Unidentified reticulocyte receptor recognized by PvAMA-1

The unidentified reticulocyte receptor recognized by Plasmodium vivax Apical Membrane Antigen 1 (PvAMA-1) is a host cell surface protein essential for the invasion of human reticulocytes by the malaria parasite. While PvAMA-1 is well-known for its interaction with the parasite-derived protein RON2 to form a moving junction, recent evidence indicates it also binds directly to a host receptor on the reticulocyte membrane. This interaction is critical for the initial attachment and reorientation of the merozoite during the invasion process. Targeting this receptor-ligand interaction with monoclonal antibodies or vaccines is a major strategy for developing blood-stage malaria interventions. Although the exact molecular identity of this host receptor has historically been unknown, recent research has identified KREMEN1 as a functional receptor for AMA-1 across multiple Plasmodium species, including P. vivax. Its role in the strict tropism of P. vivax for immature red blood cells makes it a high-priority therapeutic target for preventing clinical malaria symptoms.

Other names

PvAMA-1 host receptorUnknown reticulocyte receptor for PvAMA-1PvAMA1-binding erythrocyte proteinKREMEN1 (putative)

Blocking the interaction between PvAMA-1 and its host receptor prevents the formation of the moving junction and inhibits the invasion of reticulocytes by Plasmodium vivax merozoites.