REPEAT STRUCTURES IN A PLASMODIUM-FALCIPARUM PROTEIN (MESA) THAT BINDS HUMAN ERYTHROCYTE PROTEIN 4.1

被引:49
作者
COPPEL, RL
机构
[1] Institute of Medical Research, Royal Melbourne Hospital, Melbourne, Vic., The Walter and Eliza Hall
关键词
MESA; REPEATS; ALPHA-HELIX; PLASMODIUM-FALCIPARUM; ERYTHROCYTE MEMBRANE SKELETON; VARIABILITY;
D O I
10.1016/0166-6851(92)90231-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The mature-parasite-infected erythrocyte surface antigen (MESA, also known as PfEMP-2 and pp300) of Plasmodium falciparum is a phosphoprotein of approx. 250-300 kDa that is exported from the parasite to the erythrocyte membrane skeleton where it binds to protein 4.1. Determination of the primary sequence of MESA reveals that it is encoded by 2 exons, a structure common to other exported proteins of P. falciparum. The MESA protein is heavily charged and contains 7 distinct repeat regions that compose over 60% of the protein. The predicted secondary structure suggests that MESA is a fibrillar protein and it shows similarity to a number of cytoskeletal and neurofilament proteins, including myosin, a protein that itself binds to protein 4.1.
引用
收藏
页码:335 / 348
页数:14
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