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Updated: Mar 14, 2026

Click-Chemistry Based Fluorometric Assay for Apolipoprotein N-acyltransferase from Enzyme Characterization to High-Throughput Screening
Published on: May 13, 2020
Mouse Apolipoprotein L9 is a phosphatidylethanolamine-binding protein
Thekkinghat Anantharaman Arvind1, Pundi N Rangarajan1
1Department of Biochemistry, Indian Institute of Science, Bangalore 560012, India.
Mouse Apolipoprotein L9 (ApoL9) binds phosphatidylethanolamine (PE) and is found in cellular structures. ApoL9 enhances Japanese encephalitis virus replication, suggesting a role in processes involving PE.
Area of Science:
- Cell Biology
- Virology
- Protein Biochemistry
Background:
- Mouse Apolipoprotein L9 (ApoL9) is an understudied cytoplasmic, interferon-inducible protein.
- Its intracellular localization and normal cellular functions remain unclear.
Purpose of the Study:
- To investigate the subcellular localization and cellular functions of ApoL9.
- To determine if ApoL9 interacts with phospholipids and influences viral replication.
Main Methods:
- Immunofluorescence microscopy to determine ApoL9 localization.
- In vitro binding assays using recombinant ApoL9 to assess phospholipid interactions.
- Viral replication assays using Japanese encephalitis virus (JEV) in ApoL9-expressing cells.
Main Results:
- ApoL9 localizes to cytoplasmic puncta and aggresome-like induced structures (ALIS) containing p62, Lc3, and ubiquitin.
- Recombinant and expressed ApoL9 specifically bind phosphatidylethanolamine (PE) in vitro.
- ApoL9 expression in B16F10 cells increased Japanese encephalitis virus (JEV) titres.
Conclusions:
- ApoL9 is a PE-binding protein localized to specific cellular structures.
- ApoL9 may play a role in cellular processes involving PE, including enhancing positive-strand RNA virus replication.
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