Journal article

The knob protein KAHRP assembles into a ring-shaped structure that underpins virulence complex assembly

Oliver Looker, Adam J Blanch, Boyin Liu, Juan Nunez-Iglesias, Paul J McMillan, Leann Tilley, Matthew WA Dixon

PLOS PATHOGENS | PUBLIC LIBRARY SCIENCE | Published : 2019

Abstract

Plasmodium falciparum mediates adhesion of infected red blood cells (RBCs) to blood vessel walls by assembling a multi-protein complex at the RBC surface. This virulence-mediating structure, called the knob, acts as a scaffold for the presentation of the major virulence antigen, P. falciparum Erythrocyte Membrane Protein-1 (PfEMP1). In this work we developed correlative STochastic Optical Reconstruction Microscopy-Scanning Electron Microscopy (STORM-SEM) to spatially and temporally map the delivery of the knob-associated histidine-rich protein (KAHRP) and PfEMP1 to the RBC membrane skeleton. We show that KAHRP is delivered as individual modules that assemble in situ, giving a ring-shaped flu..

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Grants

Awarded by Australian Research Council


Awarded by National Health and Medical Research Council


Awarded by National Health and Medical Research Council Training fellowship


Funding Acknowledgements

LT is a Georgina Sweet, Australian Research Council Laureate Fellow (LE150100011) (http://www.arc.gov.au).MWAD and LT thank the Australian Research Council (DP110100624) (http://www.arc.gov.au) and the National Health and Medical Research Council (1098992) (https://www.nhmrc.gov.au) for funding this work. MWAD was supported by a National Health and Medical Research Council Training fellowship (602541). The funders had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.