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Peer-reviewedCC BY 4.0PLOS Pathogens

Palmitoylation of glycoproteins under low temperature enhances SVCV replication

  • Chen Li1
  • Yan Zhang2
  • Yujun Zhang3
  • Yan Gao4
  • Yuanan Lu5
  • Shengbo Cao6
  • Jing Ye
  • Xueqin Liu
6 affiliations
  1. 1National Key Laboratory of Agricultural Microbiology, College of Fisheries, Huazhong Agricultural University, Wuhan, Hubei, China
  2. 2Hubei Engineering Technology Research Center for Aquatic Animal Diseases Control and Prevention, Wuhan, Hubei, China
  3. 3Hubei Jiangxia Laboratory, Wuhan, China
  4. 4Ocean College, Hebei Agricultural University, Qinhuangdao, Hebei, China
  5. 5Department of Public Health Sciences, the University of Hawaii at Manoa, Honolulu, Hawaii, United States of America
  6. 6National Key Laboratory of Agricultural Microbiology, College of Veterinary Medicine, Huazhong Agricultural University, Wuhan, Hubei, China
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Abstract

The temperature of water is a crucial factor that affects rhabdovirus infections in fish. Numerous rhabdoviruses, known for their high infectivity at relative low water temperatures (below 20°C), have led to significant economic impacts on global aquaculture. However, the molecular mechanisms underlying their temperature-dependent infectivity and pathogenicity remain unclear. Here, we employed spring viremia of carp virus (SVCV), a rhabdovirus prevalent at low temperatures, as a model. We found that the low temperature markedly elevates levels of palmitic acid in zebrafish, which promotes the palmitoylation of the SVCV glycoprotein (G). This modification enhances stability and cell membrane localization of the G protein, thereby facilitating viral budding. Furthermore, we identified the acyltransferase ZDHHC15a, upregulated at low temperatures, as the mediator of this palmitoylation. A competitive peptide targeting the palmitoylation site of SVCV G exhibited potent antiviral activity. Notably, a similar mechanism was observed in other aquatic rhabdoviruses that are low-temperature susceptible. Overall, our findings elucidate the mechanism underlying the temperature sensitivity of fish rhabdoviruses and hold broader significance for understanding the temperature adaptive evolution of other aquatic viruses. Author summary: Environmental temperature critically influences pathogen–host interactions, but the underlying molecular adaptations remain unclear. Using SVCV-infected zebrafish, we show that low temperature activates fatty acid synthesis, driving palmitoylation of the viral G protein via the transferase ZDHHC15a. This modification stabilizes G, enhances membrane localization, and promotes budding—a mechanism conserved in low temperature-adapted rhabdoviruses. A rationally designed peptide blocking this palmitoylation causes G degradation and suppresses replication. Our findings reveal fatty-acid-mediated palmitoylation as a temperature-sensitive switch for viral infectivity, offering evolutionary and therapeutic insights.

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Cite

BibTeXRIS
BibTeX
@article{li2026palmitoylation,
  title = {{Palmitoylation of glycoproteins under low temperature enhances SVCV replication}},
  author = {Chen Li and Yan Zhang and Yujun Zhang and Yan Gao and Yuanan Lu and Shengbo Cao and Jing Ye and Xueqin Liu},
  journal = {PLOS Pathogens},
  year = {2026},
  month = sep,
  doi = {10.1371/journal.ppat.1014654},
  url = {https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014654},
  note = {CC BY 4.0},
}
RIS
TY  - JOUR
TI  - Palmitoylation of glycoproteins under low temperature enhances SVCV replication
AU  - Chen Li
AU  - Yan Zhang
AU  - Yujun Zhang
AU  - Yan Gao
AU  - Yuanan Lu
AU  - Shengbo Cao
AU  - Jing Ye
AU  - Xueqin Liu
PY  - 2026
DA  - 2026/09/28
JO  - PLOS Pathogens
DO  - 10.1371/journal.ppat.1014654
UR  - https://journals.plos.org/plospathogens/article?id=10.1371/journal.ppat.1014654
AB  - The temperature of water is a crucial factor that affects rhabdovirus infections in fish. Numerous rhabdoviruses, known for their high infectivity at relative low water temperatures (below 20°C), have led to significant economic impacts on global aquaculture. However, the molecular mechanisms underlying their temperature-dependent infectivity and pathogenicity remain unclear. Here, we employed spring viremia of carp virus (SVCV), a rhabdovirus prevalent at low temperatures, as a model. We found that the low temperature markedly elevates levels of palmitic acid in zebrafish, which promotes the palmitoylation of the SVCV glycoprotein (G). This modification enhances stability and cell membrane localization of the G protein, thereby facilitating viral budding. Furthermore, we identified the acyltransferase ZDHHC15a, upregulated at low temperatures, as the mediator of this palmitoylation. A competitive peptide targeting the palmitoylation site of SVCV G exhibited potent antiviral activity. Notably, a similar mechanism was observed in other aquatic rhabdoviruses that are low-temperature susceptible. Overall, our findings elucidate the mechanism underlying the temperature sensitivity of fish rhabdoviruses and hold broader significance for understanding the temperature adaptive evolution of other aquatic viruses. Author summary: Environmental temperature critically influences pathogen–host interactions, but the underlying molecular adaptations remain unclear. Using SVCV-infected zebrafish, we show that low temperature activates fatty acid synthesis, driving palmitoylation of the viral G protein via the transferase ZDHHC15a. This modification stabilizes G, enhances membrane localization, and promotes budding—a mechanism conserved in low temperature-adapted rhabdoviruses. A rationally designed peptide blocking this palmitoylation causes G degradation and suppresses replication. Our findings reveal fatty-acid-mediated palmitoylation as a temperature-sensitive switch for viral infectivity, offering evolutionary and therapeutic insights.
SN  - 1553-7374
ER  -