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Structural basis for complement receptor engagement and virus neutralization through Epstein-Barr virus gp350.

M Gordon Joyce¹, Wei Bu², Wei-Hung Chen³

¹Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892, USA; Henry M. Jackson Foundation for the Advancement of Military Medicine, Inc, Bethesda, MD 20817, USA; Emerging Infectious Diseases Branch, Walter Reed Army Institute of Research, Silver Spring, MD 20910, USA.

|February 5, 2025

Summary

This summary is machine-generated.

Epstein-Barr virus (EBV) uses glycoprotein 350 (gp350) to infect B cells by binding complement receptor 2 (CR2). This study reveals gp350

Keywords:

CR2 EBV Epstein-Barr virus Herpesvirus antibody therapeutics gp350 human complement receptor 2 mAb molecular mimicry sites of vulnerability

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Area of Science:

Structural biology
Virology
Immunology

Background:

Epstein-Barr virus (EBV) causes infectious mononucleosis and is linked to human cancers.
EBV infects B cells via its glycoprotein 350 (gp350) binding to complement receptor 2 (CR2).
Lack of atomic-level understanding of the virus-host interface hinders EBV vaccine and therapeutic development.

Purpose of the Study:

To determine the atomic-level structure of the EBV gp350-CR2 complex.
To investigate the structural basis of neutralizing antibody interactions with gp350.
To provide insights for developing EBV vaccines and therapeutics.

Main Methods:

X-ray crystallography was used to determine the structures of gp350 in complex with CR2 and neutralizing antibodies.
Structural analysis focused on identifying key residues and interaction interfaces.

Main Results:

The 1.7 Å structure of gp350 complexed with CR2 was determined.
gp350 utilizes specific arginine residues for CR2 binding, mimicking its interaction with complement C3d.
Structures of gp350 with three neutralizing antibodies revealed they target the CR2-binding site using similar arginine residues.

Conclusions:

The study elucidates the molecular mimicry between EBV gp350-CR2 interaction and the gp350-antibody interaction.
Findings offer a structural basis for understanding EBV entry and antibody neutralization.
The identified structural features provide critical insights for designing effective EBV vaccines and antiviral therapies.