Integrin αvβ1 Modulation Affects Subtype B Avian Metapneumovirus Fusion Protein-mediated Cell-Cell Fusion and Virus
Bing-Ling Yun1, Xiao-Lu Guan1, Yong-Zhen Liu1
1From the Division of Avian Infectious Diseases, State Key Laboratory of Veterinary Biotechnology, Harbin Veterinary Research Institute, Chinese Academy of Agricultural Sciences, No. 427 Maduan Street, Nan Gang District, Harbin 150001, Heilongjiang Province and.
Abstract:
Avian metapneumovirus (aMPV) fusion (F) protein mediates virus-cell membrane fusion to initiate viral infection, which requires F protein binding to its receptor(s) on the host cell surface. However, the receptor(s) for aMPV F protein is still not identified. All known subtype B aMPV (aMPV/B) F proteins contain a conserved Arg-Asp-Asp (RDD) motif, suggesting that the aMPV/B F protein may mediate membrane fusion via the binding of RDD to integrin. When blocked with integrin-specific peptides, aMPV/B F protein fusogenicity and viral replication were significantly reduced. Specifically we identified integrin αv and/or β1-mediated F protein fusogenicity and viral replication using antibody blocking, small interfering RNAs (siRNAs) knockdown, and overexpression. Additionally, overexpression of integrin αv and β1 in aMPV/B non-permissive cells conferred aMPV/B F protein binding and aMPV/B infection. When RDD was altered to RAE (Arg-Ala-Glu), aMPV/B F protein binding and fusogenic activity were profoundly impaired. These results suggest that integrin αvβ1 is a functional receptor for aMPV/B F protein-mediated membrane fusion and virus infection, which will provide new insights on the fusogenic mechanism and pathogenesis of aMPV.
Insights
Avian metapneumovirus subtype B uses integrin αvβ1 as a receptor for its fusion protein. This interaction is crucial for viral entry and replication, offering new insights into avian metapneumovirus pathogenesis.
Area of Science:
- Virology
- Cell Biology
- Molecular Medicine
Background:
- Avian metapneumovirus (aMPV) fusion (F) protein mediates viral entry by fusing with host cell membranes.
- The specific host cell receptors for aMPV F protein remain unidentified.
- Subtype B aMPV (aMPV/B) F proteins possess a conserved Arg-Asp-Asp (RDD) motif.
Purpose of the Study:
- To identify the host cell receptor(s) for the aMPV/B F protein.
- To elucidate the role of the RDD motif in aMPV/B F protein-mediated membrane fusion and viral infection.
Main Methods:
- Integrin-specific peptide blocking assays.
- Antibody blocking and small interfering RNA (siRNA) knockdown of integrins αv and β1.
- Overexpression of integrin αv and β1 in non-permissive cells.
- Site-directed mutagenesis of the RDD motif to RAE (Arg-Ala-Glu).
Main Results:
- Integrin-specific peptides significantly reduced aMPV/B F protein fusogenicity and viral replication.
- Integrin αv and/or β1 were identified as mediators of aMPV/B F protein fusogenicity and viral replication.
- Overexpression of integrin αv and β1 in non-permissive cells enabled aMPV/B F protein binding and infection.
- Alteration of the RDD motif to RAE profoundly impaired aMPV/B F protein binding and fusogenic activity.
Conclusions:
- Integrin αvβ1 functions as a key receptor for aMPV/B F protein-mediated membrane fusion and viral infection.
- The RDD motif is critical for integrin binding and subsequent viral entry.
- These findings provide novel insights into the fusogenic mechanisms and pathogenesis of aMPV.
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