Journal article
Analysis of structure and function of the giant protein Pf332 in Plasmodium falciparum
AN Hodder, AG Maier, M Rug, M Brown, M Hommel, I Pantic, M Puig-De-Morales-Marinkovic, B Smith, T Triglia, J Beeson, AF Cowman
Molecular Microbiology | WILEY | Published : 2009
Abstract
Virulence of Plasmodium falciparum, the most lethal parasitic disease in humans, results in part from adhesiveness and increased rigidity of infected erythrocytes. Pf332 is trafficked to the parasite-infected erythrocyte via Maurer's clefts, structures for protein sorting and export in the host erythrocyte. This protein has a domain similar to the Duffy-binding-like (DBL) domain, which functions by binding to receptors for adherence and invasion. To address structure of the Pf332 DBL domain, we expressed this region, and validated its fold on the basis of the disulphide bond pattern, which conformed to the generic pattern for DBL domains. The modelled structure for Pf332 DBL had differences ..
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Awarded by National Heart, Lung, and Blood Institute
Funding Acknowledgements
We thank Brian Shiell and Gary Beddome from CSIRO Australian Animal Health Laboratory for their assistance with Edman sequencing and mass spectrometry. Also we thank Dr Simon Crawford and Anna Friedhuber (University of Melbourne) for assistance with transmission electron microscopy, Paul Gilson and Brendan Crabb for the anti-MSP1 antibody. A. G. M. is an ARC Australian Research Fellow. A. F. C. is an International Howard Hughes Scholar and a NHMRC Australia Fellow. We thank the WEHI Monoclonal Facility for antibodies, donors and Red Cross Blood Service (Melbourne, Australia) for erythrocytes and serum and study participants in PNG. M. P.-d.-M. M. acknowledges support from the NHLBI Grant HL-007118 and REG from Harvard University. This work was supported by the NIH (RO1 AI44008), Wellcome Trust and the NHMRC of Australia.