Related Experiment Video
Updated: Aug 17, 2026

Generation, Amplification, and Titration of Recombinant Respiratory Syncytial Viruses
Published on: April 4, 2019
Interaction between the respiratory syncytial virus G glycoprotein cytoplasmic domain and the matrix protein
Reena Ghildyal1,2,3, Dongsheng Li4, Irene Peroulis1
1Macfarlane Burnet Institute for Medical Research and Public Health, Melbourne, Australia.
Abstract:
Paramyxovirus assembly at the cell membrane requires the movement of viral components to budding sites and envelopment of nucleocapsids by cellular membranes containing viral glycoproteins, facilitated by interactions with the matrix protein. The specific protein interactions during assembly of respiratory syncytial virus (RSV) are unknown. Here, the postulated interaction between the RSV matrix protein (M) and G glycoprotein (G) was investigated. Partial co-localization of M with G was demonstrated, but not with a truncated variant lacking the cytoplasmic domain and one-third of the transmembrane domain, in cells infected with recombinant RSV or transfected to express G and M. A series of G mutants was constructed with progressively truncated or modified cytoplasmic domains. Data from co-expression in cells and a cell-free binding assay showed that the N-terminal aa 2-6 of G play a key role in G-M interaction, with serine at position 2 and aspartate at position 6 playing key roles.
Insights
The matrix protein (M) of respiratory syncytial virus (RSV) interacts with the G glycoprotein (G) via its N-terminal residues 2-6. This interaction is crucial for viral assembly at the cell membrane.
Area of Science:
- Virology
- Molecular Biology
- Cell Biology
Background:
- Paramyxovirus assembly involves matrix protein interactions with viral glycoproteins at the cell membrane.
- Specific protein interactions during respiratory syncytial virus (RSV) assembly are not fully understood.
Purpose of the Study:
- To investigate the interaction between the RSV matrix protein (M) and the G glycoprotein (G).
- To identify the specific regions of G glycoprotein involved in M protein interaction.
Main Methods:
- Co-localization studies in RSV-infected and transfected cells.
- Expression of wild-type and mutant G glycoproteins.
- Cell-free binding assays.
Main Results:
- Partial co-localization of M and G proteins was observed.
- Truncated G variants lacking the cytoplasmic domain showed reduced M interaction.
- The N-terminal amino acids 2-6 of G, specifically serine at position 2 and aspartate at position 6, are critical for M-G interaction.
Conclusions:
- The N-terminal region of RSV G glycoprotein is essential for its interaction with the M protein.
- This M-G interaction likely plays a significant role in the assembly of RSV virions at the host cell membrane.
More Related Videos
Related Concept Videos
Respiratory Syncytial Virus Disease
Coronavirus
Rab Proteins
Rab proteins switch between a cytosolic, GDP-bound inactive state and a membrane-anchored, GTP-bound active state. By themselves, Rabs show slow rates of GDP/GTP exchange and GTP hydrolysis. Thus, Rab proteins are considered...
Inhibitors Of Virion Release
Cytomegalovirus Disease
Inhibitors of Virion Maturation and Assembly

