TY - JOUR
T1 - Hotspots in plasmodium and RBC receptor-ligand interactions
T2 - Key pieces for inhibiting malarial parasite invasion
AU - Patarroyo, Manuel Alfonso
AU - Molina-Franky, Jessica
AU - Gómez, Marcela
AU - Arévalo-Pinzón, Gabriela
AU - Patarroyo, Manuel Elkin
N1 - Publisher Copyright:
© 2020 by the authors. Licensee MDPI, Basel, Switzerland.
PY - 2020/7/1
Y1 - 2020/7/1
N2 - 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 (Pf Rh5)-basigin, and erythrocyte binding antigen 175 (EBA175)-glycophorin A (GPA).
AB - 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 (Pf Rh5)-basigin, and erythrocyte binding antigen 175 (EBA175)-glycophorin A (GPA).
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U2 - 10.3390/ijms21134729
DO - 10.3390/ijms21134729
M3 - Review article
C2 - 32630804
AN - SCOPUS:85087461505
SN - 1661-6596
VL - 21
SP - 1
EP - 24
JO - International Journal of Molecular Sciences
JF - International Journal of Molecular Sciences
IS - 13
M1 - 4729
ER -