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Analysis of Group IV Viral SSHHPS Using In Vitro and In Silico Methods

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Structural insights into VLDLR recognition by western equine encephalitis virus.

Shengjian Liang¹, Zhili Xu², Xiaoke Liu³

¹School of Basic Medical Sciences, Tsinghua University, Beijing, China. liangsj22@mails.tsinghua.edu.cn.

Nature Communications

|December 6, 2025

Summary

Western equine encephalitis virus (WEEV) has shifted its receptor usage from VLDLR. This study reveals specific VLDLR domains interacting with WEEV, offering insights into viral tropism and antiviral development.

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Area of Science:

Virology
Structural Biology
Molecular Biology

Background:

Western equine encephalitis virus (WEEV) causes severe neurological disease in humans and equids.
Historically, WEEV utilized the very-low-density lipoprotein receptor (VLDLR) for cell entry, but current strains have altered receptor tropism.

Purpose of the Study:

To elucidate the structural basis of WEEV interaction with VLDLR.
To identify specific VLDLR domains involved in WEEV binding.
To understand the molecular determinants of WEEV receptor usage shifts.

Main Methods:

Cryo-electron microscopy (cryo-EM) to determine complex structures of WEEV with VLDLR fragments.
Biochemical assays to assess binding affinities between WEEV and VLDLR concatemers.
Site-directed mutagenesis to investigate the role of E2 glycoprotein polymorphisms in WEEV entry.

Main Results:

Identified direct interactions between WEEV and specific VLDLR domains (LA1, LA2, LA3, LA5).
Cryo-EM revealed LA1 and LA2 binding within a cleft of the WEEV spike protein, while LA3 and LA5 interact with the E1 protein's DIII region.
The VLDLR LA1-5 concatemer showed the highest binding affinity for WEEV.
A single polymorphism in the WEEV E2 glycoprotein was found to determine receptor tropism, with specific mutations enhancing VLDLR-mediated entry.

Conclusions:

Detailed structural insights into WEEV-VLDLR interactions.
Understanding of how viral glycoproteins mediate receptor binding and entry.
Identification of key viral determinants for receptor tropism shifts.
Provides a foundation for developing targeted antiviral therapies against WEEV and related alphaviruses.