Mattila, S., Merilahti, P., Wazir, S., Quirin, T., Maksimainen, M. M., Zhang, Y., Xhaard, H., Lehtiö, L., & Ahola, T. (2021). Macrodomain Binding Compound MRS 2578 Inhibits Alphavirus Replication. Antimicrobial Agents and Chemotherapy, 65(12), e01398-21, https://doi.org/10.1128/aac.01398-21
Macrodomain binding compound MRS 2578 inhibits alphavirus replication
|Author:||Mattila, Sari1; Merilahti, Pirjo1; Wazir, Sarah2;|
1Department of Microbiology, Faculty of Agriculture and Forestry, University of Helsinkigrid.7737.4, Helsinki, Finland
2Faculty of Biochemistry and Molecular Medicine, University of Oulu, Oulu, Finland
3Biocenter Oulu, University of Oulu, Oulu, Finland
4Drug Research Program, Division of Pharmaceutical Chemistry and Technology, Faculty of Pharmacy, University of Helsinkigrid.7737.4, Helsinki, Finland
|Online Access:||PDF Full Text (PDF, 1.7 MB)|
|Persistent link:|| http://urn.fi/urn:nbn:fi-fe2021122162296
American Society for Microbiology,
|Publish Date:|| 2022-05-17
Alphaviruses are positive-strand RNA viruses causing febrile disease. Macrodomain-containing proteins, involved in ADP-ribose-mediated signaling, are encoded by both host cells and several virus groups, including alphaviruses. In this study, compound MRS 2578 that targets the human ADP-ribose glycohydrolase MacroD1 inhibited Semliki Forest virus production as well as viral RNA replication and replicase protein expression. The inhibitor was similarly active in alphavirus trans-replication systems, indicating that it targets the viral RNA replication stage.
Antimicrobial agents and chemotherapy
|Type of Publication:||
A1 Journal article – refereed
|Field of Science:||
1182 Biochemistry, cell and molecular biology
This work was supported by the Academy of Finland (grants 307802 (TA), 287063 (LL) and 294085 (LL)), and the Sigrid Jusélius Foundation (LL). The funders had no role in study design, data collection and interpretation,or the decision to submit the work for publication.
© American Society for Microbiology.