein involved in tethering a specific complex to an actively transcribed region and several other interesting proteins. Their interaction with integrase has been tested in vivo. The work was supported by RSF grant 19-74-10021
- Добавил в систему: Галкин Семен Олегович
Прикрепленные файлы
| № | Имя | Описание | Имя файла | Размер | Добавлен |
|---|---|---|---|---|---|
| 1. | Полный текст | Protein_Science.pdf | 538,7 КБ | 25 ноября 2021 [scibro] |