Mitchell G H, Thomas A W, Margos G, Dluzewski A R, Bannister L H
Department of Immunobiology, Guy's, King's and St Thomas' School of Medicine, Guy's Hospital, London SE1 9RT, United Kingdom.
Infect Immun. 2004 Jan;72(1):154-8. doi: 10.1128/IAI.72.1.154-158.2004.
Apical membrane antigen 1 (AMA-1) of Plasmodium merozoites is established as a candidate molecule for inclusion in a human malaria vaccine and is strongly conserved in the genus. We have investigated its function in merozoite invasion by incubating Plasmodium knowlesi merozoites with red cells in the presence of a previously described rat monoclonal antibody (MAb R31C2) raised against an invasion-inhibitory epitope of P. knowlesi AMA-1 and then fixing the material for ultrastructural analysis. We have found that the random, initial, long-range (12 nm) contact between merozoites and red cells occurs normally in the presence of the antibody, showing that AMA-1 plays no part in this stage of attachment. Instead, inhibited merozoites fail to reorientate, so they do not bring their apices to bear on the red cell surface and do not make close junctional apical contact. We conclude that AMA-1 may be directly responsible for reorientation or that the molecule may initiate the junctional contact, which is then presumably dependent on Duffy binding proteins for its completion.
疟原虫裂殖子的顶端膜抗原1(AMA-1)已被确定为一种可用于人类疟疾疫苗的候选分子,并且在疟原虫属中高度保守。我们通过在先前描述的针对诺氏疟原虫AMA-1的入侵抑制表位产生的大鼠单克隆抗体(单克隆抗体R31C2)存在的情况下,将诺氏疟原虫裂殖子与红细胞一起孵育,然后固定材料进行超微结构分析,来研究其在裂殖子入侵中的功能。我们发现,在抗体存在的情况下,裂殖子与红细胞之间随机、初始的长距离(12纳米)接触正常发生,这表明AMA-1在这个附着阶段不起作用。相反,受抑制的裂殖子无法重新定向,因此它们不会将其顶端压在红细胞表面,也不会形成紧密的顶端连接接触。我们得出结论,AMA-1可能直接负责重新定向,或者该分子可能启动连接接触,然后推测其完成可能依赖于达菲结合蛋白。