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Specific Binding of the $\upalpha$-Component of the Lantibiotic Lichenicidin to the Peptidoglycan Precursor Lipid II Predetermines Its Antimicrobial Activityстатья
Статья опубликована в высокорейтинговом журнале
Информация о цитировании статьи получена из
Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 17 апреля 2024 г.
- Авторы: Panina Irina S., Balandin Sergey V., Tsarev Andrey V., Chugunov Anton O., Tagaev Andrey A., Finkina Ekaterina I., Antoshina Daria V., Sheremeteva Elvira V., Paramonov Alexander S., Rickmeyer Jasmin, Bierbaum Gabriele, Efremov Roman G., Shenkarev Zakhar O., Ovchinnikova Tatiana V.
- Журнал: International Journal of Molecular Sciences
- Том: 24
- Номер: 2
- Год издания: 2023
- Издательство: MDPI
- Местоположение издательства: Basel, Switzerland
- Номер статьи: 1332
- DOI: 10.3390/ijms24021332
- Аннотация: To date, a number of lantibiotics have been shown to use lipid II—a highly conserved peptidoglycan precursor in the cytoplasmic membrane of bacteria—as their molecular target. The α-component (Lchα) of the two-component lantibiotic lichenicidin, previously isolated from the Bacillus licheniformis VK21 strain, seems to contain two putative lipid II binding sites in its N-terminal and C-terminal domains. Using NMR spectroscopy in DPC micelles, we obtained convincing evidence that the C-terminal mersacidin-like site is involved in the interaction with lipid II. These data were confirmed by the MD simulations. The contact area of lipid II includes pyrophosphate and disaccharide residues along with the first isoprene units of bactoprenol. MD also showed the potential for the formation of a stable N-terminal nisin-like complex; however, the conditions necessary for its implementation in vitro remain unknown. Overall, our results clarify the picture of two component lantibiotics mechanism of antimicrobial action.
- Добавил в систему: Фурсова Полина Викторовна