Molecular interactions and signaling mechanisms during erythrocyte invasion by malaria parasites

Curr Opin Microbiol. 2011 Aug;14(4):422-8. doi: 10.1016/j.mib.2011.07.018. Epub 2011 Jul 29.

Abstract

Invasion of erythrocytes by Plasmodium merozoites is a complex process that is mediated by specific molecular interactions. Here, we review recent studies on interactions between erythrocyte binding antigens (EBA) and PfRH proteins from the parasite and erythrocyte receptors involved in invasion. The timely release of these parasite ligands from internal organelles such as micronemes and rhoptries to the merozoite surface is critical for receptor-engagement leading to successful invasion. We review information on signaling mechanisms that control the regulated secretion of parasite proteins during invasion. Erythrocyte invasion involves the formation and movement of a junction between the invading merozoite and host erythrocyte. We review recent studies on the molecular composition of the junction and the molecular motor that drives movement of the junction.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Actins / metabolism
  • Animals
  • Antigens, Protozoan / metabolism
  • Calcium / metabolism
  • Cell Movement
  • Erythrocytes / immunology
  • Erythrocytes / metabolism
  • Erythrocytes / parasitology*
  • Host-Parasite Interactions*
  • Humans
  • Intracellular Membranes / metabolism
  • Malaria / immunology
  • Malaria / parasitology
  • Merozoites / immunology
  • Merozoites / metabolism
  • N-Acetylneuraminic Acid / metabolism
  • Plasmodium / genetics
  • Plasmodium / immunology
  • Plasmodium / pathogenicity*
  • Protozoan Proteins / metabolism
  • Receptors, Cell Surface / metabolism
  • Signal Transduction*
  • Tight Junctions / immunology
  • Tight Junctions / metabolism

Substances

  • Actins
  • Antigens, Protozoan
  • Duffy antigen binding protein, Plasmodium
  • Protozoan Proteins
  • Receptors, Cell Surface
  • rhoptry associated protein, Plasmodium
  • N-Acetylneuraminic Acid
  • Calcium