ApiLoc - A database of published protein sub-cellular localisation in Apicomplexa

version 3 (curated until May 28, 2011)

Molecular characterization and inhibition of a Plasmodium falciparum aspartic hemoglobinase.

Francis, S. E., Gluzman, I. Y., Oksman, A., Knickerbocker, A., Mueller, R., Bryant, M. L., Sherman, D. R., Russell, D. G., Goldberg, D. E. (1994 Jan 15, EMBO J)

Intraerythrocytic malaria parasites rapidly degrade virtually all of the host cell hemoglobin. We have cloned the gene for an aspartic hemoglobinase that initiates the hemoglobin degradation pathway in Plasmodium falciparum. It encodes a protein with 35% homology to human renin and cathepsin D, but has an unusually long pro-piece that includes a putative membrane spanning anchor. Immunolocalization studies place the enzyme in the digestive vacuole and throughout the hemoglobin ingestion pathway, suggesting an unusual protein targeting route. A peptidomimetic inhibitor selectively blocks the aspartic hemoglobinase, prevents hemoglobin degradation and kills the organism. We conclude that Plasmodium hemoglobin catabolism is a prime target for antimalarial chemotherapy and have identified a lead compound towards this goal.

PubMed: 8313875, full text

Localisation information

PF14_0076 (FAF-2, aspartic hemoglobinase I, PMI, PM1, Plasmepsin I, PM I) plasmepsin I

Experimental localisation: trophozoite
  • Species: Plasmodium falciparum
  • Quote inferring localisation: "Immunolocalization studies place the enzyme in the digestive vacuole and throughout the hemoglobin ingestion pathway, suggesting an unusual protein targeting route."
  • Microscopy type: Light, EM
  • Microscopy method: antibody
  • Strain: HB3
  • Gene model mapping comments: Blast from X75787.1, inconsistent 5' and 3' UTR
  • Localisation record: during troph
  • Comment: protein named PMI by 14709539