Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK.
Trends Microbiol. 2023 Aug;31(8):805-815. doi: 10.1016/j.tim.2023.02.011. Epub 2023 Mar 20.
Neisseria meningitidis is a human-adapted pathogen that causes meningitis and sepsis worldwide. N. meningitidis factor H-binding protein (fHbp) provides a mechanism for immune evasion by binding human complement factor H (CFH) to protect it from complement-mediated killing. Here, we discuss features of fHbp which enable it to engage human CFH (hCFH), and the regulation of fHbp expression. Studies of host susceptibility and bacterial genome-wide association studies (GWAS) highlight the importance of the interaction between fHbp and CFH and other complement factors, such as CFHR3, on the development of invasive meningococcal disease (IMD). Understanding the basis of fHbp:CFH interactions has also informed the design of next-generation vaccines as fHbp is a protective antigen. Structure-informed refinement of fHbp vaccines will help to combat the threat posed by the meningococcus, and accelerate the elimination of IMD.
脑膜炎奈瑟菌是一种适应人类的病原体,可在全球范围内引起脑膜炎和败血症。脑膜炎奈瑟菌因子 H 结合蛋白(fHbp)通过与人补体因子 H(CFH)结合提供了一种免疫逃避机制,以保护其免受补体介导的杀伤。在这里,我们讨论了 fHbp 使其能够与人类 CFH(hCFH)结合的特征,以及 fHbp 表达的调节。宿主易感性研究和细菌全基因组关联研究(GWAS)强调了 fHbp 与 CFH 以及其他补体因子(如 CFHR3)之间相互作用在侵袭性脑膜炎球菌病(IMD)发展中的重要性。对 fHbp:CFH 相互作用的基础的了解也为下一代疫苗的设计提供了信息,因为 fHbp 是一种保护性抗原。基于结构的 fHbp 疫苗的改进将有助于应对脑膜炎球菌带来的威胁,并加速消除 IMD。