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A Method to Assess Fc-mediated Effector Functions Induced by Influenza Hemagglutinin Specific Antibodies
Published on: February 23, 2018
CD147 mediates the adsorption of influenza A virus on the cell surface through direct interaction with HA
Ting Wang1,2,3, Lei Cao1,2,3, Yufei Zhang1,2
1State Key Laboratory of Agricultural Microbiology, Huazhong Agricultural University, Wuhan, China.
Abstract:
The adsorption of avian influenza virus (AIV) initiates the viral lifecycle, determining host tropism and pathogenicity. In addition to the classical AIV receptor, auxiliary receptors also play important roles in viral adsorption, though these remains to be fully elucidated. In this study, we identified 25 avian membrane proteins that interact with H5N6 hemagglutinin (HA), one of which, CD147, was confirmed to play a crucial role in promoting AIV adsorption and replication through overexpression and knockout experiments in DF1 and A549 cells. As a highly glycosylated transmembrane protein, CD147 was further shown to directly bind to the HA receptor-binding domain via its extracellular immunoglobulin-like domains, independently of its glycosylation, thereby mediating viral adsorption. Moreover, AIV infection upregulated the hyperglycosylated form (HG-CD147), while glycosylation inhibitors reduced viral adsorption, highlighting the role of glycosylation in modulating CD147 function. Finally, disrupting the CD147-HA interaction with soluble proteins or monoclonal antibodies inhibited viral adsorption and replication. This study identifies CD147 as an adjuvant receptor that promotes influenza virus adsorption and provides a mechanistic foundation basis for developing broad-spectrum therapeutics targeting HA-host protein interactions.
Insights
CD147 is identified as a key auxiliary receptor that binds avian influenza virus (AIV) hemagglutinin (HA), promoting viral adsorption and replication. This finding offers a new target for developing broad-spectrum antiviral therapies.
Area of Science:
- Virology
- Cell Biology
- Immunology
Background:
- Avian influenza virus (AIV) adsorption is critical for its lifecycle, host tropism, and pathogenicity.
- While classical receptors are known, auxiliary receptors mediating AIV adsorption require further elucidation.
Purpose of the Study:
- To identify novel avian membrane proteins interacting with H5N6 hemagglutinin (HA).
- To investigate the role of identified proteins, particularly CD147, in AIV adsorption and replication.
- To elucidate the mechanism of CD147-mediated viral entry.
Main Methods:
- Screening of avian membrane proteins interacting with H5N6 HA.
- Overexpression and knockout experiments in DF1 and A549 cells to assess CD147 function.
- Binding assays to determine direct interaction between CD147 and HA.
- Analysis of CD147 glycosylation and its impact on viral adsorption.
- Inhibition assays using soluble proteins and monoclonal antibodies targeting the CD147-HA interaction.
Main Results:
- Identified 25 avian membrane proteins interacting with H5N6 HA, including CD147.
- Confirmed CD147's crucial role in promoting AIV adsorption and replication.
- Demonstrated direct binding of CD147's extracellular domains to the HA receptor-binding domain, independent of glycosylation.
- Showed that AIV infection upregulates hyperglycosylated CD147 (HG-CD147), and glycosylation inhibitors reduce viral adsorption.
- Inhibition of the CD147-HA interaction significantly reduced viral adsorption and replication.
Conclusions:
- CD147 acts as an essential adjuvant receptor for avian influenza virus (AIV) adsorption.
- The interaction between CD147 and HA is a key mechanism mediating viral entry.
- Targeting the CD147-HA interaction presents a promising strategy for developing broad-spectrum antiviral therapeutics against influenza viruses.
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