A reticulocyte-binding protein complex of Plasmodium vivax merozoites

Cell. 1992 Jun 26;69(7):1213-26. doi: 10.1016/0092-8674(92)90642-p.


Plasmodium vivax merozoites primarily invade reticulocytes. The basis of this restricted host cell preference has been debated. Here we introduce two novel P. vivax proteins that comigrate on reducing SDS-polyacrylamide gels, colocalize at the apical pole of merozoites, and adhere specifically to reticulocytes. The genes encoding these proteins, P. vivax reticulocyte-binding proteins 1 and 2 (PvRBP-1 and PvRBP-2), have been cloned and analyzed. Homologous genes are evident in the closely related simian malaria parasite, P. cynomolgi, which also prefers to invade reticulocytes, but are not evident in the genome of another related simian malaria parasite, P. knowlesi, which invades all red blood cell subpopulations. Native PvRBP-1 is likely a transmembrane-anchored disulfide-linked protein, and along with PvRBP-2 may function as an adhesive protein complex. We propose that the RBPs of P. vivax, and homologous proteins of P. cynomolgi, function to target the reticulocyte subpopulation of red blood cells for invasion.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, Non-P.H.S.
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • Membrane Proteins / analysis*
  • Membrane Proteins / genetics
  • Molecular Sequence Data
  • Plasmodium knowlesi / genetics
  • Plasmodium vivax / genetics*
  • Plasmodium vivax / parasitology
  • Protozoan Proteins / analysis*
  • Protozoan Proteins / metabolism
  • Reticulocytes / metabolism*


  • Membrane Proteins
  • Protozoan Proteins
  • reticulocyte-binding protein, Plasmodium vivax

Associated data

  • GENBANK/M88097
  • GENBANK/M88098