Fundación Instituto de Inmunología de Colombia (FIDIC), Bogotá, Colombia.
Vaccine. 2010 Mar 19;28(14):2653-63. doi: 10.1016/j.vaccine.2010.01.004. Epub 2010 Jan 17.
In this study, we synthesized the complete sequence of the CLAG-9 protein as 67 20-mer-long non-overlapped peptides and assessed their ability to bind to erythrocytes in receptor-ligand assays. Twenty CLAG-9 peptides were found to have specific high-affinity binding ability to erythrocytes (thereby named as HABPs), with nanomolar dissociation constants. CLAG-9 HABPs interacted with different erythrocyte surface receptors having apparent molecular weights of 85, 63 and 34 kDa. CLAG-9 HABPs binding was also affected by pre-treatment of RBCs with enzymes and inhibited erythrocyte invasion in vitro by up to 72% at 200 microM. These results suggest that some protein fragments of CLAG-9 may be part of the molecular machinery used by malaria parasites to invade erythrocytes, hence supporting their study as possible vaccine candidates.
在这项研究中，我们合成了全长 67 个 20 个氨基酸长的不重叠肽段，并评估了它们在受体配体测定中与红细胞结合的能力。发现 20 个 CLAG-9 肽段具有与红细胞特异性高亲和力结合的能力（因此命名为 HABP），解离常数为纳摩尔级。CLAG-9 HABP 与不同的红细胞表面受体相互作用，这些受体的表观分子量分别为 85、63 和 34 kDa。CLAG-9 HABP 的结合也受到 RBC 预处理酶的影响，并在 200μM 时抑制体外红细胞入侵达 72%。这些结果表明，CLAG-9 的一些蛋白片段可能是疟原虫入侵红细胞所使用的分子机制的一部分，因此支持将其作为可能的疫苗候选物进行研究。
