Key result
The crystal structure of ASFV core shell protein p15 revealed disulfide-linked trimers and identified Lys10 and Lys39 as essential for nucleic acid-binding affinity.
Why the study?
No commercial antiviral drug exists for ASFV, and the structural details of four of the five viral layers remain unclear.
The crystal structure of ASFV core shell protein p15 reveals disulfide-linked trimers and identifies Lys10 and Lys39 as essential for DNA binding, providing potential targets for antiviral drug development.
African swine fever (ASF) is an acute, hemorrhagic, and highly contagious disease caused by African swine fever virus (ASFV). The mortality rate of acute infection up to 100% have posed an unprecedented challenge of the swine industry. Currently no commercial antiviral drug is available for the control and treatment of ASFV. The structural resolution of ASFV virions reveals the details of ASFV morphogenesis, providing a new perspective for the research and promotion of the development of ASFV vaccines. Although the architecture of ASFV have been solved via cryo-EM, the structural details of four of the five viral layers remain unclear (except the outer capsid). In this study, we resolved the crystal structure of the ASFV core shell protein p15. The secondary structural elements of a protomer include four α-helix structures and six antiparallel β-strands. Further analysis revealed that ASFV p15 forms disulfide-linked trimers between the Cys9 from one protomer and Cys30 from other protomer. Additionally, the nucleic acid-binding property was characterized by electrophoretic mobility shift assay. Two critical amino acid Lys10 and Lys39 have been identified which is essential to the nucleic acid-binding affinity of ASFV p15. Together, these findings may provide new insight into antiviral drug development.
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Guo et al. (2021) studied African swine fever. Crystal structure resolution of ASFV core shell protein p15 was evaluated on Crystal structure and nucleic acid-binding property of ASFV p15. The crystal structure of ASFV core shell protein p15 revealed disulfide-linked trimers and identified Lys10 and Lys39 as essential for nucleic acid-binding affinity.
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