scholarly journals Plasmodium falciparum ring-infected erythrocyte surface antigen is released from merozoite dense granules after erythrocyte invasion.

1991 ◽  
Vol 59 (3) ◽  
pp. 1183-1187 ◽  
Author(s):  
J G Culvenor ◽  
K P Day ◽  
R F Anders
Keyword(s):  
Plasmodium Falciparum ◽  
Surface Antigen ◽  
Infected Erythrocyte ◽  
Dense Granules ◽  
Erythrocyte Invasion ◽  
Erythrocyte Surface

Expression of the RESA gene in Plasmodium falciparum isolate FCR3 is prevented by a subtelomeric deletion

1989 ◽  
Vol 9 (8) ◽  
pp. 3584-3587
Author(s):  
R Cappai ◽  
M R van Schravendijk ◽  
R F Anders ◽  
M G Peterson ◽  
L M Thomas ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Surface Antigen ◽  
Infected Erythrocyte ◽  
Falciparum Isolate ◽  
Erythrocyte Surface ◽  
Subtelomeric Deletion

We show here that the Plasmodium falciparum isolate FCR3 does not express the ring-infected erythrocyte surface antigen (RESA). This is because the 5' end of the RESA gene has been inverted and partly deleted and a telomere has been added to it. We propose a model to explain these events.

scholarly journals The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion

Blood ◽  
2007 ◽  
Vol 110 (3) ◽  
pp. 1036-1042 ◽  
Author(s):  
Xinhong Pei ◽  
Xinhua Guo ◽  
Ross Coppel ◽  
Souvik Bhattacharjee ◽  
Kasturi Haldar ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Surface Antigen ◽  
Infected Erythrocyte ◽  
Host Cell Membrane ◽  
Acid Fragment ◽  
Erythrocyte Surface ◽  
Parasite Plasmodium Falciparum ◽  
Functional Consequences ◽  
Self Association ◽  
Resistance To Invasion

AbstractThe malaria parasite Plasmodium falciparum releases the ring-infected erythrocyte surface antigen (RESA) inside the red cell on entry. The protein migrates to the host cell membrane, where it binds to spectrin, but neither the nature of the interaction nor its functional consequences have previously been defined. Here, we identify the binding motifs involved in the interaction and describe a possible function. We have found that spectrin binds to a 108–amino acid fragment (residues 663-770) of RESA, and that this RESA fragment binds to repeat 16 of the β-chain, close to the labile dimer-dimer self-association site. We further show that the RESA fragment stabilizes the spectrin tetramer against dissociation into its constituent dimers, both in situ and in solution. This is accompanied by enhanced resistance of the cell to both mechanical and thermal degradation. Resealed erythrocytes containing RESA663-770 display resistance to invasion by merozoites of P falciparum. We infer that the evolutionary advantage of RESA to the parasite lies in its ability to prevent invasion of cells that are already host to a developing parasite, as well as possibly to guard the cell against thermal damage at the elevated body temperatures prevailing in febrile crises.

Immunization Trials with the Ring-Infected Erythrocyte Surface Antigen of Plasmodium falciparum in Owl Monkeys (Aotus Vociferans)

1988 ◽  
Vol 38 (2) ◽  
pp. 268-282 ◽  
Author(s):  
William E. Collins ◽  
Graham F. Mitchell ◽  
Marguerite Pappaioanou ◽  
Graham V. Brown ◽  
Gary H. Campbell ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Surface Antigen ◽  
Infected Erythrocyte ◽  
Erythrocyte Surface ◽  
Owl Monkeys

Assessment of the Protective Value of Antibodies to the Plasmodium falciparum Ring-infected Erythrocyte Surface Antigen (RESA): An Epidemiologic Study in Madagascar

1991 ◽  
Vol 133 (2) ◽  
pp. 177-184 ◽  
Author(s):  
Pascal Astagneau ◽  
Jean Paul Lepers ◽  
Claire Chougnet ◽  
Claude Gaudebout ◽  
Marie Danielle Andriarnangatiana-Rason ◽  
...  
Keyword(s):  
Plasmodium Falciparum ◽  
Surface Antigen ◽  
Infected Erythrocyte ◽  
Epidemiologic Study ◽  
Erythrocyte Surface
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