Studies of Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) protein peptides specifically binding to human RBC.
Plasmodium falciparum rhoptry-associated membrane antigen (RAMA) peptides used in normal red blood cell (RBC) binding assays revealed that peptides 33426 (79NINILSSVHRKGRILYDSF97) and 33460 (777HKKREKSISPHSYQKVSTKVQ797) bound with high activity, presenting nanomolar affinity constants. Such high binding activity peptides (HABPs) displayed helicoid and random coil structures as determined by circular dichroism. HABPs inhibited P. falciparumin vitro invasion of normal RBC by up to 61% (depending on concentration), suggesting that some RAMA protein regions could be involved in P. falciparum invasion of RBC. The nature and localisation of receptors on RBC surface responsible for HABP binding were studied using enzyme-treated erythrocytes and structural analysis.
Pinzón
Carlos Giovanni
CG
Fundación Instituto de Inmunologia de Colombia (FIDIC), Colombia.
Curtidor
Hernando
H
Bermúdez
Adriana
A
Forero
Martha
M
Vanegas
Magnolia
M
Rodríguez
Jorge
J
Patarroyo
Manuel E
ME
D000595:Amino Acid Sequence; D000818:Animals; D000953:Antigens, Protozoan / Q000737:chemistry / Q000378:metabolism*; D002942:Circular Dichroism; D004912:Erythrocytes / Q000187:drug effects / Q000378:metabolism* / Q000469:parasitology; D006801:Humans; D008565:Membrane Proteins / Q000032:analysis / Q000378:metabolism; D008969:Molecular Sequence Data; D010455:Peptides / Q000138:chemical synthesis / Q000235:genetics / Q000378:metabolism / Q000494:pharmacology; D010963:Plasmodium falciparum / Q000378:metabolism; D011485:Protein Binding; D015800:Protozoan Proteins / Q000737:chemistry / Q000378:metabolism*; D052939:Schizonts / Q000378:metabolism
D000953:Antigens, Protozoan; D008565:Membrane Proteins; D010455:Peptides; D015800:Protozoan Proteins; C065352:rhoptry associated protein, Plasmodium