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

Here, we found that fatty acid synthase (FASN) protein is potentially involved in virus infection both <i>in vitro</i> and <i>in vivo</i>. 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.

Authors

Institutions

Publication Details

Journal
Microbiology Spectrum
Published
2025-11-06
DOI
https://doi.org/10.1128/spectrum.01388-25
Citations
2
Primary Topic
Peroxisome Proliferator-Activated Receptors
Type
article
Field-Weighted Citation Impact
1.61
Controls
|||
ALL TIME
JAN
FEB
MAR
APR
MAY
JUN
JUL
AUG
SEP
OCT
article

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

Liqian Zhu, Xiaozhen Ma, Wenyuan Gu, Xuan Li et al.
2 citations
Microbiology Spectrum
Peroxisome Proliferator-Activated Receptors
1.61
article

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

Liqian Zhu, Xiaozhen Ma, Wenyuan Gu, Xuan Li, Xiuyan Ding
article en
2 citations

Abstract

Here, we found that fatty acid synthase (FASN) protein is potentially involved in virus infection both <i>in vitro</i> and <i>in vivo</i>. 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.

Microbiology SpectrumVol. 13(12)
Hebei Provincial Center for Disease Control and Prevention (CN), Hebei University (CN)
Openalex Percentile: Top 14%
Peroxisome Proliferator-Activated Receptors
1.61
AI Navigator

Ask Laika to Summarize, Analyze, and Connect papers live on the map.

Summarize Papers & Methodologies

Extract key findings, datasets, and comparative methods across publications.

Benchmark Rankings & Visual Analytics

Rank top research institutions, authors, funders, topics, and journals by Field-Weighted Citation Impact (FWCI) and paper volume with instant charts.

Connect Distant Disciplines

Bridge topological clusters on the map to find hidden collaborative intersections.

Fatty acid synthase may facilitate the trafficking of bovine alpha herpesvirus 1 out of the Golgi apparatus, potentially promoting viral infection — Liqian Zhu, Xiaozhen Ma, et al. · Microbiology Spectrum (2025) | TGRS Research Map | TGRS