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Structures of two lyssavirus glycoproteins trapped in pre- and post-fusion states and the implications on the
Fanli Yang1, Sheng Lin1, Xin Yuan1
1Department of Emergency Medicine, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, Chengdu, Sichuan, China.
Plos Pathogens
|February 19, 2025
Summary
Researchers mapped the structures of Ikoma and Mokola lyssavirus glycoproteins, revealing a sequential conformational change model. This finding aids in developing new vaccines and antiviral drugs against lyssaviruses.
Area of Science:
- Virology
- Structural Biology
- Immunology
Background:
- Lyssavirus glycoprotein is essential for viral entry and a key target for neutralizing antibodies.
- This glycoprotein undergoes significant low-pH-induced conformational changes during membrane fusion.
Purpose of the Study:
- To determine the structures of Ikoma lyssavirus and Mokola lyssavirus glycoproteins.
- To elucidate the conformational transitions of lyssavirus glycoproteins during membrane fusion.
- To develop a sequential conformation-transition model for lyssaviral glycoproteins.
Main Methods:
- X-ray crystallography to determine glycoprotein structures.
- Analysis of available lyssaviral glycoprotein structures.
- Surface plasmon resonance assay to study pH-regulated interactions.
Main Results:
- Structures of Ikoma and Mokola lyssavirus glycoproteins were determined, representing pre-fusion and post-fusion states.
- A sequential conformation-transition model was proposed, involving secondary structural changes from hairpin to linear conformations.
- pH-regulated interactions between specific domains facilitate conformational changes.
Conclusions:
- The elucidated structural features provide insights into lyssavirus glycoprotein function.
- Understanding these conformational dynamics can guide the design of novel vaccines and antiviral therapies against lyssaviruses.
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