Journal article
A lysine-rich membrane-associated PHISTb protein involved in alteration of the cytoadhesive properties of Plasmodium falciparum-infected red blood cells
NI Proellocks, S Herrmann, DW Buckingham, E Hanssen, EK Hodges, B Elsworth, BJ Morahan, RL Coppel, BM Cooke
FASEB Journal | Published : 2014
DOI: 10.1096/fj.14-250399
Abstract
The genomes of malaria parasites (Plasmodium spp.) contain a family of genes encoding proteins with a Plasmodium helical interspersed subtelo-meric (PHIST) domain, most of which are predicted to be exported into the parasite-infected human red blood cell (iRBC). Here, using transgenic parasites and a combination of cellular, biochemical, and biophysical assays, we have characterized and determined the function of a novel member of the PHIST protein family in Plasmodium falciparum, termed lysine-rich membrane-associated PHISTb (LyMP). LyMP was shown to associate directly with the cytoskeleton of iRBCs where it plays a role in their abnormal ability to adhere to a protein expressed on vascular..
View full abstractGrants
Funding Acknowledgements
The authors thank Dr. Alexander Maier (Australian National University, Canberra) for providing the antiserum against PFB0090c (J-dots) and are grateful to the Australian Red Cross Blood Service for generously providing human RBCs for malaria culture. B. M. C. was supported by the National Health and Medical Research Council of Australia (NHMRC). The authors also acknowledge the Faculty of Medicine, Nursing and Health Sciences of Monash University for supporting N.I.P. with a Faculty Bridging Fellowship that enabled this work. E.H. was supported by an Australian Postgraduate Award.