6LNL

ASFV core shell protein p15

Summary for 6LNL

• Entry DOI: 10.2210/pdb6lnl/pdb
• Descriptor: 60 kDa polyprotein (2 entities in total)
• Functional Keywords: viral protein
• Biological source: African swine fever virus (ASFV)
• Total number of polymer chains: 3
• Total formula weight: 57876.79

Authors

Guo, F.,Shi, Y.,Peng, G. (deposition date: 2019-12-30, release date: 2020-12-30, Last modification date: 2024-11-13)

Primary citation

Guo, F.,Shi, Y.,Yang, M.,Guo, Y.,Shen, Z.,Li, M.,Chen, Y.,Liang, R.,Yang, Y.,Chen, H.,Peng, G.
The structural basis of African swine fever virus core shell protein p15 binding to DNA.
Faseb J., 35:e21350-e21350, 2021

PubMed Abstract: 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.

PubMed: 33629764
DOI: 10.1096/fj.202002145R

Experimental method

X-RAY DIFFRACTION (1.9286 Å)