Developing meningococcal vaccines through the gonococcal homologue of factor H binding protein
Professor Christoph Tang, University of Oxford
Professor Tang and his team will use the gonococcal homologue of factor H binding protein to make new vaccines to protect against meningococcal meningitis.
There is a recognised need to develop universal vaccines against the meningitis causing bacteria Neisseria meningitidis. Professor Tang and his team have identified an alternative approach to vaccine design that could lead to new meningococcal vaccines.
An important component of the vaccines currently under development to protect against Meningitis B is factor H binding protein (fHbp). fHbp helps the meningitis bacteria to survive by blocking factor H (a substance produced by the human immune system to kill bacteria) and is produced by the Meningitis B bacteria in one of three forms, complicating the design of new vaccines.
Professor Tang and his team have identified an alternative fHbp in Neisseria gonorrhoeae, named gonococcal homologue fHbp (ghfp). The main aim of this project is to use ghfp to make new vaccines to protect against meningococcal meningitis.
The use of ghfp in vaccine design could lead to more effective vaccines to protect against meningococcal meningitis (including Meningitis B).
Update due September 2012
Outcomes will be shown here once the project is complete.
Developing meningococcal vaccines through the gonococcal homologue of factor H binding protein
Professor Christoph Tang, University of Oxford
Professor Tang and his team will use the gonococcal homologue of factor H binding protein to make new vaccines to protect against meningococcal meningitis.
There is a recognised need to develop universal vaccines against Neisseria meningitidis. Professor Tang and his team have identified an alternative approach to vaccine design that could lead to new meningococcal vaccines.
Factor H binding protein (fHbp) is an important component of vaccines currently under development. Neisseria meningitidis (Nm) isolates express one of three variants of fHbp (v1, 2 or 3), defined by their predicted amino acid sequence. However, immunisation with fHbp is largely ‘variant specific’; v1 fHbp does not elicit bactericidal antibodies against Nm strains expressing either of the other variants, or vice versa. There is also evidence that high affinity binding of fH to fHbp may impair its efficacy and safety, and there are insufficient data to enable the construction of non-functional v2 and v3 fHbps.
Professor Tang and his team have identified a fHbp homologue in N. gonorrhoeae, named gonococcal homologue fHbp (ghfp); ghfp is most closely related to v3, then v2 and finally v1 fHbp (with approximately 86%, 83% and 62% amino acid identity, respectively). The overall goal of the project is to exploit ghfp as vaccine candidate and to use it to inform the design of new fHbp related vaccines. These will be evaluated in a novel, relevant model that can be used to test vaccines designed for use in humans.
Update due September 2012
Outcomes will be shown here once the project is complete.
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