Structure and inhibition of SARS-CoV-1 and SARS-CoV-2 main proteases by oral antiviral compound AG7404.

ABSTRACT: Severe acute respiratory syndrome coronaviruses 1 and 2 (SARS-CoV-1 and SARS-CoV-2) pose a threat to global public health. The 3C-like main protease (M^pro), which presents structural similarity with the active site domain of enterovirus 3C protease, is one of the best-characterized drug targets of these viruses. Here we studied the antiviral activity of the orally bioavailable enterovirus protease inhibitor AG7404 against SARS-CoV-1 and SARS-CoV-2 from a structural, biochemical, and cellular perspective, comparing it with the related molecule rupintrivir (AG7800). Crystallographic structures of AG7404 in complex with SARS-CoV-1 M^pro and SARS-CoV-2 M^pro and of rupintrivir in complex with SARS-CoV-2 M^pro were solved, revealing that all protein resi

SUBMITTER: Fabrega-Ferrer M 

PROVIDER: S-EPMC9632241 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature