Technology ID
TAB-4925
Stabilizing the Prefusion Conformation of the RSV F Glycoprotein without Foldon Domain Dependency
E-Numbers
E-112-2015-0
Lead Inventor
Chen, Man
Lead IC
NIAID
Co-Inventors
Graham, Barney
Joyce, Michael
Sastry, Mallika
Yang, Yongping
Kwong, Peter
Stewart-Jones, Guillaume
Paul, Thomas
Druz, Aliaksandr
ICs
NIAID
Applications
Vaccines
Therapeutic Areas
Respiratory
Infectious Disease
Development Stages
Discovery
Research Products
Research Equipment
Antibodies
The technology focuses on stabilizing the respiratory syncytial virus (RSV) fusion (F) glycoprotein in its prefusion conformation, crucial for developing effective RSV vaccines. By introducing specific mutations (S155C-S290C, S190F, V207L) and creating interprotomer disulfides, trimer stabilization is achieved without relying on a foldon domain. This innovative approach enhances the immunogenicity of the RSV F protein, potentially leading to more potent and focused immune responses against RSV. The technology's impact extends to reducing the risk of unwanted immune responses and improving the overall efficacy and safety of RSV vaccines.
Commercial Applications
The technology's potential applications extend beyond RSV vaccine development. It could be utilized in other viral vaccines where stabilizing glycoproteins in prefusion conformation is beneficial for eliciting potent immune responses. Additionally, the approach of stabilizing proteins without the need for foldon domains could have implications in protein engineering and biotechnology, enabling the design of more stable and functional proteins for various applications. The removal of non-essential sequences to focus the immune response could also be relevant in designing vaccines for other pathogens or in immunotherapy approaches. Overall, the technology's broad applicability highlights its potential impact across multiple fields beyond RSV vaccine development.
Competitive Advantages
The technology presents competitive advantages in RSV vaccine development by stabilizing the F glycoprotein in its prefusion conformation without requiring a foldon domain. This streamlined approach simplifies vaccine design and production, potentially reducing costs and increasing efficiency. By enhancing the immunogenicity of the RSV F protein, the vaccine may elicit a more potent immune response compared to existing candidates. Moreover, the removal of non-RSV F sequences reduces the risk of unwanted immune responses, enhancing the vaccine's safety and specificity. Overall, these advantages position the technology as a promising and competitive option in the RSV vaccine market.
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