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Updated: Sep 29, 2026
Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
Published on: July 27, 2021
Sorting of the respiratory syncytial virus matrix protein into detergent-resistant structures is dependent on
Gary Henderson1, Jillian Murray, Robert P Yeo
1MRC Virology Unit, Institute of Virology, Church Street, Glasgow, G11 5JR, Scotland, United Kingdom.
Abstract:
The interaction of the respiratory syncytial virus (RSV) Matrix (M) protein with the plasma membrane was investigated using polyclonal and monoclonal antisera raised against recombinant M expressed in bacteria. M bound mainly to the plasma membrane, although a significant proportion bound to internal membranes. However, no localisation of M with the Golgi was observed, suggesting that transport of M to the plasma membrane was independent of the transport mechanism for the viral glycoproteins. Expression from a recombinant baculovirus demonstrated the ability of M to bind membranes in the absence of viral glycoprotein expression. When cell-surface expression of the viral glycoproteins was prevented using Brefeldin A, M was still found in association with the plasma membrane, but the characteristics of M's membrane-binding ability were different to that found in untreated infected cells. In the presence of normal glycoprotein expression, M was sorted into lipid rafts and, in addition, formed structures that could only be disrupted by treatment with high salt buffers, a feature suggesting an interaction with the cytoskeleton or the formation of strong intramolecular associations. Brefeldin A prevented M from being sorted into lipid rafts or from forming strong intramolecular associations. Brefeldin A also affected the stability of M bound to the plasma membrane, as M was more readily dissociated in the presence of the inhibitor. Coexpression of M and F resulted in the incorporation of M into lipid rafts but did not cause the formation of the strong intramolecular bonds, suggesting that additional factors are required for this phenomena.
Insights
Respiratory syncytial virus (RSV) Matrix (M) protein primarily binds to the plasma membrane, independent of viral glycoproteins. Its membrane association is influenced by Brefeldin A, affecting lipid raft sorting and stability.
Area of Science:
- Virology
- Cell Biology
- Protein Interactions
Background:
- The respiratory syncytial virus (RSV) Matrix (M) protein plays a crucial role in viral assembly and budding.
- Understanding the M protein's interaction with host cell membranes is vital for comprehending RSV replication.
Purpose of the Study:
- To investigate the localization and membrane-binding properties of the RSV M protein.
- To determine the M protein's interaction with the plasma membrane and internal cellular compartments.
- To elucidate the role of viral glycoproteins and Brefeldin A in M protein membrane association.
Main Methods:
- Utilized polyclonal and monoclonal antisera against recombinant M protein.
- Employed recombinant baculovirus expression systems.
- Investigated M protein localization in the presence and absence of viral glycoproteins and Brefeldin A.
- Analyzed M protein association with lipid rafts and potential cytoskeleton interactions.
Main Results:
- RSV M protein predominantly binds to the plasma membrane, with some association with internal membranes.
- M protein membrane binding is independent of viral glycoprotein expression.
- Brefeldin A treatment alters M protein's membrane-binding characteristics, preventing lipid raft sorting and strong intramolecular associations.
- M protein sorts into lipid rafts and forms strong associations (potentially with cytoskeleton) in untreated cells, but not when glycoprotein expression is inhibited.
Conclusions:
- RSV M protein's transport to the plasma membrane is independent of the viral glycoprotein pathway.
- M protein's interaction with the plasma membrane is complex, involving lipid raft sorting and potentially cytoskeleton association, which are modulated by viral glycoproteins and Brefeldin A.
- The formation of strong M protein intramolecular bonds requires additional factors beyond M and F protein co-expression.
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