Rational Design of an Epstein-Barr Virus Vaccine Targeting the Receptor-Binding Site

Cell. 2015 Aug 27;162(5):1090-100. doi: 10.1016/j.cell.2015.07.043. Epub 2015 Aug 13.

Abstract

Epstein-Barr virus (EBV) represents a major global health problem. Though it is associated with infectious mononucleosis and ∼200,000 cancers annually worldwide, a vaccine is not available. The major target of immunity is EBV glycoprotein 350/220 (gp350) that mediates attachment to B cells through complement receptor 2 (CR2/CD21). Here, we created self-assembling nanoparticles that displayed different domains of gp350 in a symmetric array. By focusing presentation of the CR2-binding domain on nanoparticles, potent neutralizing antibodies were elicited in mice and non-human primates. The structurally designed nanoparticle vaccine increased neutralization 10- to 100-fold compared to soluble gp350 by targeting a functionally conserved site of vulnerability, improving vaccine-induced protection in a mouse model. This rational approach to EBV vaccine design elicited potent neutralizing antibody responses by arrayed presentation of a conserved viral entry domain, a strategy that can be applied to other viruses.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, N.I.H., Intramural

MeSH terms

  • Animals
  • Antibodies, Neutralizing / immunology
  • Crystallography, X-Ray
  • Drug Design
  • Female
  • Herpesvirus 4, Human
  • Herpesvirus Vaccines / chemistry*
  • Herpesvirus Vaccines / genetics
  • Herpesvirus Vaccines / immunology*
  • Herpesvirus Vaccines / isolation & purification
  • Macaca fascicularis
  • Mice
  • Mice, Inbred BALB C
  • Nanoparticles / chemistry
  • Nanoparticles / ultrastructure
  • Receptors, Complement 3d / chemistry
  • Receptors, Complement 3d / immunology
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / genetics
  • Recombinant Proteins / immunology
  • Recombinant Proteins / isolation & purification

Substances

  • Antibodies, Neutralizing
  • Herpesvirus Vaccines
  • Receptors, Complement 3d
  • Recombinant Proteins