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TitleRational Design of an Epstein-Barr Virus Vaccine Targeting the Receptor-Binding Site.
Journal, issue, pagesCell, Vol. 162, Issue 5, Page 1090-1100, Year 2015
Publish dateAug 27, 2015
AuthorsMasaru Kanekiyo / Wei Bu / M Gordon Joyce / Geng Meng / James R R Whittle / Ulrich Baxa / Takuya Yamamoto / Sandeep Narpala / John-Paul Todd / Srinivas S Rao / Adrian B McDermott / Richard A Koup / Michael G Rossmann / John R Mascola / Barney S Graham / Jeffrey I Cohen / Gary J Nabel /
PubMed AbstractEpstein-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 ...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.
External linksCell / PubMed:26279189 / PubMed Central
MethodsEM (single particle)
Resolution35.0 Å
Structure data

EMDB-3025:
Electron cryo-microscopy of EBV gp350-based ferritin nanoparticle
Method: EM (single particle) / Resolution: 35.0 Å

EMDB-6341:
Electron cryo-microscopy EBV gp350-based encapsulin nanoparticle
Method: EM (single particle) / Resolution: 35.0 Å

Source
  • Homo sapiens (human)

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