1. Academic Validation
  2. Phospholipase C-γ1 potentially facilitates subcellular localization of activated β-catenin, p-β-catenin(S552), during bovine herpesvirus 1 productive infection in MDBK cells

Phospholipase C-γ1 potentially facilitates subcellular localization of activated β-catenin, p-β-catenin(S552), during bovine herpesvirus 1 productive infection in MDBK cells

  • Vet Microbiol. 2022 Dec 6;276:109626. doi: 10.1016/j.vetmic.2022.109626.
Chang Liu 1 Xiuyan Ding 2 Long Chang 3 Weifeng Yuan 4 Shitao Li 5 Liqian Zhu 6
Affiliations

Affiliations

  • 1 Institute of Life Science and Green Development, College of Life Science, Hebei University, Baoding 071002, China.
  • 2 Institute of Life Science and Green Development, College of Life Science, Hebei University, Baoding 071002, China. Electronic address: [email protected].
  • 3 College of Veterinary Medicine, Yangzhou University, Yangzhou 225009, China.
  • 4 Institute of Animal Sciences, Chinese Academy of Agricultural Sciences, Beijing 100193, China.
  • 5 Department of Microbiology and Immunology, Tulane University, New Orleans, LA 70118, USA.
  • 6 Institute of Life Science and Green Development, College of Life Science, Hebei University, Baoding 071002, China; Key Laboratory of Microbial Diversity Research and Application of Hebei Province, College of Life Science, Hebei University, Baoding, China. Electronic address: [email protected].
Abstract

Bovine herpesvirus 1 (BoHV-1) is a significant risk factor for the bovine respiratory disease complex (BRDC), a severe disease causing great economic losses to the cattle industry worldwide. Previous studies have reported that both Phospholipase C-γ1 (PLC-γ1) and β-catenin are activated during BoHV-1 Infection for efficient replication. However, the interplay between PLC-γ1 and β-catenin as a consequence of virus Infection remains to be elucidated. Here, we reported that PLC-γ1 interacted with β-catenin, which was enhanced following virus Infection. PLC-γ1-specific inhibitor, U73122, significantly reduced the mRNA levels of β-catenin in BoHV-1-infected cells; however, the steady-state protein levels were not affected due to the virus Infection. Interestingly, the treatment of virus-infected cells with U73122 reduced the accumulation of activated β-catenin [p-β-catenin(S552)] in fractions of the cytoplasmic membrane as that observed with the treatment of methyl-β-cyclodextrin (MβCD), which can disrupt cytoplasmic membrane structure via sequestering Cholesterol. Nucleus accumulation of p-β-catenin(S552) was increased following U73122 treatment in virus-infected cells. In addition, the association of p-β-catenin(S552) with cytoplasmic membrane induced by the virus Infection was significantly disrupted by the treatment of U73122 and MβCD. These data indicated that the PLC-γ1 signaling is potentially involved in the regulation of β-catenin signaling stimulated by BoHV-1 Infection partially via affecting the subcellular localization of p-β-catenin(S552).

Keywords

Bovine herpesvirus 1; Phospholipase C-γ1; β-catenin.

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