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© Research
Publication : Molecular and biochemical parasitology

Pfsbp1, a Maurer’s cleft Plasmodium falciparum protein, is associated with the erythrocyte skeleton

Scientific Fields
Diseases
Organisms
Applications
Technique

Published in Molecular and biochemical parasitology - 01 Nov 2000

Blisnick T, Morales Betoulle ME, Barale JC, Uzureau P, Berry L, Desroses S, Fujioka H, Mattei D, Braun Breton C

Link to Pubmed [PMID] – 11087921

Mol. Biochem. Parasitol. 2000 Nov;111(1):107-21

Antibodies from hyperimmune monkey sera, selected by absorption to Plasmodium falciparum-infected erythrocytes, and elution at acidic pH, allowed us to characterize a novel parasite protein, Pfsbp1 (P. falciparum skeleton binding protein 1). Pfsbp1 is an integral membrane protein of parasite-induced membranous structures associated with the erythrocyte plasma membrane and referred to as Maurer’s clefts. The carboxy-terminal domain of Pfsbp1, exposed within the cytoplasm of the host cell, interacts with a 35 kDa erythrocyte skeletal protein and might participate in the binding of the Maurer’s clefts to the erythrocyte submembrane skeleton. Antibodies to the carboxy- and amino-terminal domains of Pfsbp1 labelled similar vesicular structures in the cytoplasm of Plasmodium chabaudi and Plasmodium berghei-infected murine erythrocytes, suggesting that the protein is conserved among malaria species, consistent with an important role of Maurer’s cleft-like structures in the intraerythrocytic development of malaria parasites.

http://www.ncbi.nlm.nih.gov/pubmed/11087921