1. Assembly of respiratory syncytial virus matrix protein lattice and its coordination with fusion glycoprotein trimers.
- Author
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Sibert BS, Kim JY, Yang JE, Ke Z, Stobart CC, Moore ML, and Wright ER
- Subjects
- Humans, Protein Multimerization, Virion metabolism, Virion ultrastructure, Virion chemistry, Electron Microscope Tomography, Respiratory Syncytial Viruses chemistry, Models, Molecular, Respiratory Syncytial Virus Infections virology, Animals, Viral Fusion Proteins chemistry, Viral Fusion Proteins metabolism, Viral Matrix Proteins chemistry, Viral Matrix Proteins metabolism, Viral Matrix Proteins ultrastructure, Cryoelectron Microscopy, Respiratory Syncytial Virus, Human chemistry
- Abstract
Respiratory syncytial virus (RSV) is an enveloped, filamentous, negative-strand RNA virus that causes significant respiratory illness worldwide. RSV vaccines are available, however there is still significant need for research to support the development of vaccines and therapeutics against RSV and related Mononegavirales viruses. Individual virions vary in size, with an average diameter of ~130 nm and ranging from ~500 nm to over 10 µm in length. Though the general arrangement of structural proteins in virions is known, we use cryo-electron tomography and sub-tomogram averaging to determine the molecular organization of RSV structural proteins. We show that the peripheral membrane-associated RSV matrix (M) protein is arranged in a packed helical-like lattice of M-dimers. We report that RSV F glycoprotein is frequently observed as pairs of trimers oriented in an anti-parallel conformation to support potential interactions between trimers. Our sub-tomogram averages indicate the positioning of F-trimer pairs is correlated with the underlying M lattice. These results provide insight into RSV virion organization and may aid in the development of RSV vaccines and anti-viral targets., (© 2024. The Author(s).)
- Published
- 2024
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