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Transient opening of trimeric prefusion RSV F proteins
Morgan S A Gilman1,2, Polina Furmanova-Hollenstein3, Gabriel Pascual4
1Department of Biochemistry and Cell Biology, Geisel School of Medicine at Dartmouth, Hanover, NH, 03755, USA.
Nature Communications
|May 10, 2019
Summary
Respiratory syncytial virus (RSV) F protein trimers can transiently open, a motion enhanced by the CR9501 antibody. This finding impacts RSV vaccine development and antibody therapies.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- The respiratory syncytial virus (RSV) F glycoprotein is crucial for viral entry and a key target for neutralizing antibodies.
- While prefusion RSV F structures show compact trimers, their dynamic behavior, specifically transient opening, remains largely unexplored.
Purpose of the Study:
- To investigate the dynamic conformational changes of the RSV F glycoprotein.
- To understand the role of antibodies, such as CR9501, in modulating RSV F protein dynamics.
- To explore the implications of these dynamics for viral entry and antibody-based interventions.
Main Methods:
- Structural analysis, including a 3.3 Å crystal structure of monomeric RSV F bound to CR9501.
- Biochemical studies to assess the impact of CR9501 on RSV F trimer stability and dynamics.
- Comparative analysis of over 25 existing RSV F structures to identify conformational flexibility.
Main Results:
- The antibody CR9501 was shown to enhance the opening of prefusion-stabilized RSV F trimers.
- Structural data revealed a "breathing motion" in the prefusion conformation of RSV F.
- Full-length RSV F trimers were observed to transiently open and dissociate on the cell surface.
Conclusions:
- The prefusion RSV F glycoprotein exhibits dynamic conformational flexibility, including transient opening.
- Antibody CR9501 can modulate RSV F dynamics, potentially influencing viral entry.
- These findings offer insights into the functional mechanisms of class I fusion proteins and inform RSV vaccine and antibody prophylaxis strategies.
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