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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.

|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.

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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.