Journal article

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

O Looker, AJ Blanch, B Liu, J Nunez-Iglesias, PJ McMillan, L Tilley, MWA 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-mediat-ing 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 fl..

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Grants

Awarded by Australian Research Council


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.