Centre for Medical Parasitology, Department of International Health, Immunology and Microbiology, University of Copenhagen and Department of Infectious Diseases, Copenhagen University Hospital (Rigshospitalet), CSS, Øster Farimagsgade 5A, DK-1014 Copenhagen K, Denmark.
Trends Parasitol. 2010 May;26(5):230-5. doi: 10.1016/j.pt.2010.02.002. Epub 2010 Feb 26.
Pregnancy-associated malaria (PAM) is caused by Plasmodium falciparum-infected erythrocytes (IEs) accumulating in the placenta and has dire consequences for both mother and child. The multi-domain antigen VAR2CSA confers specific adhesion of IEs to chondroitin sulphate A (CSA) in the placenta, and is the leading PAM vaccine candidate. Recent data from different laboratories show that the binding properties of individual VAR2CSA domains do not reflect the native CSA-specific adhesion of IEs, which questions the relevance of the information obtained from single domain binding assays and co-crystallization experiments. Here, we discuss the implications of these findings for VAR2CSA vaccine development and highlight the need for studying the native structure of this protein.
妊娠相关疟疾（PAM）是由感染疟原虫的红细胞（IEs）在胎盘内积聚引起的，对母亲和儿童都有严重的后果。多结构域抗原 VAR2CSA 赋予 IEs 与胎盘上的硫酸软骨素 A（CSA）特异性结合的能力，是主要的 PAM 疫苗候选物。来自不同实验室的最新数据表明，单个 VAR2CSA 结构域的结合特性并不能反映 IEs 的天然 CSA 特异性黏附，这就质疑了从单个结构域结合测定和共结晶实验中获得的信息的相关性。在这里，我们讨论了这些发现对 VAR2CSA 疫苗开发的影响，并强调了研究该蛋白天然结构的必要性。
