2. Academic Validation
  3. Carnitine palmitoyl-transferase 1A is potentially involved in bovine herpesvirus 1 productive infection

Carnitine palmitoyl-transferase 1A is potentially involved in bovine herpesvirus 1 productive infection

  • Vet Microbiol. 2023 Nov 30:288:109932. doi: 10.1016/j.vetmic.2023.109932.
Hao Yang 1,  Wenyuan Gu 2,  Junqing Ni 3,  Yabin Ma 3,  Shitao Li 4,  Donna Neumann 5,  Xiuyan Ding 1,  Liqian Zhu 6
Affiliations

Affiliations

  • 1 College of Life Sciences, Hebei University, Baoding 071002, China.
  • 2 Center for Animal Diseases Control and Prevention of Hebei Province, Shijiazhuang 050035, China.
  • 3 Hebei Province Animal Husbandry and Improved Breeds Work Station, Shijiazhuang 050061, China.
  • 4 Department of Microbiology and Immunology, Tulane University, New Orleans, LA 70118, USA.
  • 5 Department of Ophthalmology and Visual Sciences, University of Wisconsin-Madison, Madison, WI 537006, USA.
  • 6 College of Life Sciences, Hebei University, Baoding 071002, China. Electronic address: [email protected].
PMID: 38043447 DOI: 10.1016/j.vetmic.2023.109932
Abstract

Bovine herpesvirus 1(BoHV-1) is an important bovine pathogen that causes great economic loss to cattle farms worldwide. The virus-productive Infection in bovine kidney (MDBK) cells results in ATP depletion. The mechanisms are not well understood. Mitochondrial fatty acid β-oxidation (FAO) is an important energy source in many tissues with high energy demand. Since carnitine palmitoyl-transferase 1 A (CPT1A) is the rate-limiting Enzyme of FAO, we investigated the interactions between virus-productive Infection and CPT1A signaling. Here, we found that virus-productive Infection at the later stage significantly decreased CPT1A protein levels in all the detected cells, including MDBK, A549, and Neuro-2A cells, differentially altered the accumulation of CPT1A proteins in the nucleus and cytosol, and re-localized the protein in the nucleus. Etomoxir (ETO), an irreversible inhibitor of CPT1A, inhibited viral replication and partially interfered with the ability of BoHV-1 to alter CPT1A accumulation in the nucleus but not in the cytosol. Furthermore, ETO consistently reduced RNA levels of two viral regulatory proteins (bICP0 and bICP22) and protein expression of virion-associated proteins during productive Infection, further supporting the important roles of CPT1A signaling in BoHV-1 productive Infection. These data, for the first time, suggest that CPT1A is potentially involved in BoHV-1 productive Infection.

Keywords

BoHV-1; CPT1A; Etomoxir; β-oxidation.

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