Abstract
Protein-protein interactions (IPP) play an essential role in practically all biological processes, including those related to microorganism invasion of their host cells. It has been found that a broad repertoire of receptor-ligand interactions takes place in the binding interphase with host cells in malaria, these being vital interactions for successful parasite invasion. Several trials have been conducted for elucidating the molecular interface of interactions between some Plasmodium falciparum and Plasmodium vivax antigens with receptors on erythrocytes and/or reticulocytes. Structural information concerning these complexes is available; however, deeper analysis is required for correlating structural, functional (binding, invasion, and inhibition), and polymorphism data for elucidating new interaction hotspots to which malaria control methods can be directed. This review describes and discusses recent structural and functional details regarding three relevant interactions during erythrocyte invasion: Duffy-binding protein 1 (DBP1)–Duffy antigen receptor for chemokines (DARC); reticulocyte-binding protein homolog 5 (PfRh5)-basigin, and erythrocyte binding antigen 175 (EBA175)-glycophorin A (GPA).
Highlights
Malaria is a disease caused by parasites from the phylum Apicomplexa and Plasmodium genus; they are characterized by two types of unique structures within the parasite: the apicoplast and the apical complex
P. falciparum reticulocyte-binding protein homolog 5 (Pf Rh5) is a prominent blood-stage antigen which is solely expressed in the subgenus Laverania and is an exceptional member of the reticulocyte-binding protein homologs (Rhs) family as it is the only Pf Rh gene where attempts at knock-out have not been successful [79]
P. falciparum and P. vivax have multiple, complex RBC invasion routes mediated by specific receptor-ligand interactions
Summary
Malaria is a disease caused by parasites from the phylum Apicomplexa and Plasmodium genus; they are characterized by two types of unique structures within the parasite: the apicoplast (a non-photosynthetic plastid) and the apical complex. Erythrocytes become more deformed after binding and, in the second phase, the parasite reorients its apical pole to come into direct contact with the host cell membrane This is called reorientation and, in P. falciparum, is mediated by the actin-myosin motor and by the early release of erythrocyte-binding antigens (EBAs) from the micronemes and reticulocyte-binding protein homologs (Rhs) from the rhoptries, binding with high affinity to a wide range of host cell receptors [17,18]. M1/19, M1/30, M1/33, M1/83: merozoite surface protein 1–19 kDa, 30 kDa, 33 kDa and 83 kDa fragments, respectively; M6/36: merozoite surface protein 6–36 kDa fragment; MSPDBL: merozoite surface protein Duffy binding-like; MSP7: merozoite surface protein 7; ETRAMP: early transcribed membrane protein; TRAg36.6, TRAg38, TRAg40, TRAg69.4 and TRAg74: Plasmodium tryptophan-rich proteins 36.6, -38, -40, -69.4 or -74; BSG: basigin; ?: yet-unknown receptor; Rh1, Rh2a, Rh2b, Rh4 and Rh5: reticulocyte-binding protein homologues -1, -2, 2a, -2b, -4 and -5; EBA175: erythrocyte binding antigen 175; EBA140: erythrocyte binding antigen 140; EBA181: erythrocyte binding antigen 181; EBL: erythrocyte binding ligand; Y/Z/W: unidentified receptors; CR1: complement receptor 1, GPYA: glycophorin A; GYPB: glycophorin B; GYPC: glycophorin C; Ripr: Pf Rh5-interacting protein, CyRPA: cysteine-rich protective antigen; AMA1: apical membrane antigen-1, DARC: Duffy antigen receptor for chemokines, RII-DBP1: Duffy binding protein 1 - region II; RBP1a/b: reticulocyte-binding protein 1a/b; RBP2a: reticulocyte-binding protein 2a; RBP2c: reticulocyte-binding protein 2c; CD71: transferrin receptor 1; RON2: rhoptry neck protein 2; RON4: rhoptry neck protein 4; RON5: rhoptry neck protein 5; AMA1 DI-II: apical membrane antigen-1 domain I-II; RON2 RI: rhoptry neck protein 2 - region I; RON2 RII: rhoptry neck protein 2 - region II
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