Technology ID
TAB-2847

Novel Epstein-Barr Virus Vaccines

E-Numbers
E-531-2013-2
E-531-2013-0
E-531-2013-1
Lead Inventor
Kanekiyo, Masaru (NIAID)
Co-Inventors
Bu, Wei (NIAID)
Nabel, Gary (NIAID)
Cohen, Jeffrey (NIAID)
Applications
Vaccines­­­
Therapeutic Areas
Oncology
Infectious Disease
Development Stages
Pre-Clinical (in vitro)
Development Status
  • Early-stage
  • In vitro data available
  • In vivo data available (animal)
Lead IC
NIAID
ICs
NIAID
Epstein-Barr Virus (EBV) is the causative agent of infectious mononucleosis and is associated with certain types of cancers, such as Hodgkin's lymphoma, Burkitt's lymphoma, gastric carcinoma, and nasopharyngeal carcinoma. There are currently no vaccines against EBV on the market and there is only supportive treatment available for EBV infection.

The subject technologies are novel vaccine candidates against EBV that employ fusion proteins consisting of immunogenic portions of the EBV envelope glycoproteins (i.e. gp350, gH/gL, etc.) that are found on the surface of the virus fused with a self-assembling protein such as ferritin. The fusion proteins multimerize and the resulting nanoparticles serve as the antigens in the vaccine. In mice, these vaccine candidates were able to elicit neutralizing antibodies that were significantly higher than vaccination with only soluble forms of the EBV envelope glycoproteins lacking the self-assembly domains. In some cases, the fusion protein vaccine candidates were able to elicit neutralizing antibodies while vaccination with the corresponding soluble versions elicited primarily non-neutralizing antibodies. These neutralizing antibody titers in immunized mice were substantially higher than those seen in humans naturally infected with EBV.
Commercial Applications
  • Vaccines against EBV
Competitive Advantages
  • The subject technologies are novel vaccine candidates against EBV that were able to elicit significantly higher levels of neutralizing antibodies than vaccines based solely on soluble forms of the EBV envelope glycoproteins lacking self-assembly domains.
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