Humbert María Victoria, Almonacid Mendoza Hannia L, Jackson Alexandra C, Hung Miao-Chiu, Bielecka Magdalena K, Heckels John E, Christodoulides Myron
a Neisseria Research, Molecular Microbiology, Academic Unit of Clinical and Experimental Sciences, Sir Henry Wellcome Laboratories , University of Southampton Faculty of Medicine , Southampton , UK.
Expert Rev Vaccines. 2015;14(12):1633-49. doi: 10.1586/14760584.2015.1095638. Epub 2015 Oct 15.
Peptidyl prolyl cis/trans isomerases (PPIases) are a superfamily of proteins ubiquitously distributed among living organisms, which function primarily to assist the folding and structuring of unfolded and partially folded polypeptide chains and proteins. In this review, we focus specifically on the Macrophage Infectivity Potentiator (MIP)-like PPIases, which are members of the immunophilin family of FK506-binding proteins (FKBP). MIP-like PPIases have accessory roles in virulence and are candidates for inclusion in vaccines protective against both animal and human bacterial pathogens. A structural vaccinology approach obviates any issues over molecular mimicry and potential cross-reactivity with human FKBP proteins and studies with a representative antigen, the Neisseria meningitidis-MIP, support this strategy. Moreover, a dual approach of vaccination and drug targeting could be considered for controlling bacterial infectious diseases of humans and animals.
肽基脯氨酰顺/反异构酶（PPIases）是一类广泛分布于生物体内的蛋白质超家族，其主要功能是协助未折叠和部分折叠的多肽链及蛋白质进行折叠和构建。在本综述中，我们特别关注巨噬细胞感染增强因子（MIP）样PPIases，它们是FK506结合蛋白（FKBP）免疫亲和素家族的成员。MIP样PPIases在毒力方面具有辅助作用，是包含在预防动物和人类细菌病原体的疫苗中的候选成分。结构疫苗学方法避免了与人类FKBP蛋白的分子模拟和潜在交叉反应的任何问题，对代表性抗原脑膜炎奈瑟菌-MIP的研究支持了这一策略。此外，可考虑采用疫苗接种和药物靶向的双重方法来控制人类和动物的细菌感染性疾病。
