Key result
The crystal structure of ASFV dUTPase reveals a novel folding pattern where the active site is composed of two subunits instead of the classic three, providing a potential target for specific inhibitors.
Why the study?
African swine fever virus causes deadly infection in domestic pigs with recent widespread outbreaks, but there has been no vaccine for protection or effective treatment to cure it.
The crystal structure of ASFV dUTPase reveals a novel folding pattern that could be targeted for the design of specific inhibitors against African swine fever virus.
ASFV dUTPase structure may guide inhibitor design; leaves open whether it advances antiviral therapies.
African swine fever virus (AFSV), a large enveloped double-stranded DNA virus, causes a deadly infection in domestic pigs. In addition to Africa, Europe, and South America, countries in Asia, such as China, Vietnam, and Mongolia, have suffered the hazards posed by ASFV outbreaks in recent years. Until now, there has been no vaccine for protection from ASFV infection or effective treatments to cure ASF. Here, we solved the crystal structure of the ASFV dUTPase-dUMP-Mg 2+ complex. The ASFV dUTPase displays a noncanonical folding pattern that differs from that of the classic homotrimeric dUTPase, in which the active site is composed of two subunits. In addition, several nonconserved residues within the 3-fold axis channel play a vital role in ASFV dUTPase homotrimer stability. Our finding on these unique structural features of the ASFV dUTPase could be explored for the design of potential specific inhibitors that target this unique enzyme.
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Li et al. (2019) studied African swine fever virus (ASFV) infection. Structural analysis of ASFV dUTPase was evaluated on Crystal structure and folding pattern. The crystal structure of ASFV dUTPase reveals a novel folding pattern where the active site is composed of two subunits instead of the classic three, providing a potential target for specific inhibitors.
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