論文 - 詳細
| RRC ID | 86893 |
|---|---|
| 著者 | Isaji T, Qi F, Chien YC, Oyama Y, Fukuda T, Khoo KH, Gu J. |
| タイトル | ST3GAL3-mediated selective α2,3-sialylation of LDLR promotes vesicular stomatitis virus entry. |
| ジャーナル | Biochim Biophys Acta Gen Subj |
| Abstract |
BACKGROUND:Vesicular stomatitis virus (VSV) is a model rhabdovirus whose infectivity is determined primarily by its envelope glycoprotein (VSV-G). The low-density lipoprotein receptor (LDLR), a cell-surface glycoprotein, has been identified as the major receptor for VSV-G binding. However, the role of host sialylation in VSV-G-dependent entry remains poorly understood. METHODS:Viral association, uptake, and transduction were evaluated in HeLa cells lacking β-galactoside α2,3-sialyltransferase 3 (ST3GAL3), 4 (ST3GAL4), or 6 (ST3GAL6) using flow cytometry, fluorescence microscopy, and Western blotting. LDLR sialylation was analyzed by lectin binding and LC-MS/MS glycoproteomics of recombinant soluble LDLR. RESULTS:ST3GAL3 knockout (KO) significantly reduced viral association, uptake, and transduction, and this effect was reversed by re-expression of ST3GAL3. Loss of ST3GAL3 decreased α2,3-linked sialylation of endogenous LDLR N-glycans, as indicated by Maackia amurensis lectin binding. Consistent with these findings, LC-MS/MS analysis revealed site-specific decreases in sialylated glycoforms of recombinant LDLR. CONCLUSIONS:ST3GAL3-dependent sialylation of LDLR N-glycans is required for efficient viral entry and is not compensated by ST3GAL4 or ST3GAL6 in HeLa cells. GENERAL SIGNIFICANCE:These findings identify a specific glycosylation pathway essential for VSV-G-dependent infection and suggest ST3GAL3 as a potential target to modulate viral tropism, with implications for oncolytic VSV strategies. |
| ページ | 130921 |
| 公開日 | 2026-2-22 |
| DOI | 10.1016/j.bbagen.2026.130921 |
| PII | S0304-4165(26)00021-8 |
| PMID | 41734828 |
| IF | 3.422 |
| リソース情報 | |
| ヒト・動物細胞 | HeLa(RCB0007) 293T(RCB2202) |