1. Academic Validation
  2. Fatty acid synthase may facilitate the trafficking of bovine alpha herpesvirus 1 out of the Golgi apparatus, potentially promoting viral infection

Fatty acid synthase may facilitate the trafficking of bovine alpha herpesvirus 1 out of the Golgi apparatus, potentially promoting viral infection

  • Microbiol Spectr. 2025 Nov 6;13(12):e0138825. doi: 10.1128/spectrum.01388-25.
Xiaozhen Ma # 1 Wenyuan Gu # 2 Xuan Li 1 Xiuyan Ding 1 Liqian Zhu 1
Affiliations

Affiliations

  • 1 College of Life Sciences, Hebei University, Baoding, China.
  • 2 Center for Animal Diseases Control and Prevention of Hebei Province, Shijiazhuang, China.
  • # Contributed equally.
Abstract

The lipogenic enzyme fatty acid synthase (FASN) is essential for the de novo synthesis of fatty acids, and its aberrant expression has been implicated in the development of various diseases. However, the interaction between BoAHV-1 Infection and FASN remains to be fully elucidated. In this study, we observed that both viral acute Infection and latency in bovine trigeminal ganglia (TG) neurons, as well as virus productive Infection at later stages in Neuro-2A and MDBK cells, significantly reduced FASN protein levels. Notably, a subset of FASN protein co-localized with the viral glycoprotein gD, as revealed by confocal microscopy in these cell cultures. Knockdown of FASN protein expression using siRNAs or chemical inhibition of FASN by Cerulenin leads to reduced viral replication. Interestingly, a subset of FASN proteins localizes in the Golgi apparatus, and Cerulenin treatment retards the trafficking of virions out of the Golgi. Collectively, our findings reveal a novel mechanism by which FASN regulates viral replication: a portion of the FASN protein located in the Golgi apparatus facilitates viral trafficking out of the Golgi, which is essential for the completion of the viral replication cycle.

Importance: Here, we found that fatty acid synthase (FASN) protein is potentially involved in virus Infection both in vitro and in vivo. In terms of mechanism, a subset of FASN protein co-localizes with the viral glycoprotein gD, as revealed by confocal microscopy in both MDBK and Neuro-2A cell cultures. Interestingly, a subset of FASN protein localizes in the Golgi apparatus, and Cerulenin treatment retards the trafficking of virions out of the Golgi. Therefore, we propose that a portion of the FASN protein in the Golgi apparatus plays an important role in viral trafficking out of the Golgi, which is essential for the completion of the viral replication cycle. This represents a novel mechanism of virus Infection regulation, which has not been reported in Other viruses, although the FASN protein is involved in the regulation of multiple viruses through distinct mechanisms.

Keywords

BoAHV1; FASN; viral replication.

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