Key result
The high-resolution crystal structure of the ASFV pS273R protease was solved, and peptidomimetic aldehyde compounds targeting its substrate binding pocket exerted prominent inhibitory effects.
The resolution of the ASFV pS273R protease crystal structure and identification of inhibitory compounds provides a potential lead for anti-ASFV drug development.
May guide ASFV protease inhibitor design; leaves open in vivo efficacy and therapeutic translation.
African swine fever virus, a large and complex icosahedral DNA virus, causes a deadly infection in domestic pigs. In addition to Africa and Europe, countries in Asia, including China, Vietnam, and Mongolia, were negatively affected by the hazards posed by ASFV outbreaks in 2018 and 2019, at which time more than 30 million pigs were culled. Until now, there has been no vaccine for protection against ASFV infection or effective treatments to cure ASF. Here, we solved the high-resolution crystal structure of the ASFV pS273R protease. The pS273R protease has a two-domain structure that distinguishes it from other members of the SUMO protease family, while the unique "arm domain" has been proven to be essential for its hydrolytic activity. Moreover, the peptidomimetic aldehyde compounds designed to target the substrate binding pocket exert prominent inhibitory effects and can thus be used in a potential lead for anti-ASFV drug development.
No takes yet. Share an insight, caveat, or question.
Li et al. (2020) studied African swine fever virus (ASFV) infection. Peptidomimetic aldehyde compounds was evaluated on Inhibitory effects on ASFV pS273R protease. The high-resolution crystal structure of the ASFV pS273R protease was solved, and peptidomimetic aldehyde compounds targeting its substrate binding pocket exerted prominent inhibitory effects.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: