Structure-function insights into the dual role of African swine fever virus pB318L: A typical

Hai-Fan Zhao1, Ying Wang2, Xiao-Hong Liu3

  • 1School of Life Sciences, University of Science and Technology of China, Hefei 230027, China; Beijing Synchrotron Radiation Facility, Institute of High Energy Physics, Chinese Academy of Sciences, Beijing 100049, China.

Virologica Sinica
|April 4, 2025
PubMed

Insights

African swine fever virus protein pB318L functions as a geranylgeranyl-diphosphate synthase (GGPPS) crucial for viral replication. It also acts as a nuclear import protein, potentially aiding ASFV immune evasion.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • African swine fever virus (ASFV) protein pB318L is vital for viral replication.
  • pB318L functions as a membrane-bound trans-geranylgeranyl-diphosphate synthase (GGPPS).

Purpose of the Study:

  • To elucidate the enzymatic activity and structural characteristics of ASFV pB318L.
  • To investigate the role of pB318L in viral replication and potential immune evasion mechanisms.

Main Methods:

  • Structure-based mutagenesis and geranylgeranyl pyrophosphate (GGPP) production assays.
  • Phylogenetic analysis and subcellular localization studies.
  • Investigation of nuclear import pathways and protein-protein interactions.

Main Results:

  • Key residues for pB318L's GGPPS activity were identified.
  • pB318L shares structural and phylogenetic similarities with plant GGPPSs.
  • A unique N-terminal nuclear localization signal (NLS) in pB318L mediates nuclear import and interacts with KPNA1, potentially inhibiting STAT1 and ISGF3 translocation.

Conclusions:

  • ASFV pB318L is an essential GGPPS promoting viral replication.
  • pB318L functions as a nuclear import protein involved in ASFV immune evasion by interfering with host nuclear transport pathways.

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