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

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Structural basis for VLDLR recognition by eastern equine encephalitis virus.

Pan Yang¹, Wanyu Li¹, Xiaoyi Fan¹

¹Department of Microbiology, Blavatnik Institute, Harvard Medical School, Boston, MA, USA.

Nature Communications

|August 2, 2024

Summary

This summary is machine-generated.

Eastern equine encephalitis virus (EEEV) and Semliki Forest virus (SFV) use divergent binding modes to interact with the same cellular receptor, VLDLR. This finding reveals a low evolutionary barrier for viruses acquiring LDLR-related proteins as receptors.

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Bacterial Artificial Chromosomes: A Functional Genomics Tool for the Study of Positive-strand RNA Viruses

Bacterial Artificial Chromosomes: A Functional Genomics Tool for the Study of Positive-strand RNA Viruses

Published on: December 29, 2015

Area of Science:

Virology
Structural Biology
Molecular Interactions

Background:

Eastern equine encephalitis virus (EEEV) is a highly virulent alphavirus causing severe neurological sequelae in human survivors.
Alphavirus entry into host cells is mediated by spike glycoproteins (E2 and E1) that bind cellular receptors and facilitate membrane fusion.
Very-low density lipoprotein receptor (VLDLR) and apolipoprotein E receptor 2 (ApoER2) were previously identified as cellular receptors for EEEV and Semliki Forest virus (SFV).

Purpose of the Study:

To elucidate the structural basis of EEEV and SFV binding to their shared cellular receptor, VLDLR.
To understand the molecular mechanisms underlying alphavirus-receptor interactions and their evolutionary implications.

Main Methods:

Single-particle cryo-electron microscopy (cryo-EM) was employed to determine the structures of EEEV and SFV spike glycoproteins complexed with the VLDLR ligand-binding domain.
Comparative structural analysis of the virus-receptor complexes.

Main Results:

The cryo-EM structures revealed that EEEV and SFV bind to the VLDLR ligand-binding domain through distinct binding modes.
Despite divergent binding modes, both viruses utilize the same cellular receptor, VLDLR.

Conclusions:

The flexible binding modes and small interaction footprints of LDLR-related proteins with viral spike proteins facilitate their adoption as cellular receptors by diverse viruses.
This adaptability suggests a low evolutionary barrier for alphaviruses to utilize LDLR family members, contributing to their broad host range and emergence potential.