Crandall I, Sherman I W
Department of Biology, University of California, Riverside 92521, USA.
Parasitology. 1996 Mar;112 ( Pt 3):261-7. doi: 10.1017/s003118200006577x.
Epitope mapping of a murine monoclonal antibody (mAb), 5H12, prepared against live Plasmodium falciparum-infected red blood cells indicated that the epitope consisted of amino acid residues 474-487 of the human anion transport protein, band 3. mAb 5H12 enhanced cytoadherence, but inhibited the CD36-like mediated rosetting. A synthetic peptide based on the sequence of the epitope (FSFCETNGLE) blocked both rosetting and cytoadherence, suggesting that this amino acid sequence may form the CD36-like receptor. The CD36-like region of band 3 was antigenically distinct from platelet or endothelial CD36.
针对感染恶性疟原虫的活红细胞制备的鼠单克隆抗体（mAb）5H12的表位作图表明，该表位由人阴离子转运蛋白带3的474 - 487位氨基酸残基组成。单克隆抗体5H12增强了细胞黏附，但抑制了CD36样介导的玫瑰花结形成。基于该表位序列（FSFCETNGLE）的合成肽阻断了玫瑰花结形成和细胞黏附，表明该氨基酸序列可能构成CD36样受体。带3的CD36样区域在抗原性上与血小板或内皮细胞CD36不同。
