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

Author(s): Coppel, RL;
Details: Publication Year 1992-02,Volume 50,Issue #2,Page 335-348
Journal Title: MOLECULAR AND BIOCHEMICAL PARASITOLOGY
Publication Type: Journal Article
Abstract: 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.
Publisher: ELSEVIER SCIENCE BV
Keywords: INFECTED ERYTHROCYTES; MALARIA PARASITES; SURFACE-ANTIGEN; RESA GENE; MEMBRANE; SEQUENCE; CYTOADHERENCE; TRANSPORT; CELLS; DNA
Publisher's Version: https://doi.org/10.1016/0166-6851(92)90231-8
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 1992-02-01 12:00:00