Bentley Graham A
Unité d'Immunologie Structurale, CNRS URA 2185, Département de Biologie Structurale et Chimie, Institut Pasteur, 25 rue du Dr. Roux, 75724 Paris Cedex 15, France.
Curr Opin Microbiol. 2006 Aug;9(4):395-400. doi: 10.1016/j.mib.2006.06.002. Epub 2006 Jun 21.
Malaria is a major global health problem and is caused by the unicellular parasite Plasmodium. Plasmodial surface proteins have important roles in host cell invasion and are responsible for antigenic diversity in this organism. Knowledge of the three-dimensional structure of surface proteins can facilitate our understanding their biological function, and contribute to the development of therapeutic and vaccine strategies against malaria. Structural studies allow rational drug design when ligand- or receptor-binding sites are identified and characterized. Analysis of the three-dimensional distribution of protective antibody epitopes and polymorphic residues can facilitate vaccine candidate optimization. With this in mind, some Plasmodium surface-protein structures have determined by X-ray crystallography or nuclear magnetic resonance.
疟疾是一个重大的全球健康问题，由单细胞寄生虫疟原虫引起。疟原虫表面蛋白在宿主细胞入侵中起重要作用，并导致该生物体的抗原多样性。了解表面蛋白的三维结构有助于我们理解其生物学功能，并有助于开发抗疟疾的治疗和疫苗策略。当确定并表征配体或受体结合位点时，结构研究有助于合理的药物设计。分析保护性抗体表位和多态性残基的三维分布有助于优化候选疫苗。考虑到这一点，一些疟原虫表面蛋白的结构已通过X射线晶体学或核磁共振确定。
