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EMBO Rep. 2019 Jun;20(6). pii: e47102. doi: 10.15252/embr.201847102. Epub 2019 May 16.

A pan-apicomplexan phosphoinositide-binding protein acts in malarial microneme exocytosis.

Author information

1
Centre de Recherche en Infectiologie, CRCHU de Québec-Université Laval, Québec, QC, Canada.
2
Department of Medicinal Chemistry and Molecular Pharmacology and the Purdue Institute of Inflammation, Immunology and Infectious Disease, Purdue University, West Lafayette, IN, USA.
3
Division of Infectious Disease, Department of Medicine, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, AB, Canada.
4
Centre de Recherche en Infectiologie, CRCHU de Québec-Université Laval, Québec, QC, Canada dave.richard@crchudequebec.ulaval.ca.

Abstract

Invasion of human red blood cells by the malaria parasite Plasmodium falciparum is an essential step in the development of the disease. Consequently, the molecular players involved in host cell invasion represent important targets for inhibitor design and vaccine development. The process of merozoite invasion is a succession of steps underlined by the sequential secretion of the organelles of the apical complex. However, little is known with regard to how their contents are exocytosed. Here, we identify a phosphoinositide-binding protein conserved in apicomplexan parasites and show that it is important for the attachment and subsequent invasion of the erythrocyte by the merozoite. Critically, removing the protein from its site of action by knock sideways preferentially prevents the secretion of certain types of micronemes. Our results therefore provide evidence for a role of phosphoinositide lipids in the malaria invasion process and provide further insight into the secretion of microneme organelle populations, which is potentially applicable to diverse apicomplexan parasites.

KEYWORDS:

exocytosis; invasion; malaria; microneme

PMID:
31097469
PMCID:
PMC6549027
[Available on 2020-06-01]
DOI:
10.15252/embr.201847102

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