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

PubMed ID: 38043447

Author(s): Yang H, Gu W, Ni J, Ma Y, Li S, Neumann D, Ding X, Zhu L. 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. Online ahead of print. PMID 38043447

Journal: Veterinary Microbiology, Volume 288, Nov 2023

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.