Abstract
Enveloped viruses require viral fusion proteins to promote fusion of the viral envelope with a target cell membrane. To drive fusion, these proteins undergo large conformational changes that must occur at the right place and at the right time. Understanding the elements which control the stability of the prefusion state and the initiation of conformational changes is key to understanding the function of these important proteins. The construction of mutations in the fusion protein transmembrane domains (TMDs) or the replacement of these domains with lipid anchors has implicated the TMD in the fusion process. However, the structural and molecular details of the role of the TMD in these fusion events remain unclear. Previously, we demonstrated that isolated paramyxovirus fusion protein TMDs associate in a monomer-trimer equilibrium, using sedimentation equilibrium analytical ultracentrifugation. Using a similar approach, the work presented here indicates that trimeric interactions also occur between the fusion protein TMDs of Ebola virus, influenza virus, severe acute respiratory syndrome coronavirus (SARS CoV), and rabies virus. Our results suggest that TM-TM interactions are important in the fusion protein function of diverse viral families.
Document Type
Article
Publication Date
4-18-2018
Digital Object Identifier (DOI)
https://doi.org/10.1128/mSphere.00047-18
Related Content
Supplemental material for this article may be found at https://doi.org/10.1128/mSphere.00047-18.
Repository Citation
Webb, Stacy R.; Smith, Stacy E.; Fried, Michael G.; and Dutch, Rebecca Ellis, "Transmembrane Domains of Highly Pathogenic Viral Fusion Proteins Exhibit Trimeric Association In Vitro" (2018). Molecular and Cellular Biochemistry Faculty Publications. 138.
https://uknowledge.uky.edu/biochem_facpub/138
FIG S1
inline-supplementary-material-2.tif (928 kB)
FIG S2
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Amino Acids, Peptides, and Proteins Commons, Biochemistry, Biophysics, and Structural Biology Commons, Microbiology Commons, Viruses Commons
Notes/Citation Information
Published in mSphere, v. 3, issue 2, e00047-18, p. 1-6.
Copyright © 2018 Webb et al.
This is an open-access article distributed under the terms of the Creative Commons Attribution 4.0 International license.