THE PLASMODIUM-FALCIPARUM PROTEIN RESA INTERACTS WITH THE ERYTHROCYTE CYTOSKELETON AND MODIFIES ERYTHROCYTE THERMAL-STABILITY
- Author(s)
- DASILVA, E; Foley, M; DLUZEWSKI, AR; MURRAY, LJ; Anders, RF; Tilley, L;
- Details
- Publication Year 1994-07,Volume 66,Issue #1,Page 59-69
- Journal Title
- MOLECULAR AND BIOCHEMICAL PARASITOLOGY
- Publication Type
- Journal Article
- Abstract
- The ring-infected erythrocyte surface antigen (RESA) associates with spectrin in the erythrocyte membrane (Foley, M., Tilley, L., Sawyer, W.H. and Anders, R.F. (1991) Mol. Biochem. Parasitol., 46, 137-148). A fragment of the RESA protein, which was expressed in Escherichia coli, was found to bind to inside-out vesicles of erythrocyte membranes in an apparently saturable manner. Upon extraction of inside-out vesicles with Triton X-100, the RESA fragment remained associated with the erythrocyte cytoskeleton. Using the technique of steady-state fluorescence polarisation, we have studied the thermal denaturation of fluorescein-labelled spectrin in the presence of recombinant RESA. We found that the RESA fragment partially protected spectrin against heat-induced conformational changes. Furthermore, erythrocytes infected with a RESA (-) laboratory strain (FCR3) was shown to be more susceptible to heat-induced fragmentation than erythrocytes infected with a RESA (+) strain of the parasite. RESA does not however, appear to play an essential role in the invasion process per se as erythrocytes resealed to contain anti-RESA antibodies were efficiently invaded.d
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- SURFACE-ANTIGEN; STRUCTURAL TRANSITIONS; MALARIA PARASITES; CELL MEMBRANE; SPECTRIN; GENE; DNAJ; ASSOCIATION; INVOLVEMENT; PF155/RESA
- Publisher's Version
- https://doi.org/10.1016/0166-6851(94)90036-1
- Terms of Use/Rights Notice
- Refer to copyright notice on published article.
Creation Date: 1994-07-01 12:00:00