Journal article

Interaction of the exported malaria protein Pf332 with the red blood cell membrane skeleton

Karena L Waller, Lisa M Stubberfield, Valentina Dubljevic, Donna W Buckingham, Narla Mohandas, Ross L Coppel, Brian M Cooke

BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES | ELSEVIER SCIENCE BV | Published : 2010

Abstract

Intra-erythrocytic Plasmodium falciparum malaria parasites synthesize and export numerous proteins into the red blood cell (RBC) cytosol, where some bind to the RBC membrane skeleton. These interactions are responsible for the altered antigenic, morphological and functional properties of parasite-infected red blood cells (IRBCs). Plasmodium falciparum protein 332 (Pf332) is a large parasite protein that associates with the membrane skeleton and who's function has recently been elucidated. Using recombinant fragments of Pf332 in in vitro interaction assays, we have localised the specific domain within Pf332 that binds to the RBC membrane skeleton to an 86 residue sequence proximal to the C-te..

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University of Melbourne Researchers

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Awarded by NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES


Funding Acknowledgements

We thank Dr. Klavs Berzins for providing anti-Pf332 antiserum. This research was supported by grants and fellowships from the NHMRC (Howard Florey Centenary Research Fellowship to KLW; Senior Research Fellowship to BMC) and the NIH (grant #DK32094). We thank Kate Fernandez for expert technical assistance.