scholarly journals A and T homopolymeric stretches mediate a DNA inversion in Plasmodium falciparum which results in loss of gene expression.

1990 ◽  
Vol 10 (6) ◽  
pp. 3243-3246 ◽  
Author(s):  
L G Pologe ◽  
D de Bruin ◽  
J V Ravetch
Keyword(s):  
Gene Expression ◽  
Plasmodium Falciparum ◽  
Gene Structure ◽  
Infected Erythrocyte ◽  
Dna Rearrangement ◽  
Coding Sequences ◽  
Dna Inversion ◽  
Erythrocyte Surface ◽  
Stable Substrate ◽  
Flanking Sequences

Ring-infected erythrocyte surface antigen-negative isolates of Plasmodium falciparum demonstrate a complex DNA rearrangement with inversion of 5' coding sequences, deletion of upstream and flanking sequences, and healing of the truncated chromosome by telomere addition. An inversion intermediate that results in the telomeric gene structure for RESA has been identified in the pathway. This inversion creates a mitotically stable substrate for the sequence-specific addition of telomere repeats at the deletion breakpoint.

A and T homopolymeric stretches mediate a DNA inversion in Plasmodium falciparum which results in loss of gene expression

1990 ◽  
Vol 10 (6) ◽  
pp. 3243-3246
Author(s):  
L G Pologe ◽  
D de Bruin ◽  
J V Ravetch
Keyword(s):  
Gene Expression ◽  
Plasmodium Falciparum ◽  
Gene Structure ◽  
Infected Erythrocyte ◽  
Dna Rearrangement ◽  
Coding Sequences ◽  
Dna Inversion ◽  
Erythrocyte Surface ◽  
Stable Substrate ◽  
Flanking Sequences

Ring-infected erythrocyte surface antigen-negative isolates of Plasmodium falciparum demonstrate a complex DNA rearrangement with inversion of 5' coding sequences, deletion of upstream and flanking sequences, and healing of the truncated chromosome by telomere addition. An inversion intermediate that results in the telomeric gene structure for RESA has been identified in the pathway. This inversion creates a mitotically stable substrate for the sequence-specific addition of telomere repeats at the deletion breakpoint.

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
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