The PTEX component EXP2 is critical for establishing a patent malaria infection in mice

Kalanon, Ming, Bargieri, Daniel, Sturm, Angelika, Matthews, Kathryn, Ghosh, Sreejoyee, Goodman, Christopher D., Thiberge, Sabine, Mollard, Vanessa, McFadden, Geoffrey I., Menard, Robert and de Koning-Ward, Tania F. 2016, The PTEX component EXP2 is critical for establishing a patent malaria infection in mice, Cellular microbiology, vol. 18, no. 3, pp. 399-412, doi: 10.1111/cmi.12520.

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Title The PTEX component EXP2 is critical for establishing a patent malaria infection in mice
Author(s) Kalanon, Ming
Bargieri, Daniel
Sturm, Angelika
Matthews, Kathryn
Ghosh, Sreejoyee
Goodman, Christopher D.
Thiberge, Sabine
Mollard, Vanessa
McFadden, Geoffrey I.
Menard, Robert
de Koning-Ward, Tania F.ORCID iD for de Koning-Ward, Tania F.
Journal name Cellular microbiology
Volume number 18
Issue number 3
Start page 399
End page 412
Total pages 14
Publisher Wiley
Place of publication Weinheim, Germany
Publication date 2016-03
ISSN 1462-5822
Keyword(s) EXP2
protein export
Summary Export of most malaria proteins into the erythrocyte cytosol requires the Plasmodium Translocon of Exported proteins (PTEX) and a cleavable Plasmodium Export Element (PEXEL). In contrast, the contribution of PTEX in the liver stages and export of liver stage proteins is unknown. Here, using the FLP/FRT conditional mutatagenesis system, we generate transgenic P. berghei parasites deficient in EXP2, the putative pore-forming component of PTEX. Our data reveal that EXP2 is important for parasite growth in the liver and critical for parasite transition to the blood, with parasites impaired in their ability to generate a patent blood-stage infection. Surprisingly, whilst parasites expressing a functional PTEX machinery can efficiently export a PEXEL-bearing GFP reporter into the erythrocyte cytosol during a blood stage infection, this same reporter aggregates in large accumulations within the confines of the parasitophorous vacuole membrane during hepatocyte growth. Notably HSP101, the putative molecular motor of PTEX, could not be detected during the early liver stages of infection, which may explain why direct protein translocation of this soluble PEXEL-bearing reporter or indeed native PEXEL proteins into the hepatocyte cytosol has not been observed. This suggests that PTEX function may not be conserved between the blood and liver stages of malaria infection. This article is protected by copyright. All rights reserved.
Language eng
DOI 10.1111/cmi.12520
Field of Research 110309 Infectious Diseases
Socio Economic Objective 920109 Infectious Diseases
HERDC Research category C1 Refereed article in a scholarly journal
Copyright notice ©2015, Wiley
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Document type: Journal Article
Collection: School of Medicine
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