Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton

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Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton. / Oberli, Alexander; Zurbrügg, Laura; Rusch, Sebastian; Brand, Françoise; Butler, Madeleine E; Day, Jemma L; Cutts, Erin E; Lavstsen, Thomas; Vakonakis, Ioannis; Beck, Hans-Peter.

In: Cellular Microbiology, Vol. 18, No. 10, 10.2016, p. 1415-1428.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Oberli, A, Zurbrügg, L, Rusch, S, Brand, F, Butler, ME, Day, JL, Cutts, EE, Lavstsen, T, Vakonakis, I & Beck, H-P 2016, 'Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton', Cellular Microbiology, vol. 18, no. 10, pp. 1415-1428. https://doi.org/10.1111/cmi.12583

APA

Oberli, A., Zurbrügg, L., Rusch, S., Brand, F., Butler, M. E., Day, J. L., Cutts, E. E., Lavstsen, T., Vakonakis, I., & Beck, H-P. (2016). Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton. Cellular Microbiology, 18(10), 1415-1428. https://doi.org/10.1111/cmi.12583

Vancouver

Oberli A, Zurbrügg L, Rusch S, Brand F, Butler ME, Day JL et al. Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton. Cellular Microbiology. 2016 Oct;18(10):1415-1428. https://doi.org/10.1111/cmi.12583

Author

Oberli, Alexander ; Zurbrügg, Laura ; Rusch, Sebastian ; Brand, Françoise ; Butler, Madeleine E ; Day, Jemma L ; Cutts, Erin E ; Lavstsen, Thomas ; Vakonakis, Ioannis ; Beck, Hans-Peter. / Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton. In: Cellular Microbiology. 2016 ; Vol. 18, No. 10. pp. 1415-1428.

Bibtex

@article{82a88443677d4b98ab308a040047ff8e,
title = "Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton",
abstract = "Adherence of Plasmodium falciparum-infected erythrocytes to host endothelium is conferred through the parasite-derived virulence factor P. falciparum erythrocyte membrane protein 1 (PfEMP1), the major contributor to malaria severity. PfEMP1 located at knob structures on the erythrocyte surface is anchored to the cytoskeleton, and the Plasmodium helical interspersed subtelomeric (PHIST) gene family plays a role in many host cell modifications including binding the intracellular domain of PfEMP1. Here, we show that conditional reduction of the PHIST protein PFE1605w strongly reduces adhesion of infected erythrocytes to the endothelial receptor CD36. Adhesion to other endothelial receptors was less affected or even unaltered by PFE1605w depletion, suggesting that PHIST proteins might be optimized for subsets of PfEMP1 variants. PFE1605w does not play a role in PfEMP1 transport, but it directly interacts with both the intracellular segment of PfEMP1 and with cytoskeletal components. This is the first report of a PHIST protein interacting with key molecules of the cytoadherence complex and the host cytoskeleton, and this functional role seems to play an essential role in the pathology of P. falciparum.",
author = "Alexander Oberli and Laura Zurbr{\"u}gg and Sebastian Rusch and Fran{\c c}oise Brand and Butler, {Madeleine E} and Day, {Jemma L} and Cutts, {Erin E} and Thomas Lavstsen and Ioannis Vakonakis and Hans-Peter Beck",
note = "{\textcopyright} 2016 The Authors. Cellular Microbiology published by John Wiley & Sons Ltd.",
year = "2016",
month = oct,
doi = "10.1111/cmi.12583",
language = "English",
volume = "18",
pages = "1415--1428",
journal = "Cellular Microbiology",
issn = "1462-5814",
publisher = "Wiley-Blackwell",
number = "10",

}

RIS

TY - JOUR

T1 - Plasmodium falciparum Plasmodium helical interspersed subtelomeric proteins contribute to cytoadherence and anchor P. falciparum erythrocyte membrane protein 1 to the host cell cytoskeleton

AU - Oberli, Alexander

AU - Zurbrügg, Laura

AU - Rusch, Sebastian

AU - Brand, Françoise

AU - Butler, Madeleine E

AU - Day, Jemma L

AU - Cutts, Erin E

AU - Lavstsen, Thomas

AU - Vakonakis, Ioannis

AU - Beck, Hans-Peter

N1 - © 2016 The Authors. Cellular Microbiology published by John Wiley & Sons Ltd.

PY - 2016/10

Y1 - 2016/10

N2 - Adherence of Plasmodium falciparum-infected erythrocytes to host endothelium is conferred through the parasite-derived virulence factor P. falciparum erythrocyte membrane protein 1 (PfEMP1), the major contributor to malaria severity. PfEMP1 located at knob structures on the erythrocyte surface is anchored to the cytoskeleton, and the Plasmodium helical interspersed subtelomeric (PHIST) gene family plays a role in many host cell modifications including binding the intracellular domain of PfEMP1. Here, we show that conditional reduction of the PHIST protein PFE1605w strongly reduces adhesion of infected erythrocytes to the endothelial receptor CD36. Adhesion to other endothelial receptors was less affected or even unaltered by PFE1605w depletion, suggesting that PHIST proteins might be optimized for subsets of PfEMP1 variants. PFE1605w does not play a role in PfEMP1 transport, but it directly interacts with both the intracellular segment of PfEMP1 and with cytoskeletal components. This is the first report of a PHIST protein interacting with key molecules of the cytoadherence complex and the host cytoskeleton, and this functional role seems to play an essential role in the pathology of P. falciparum.

AB - Adherence of Plasmodium falciparum-infected erythrocytes to host endothelium is conferred through the parasite-derived virulence factor P. falciparum erythrocyte membrane protein 1 (PfEMP1), the major contributor to malaria severity. PfEMP1 located at knob structures on the erythrocyte surface is anchored to the cytoskeleton, and the Plasmodium helical interspersed subtelomeric (PHIST) gene family plays a role in many host cell modifications including binding the intracellular domain of PfEMP1. Here, we show that conditional reduction of the PHIST protein PFE1605w strongly reduces adhesion of infected erythrocytes to the endothelial receptor CD36. Adhesion to other endothelial receptors was less affected or even unaltered by PFE1605w depletion, suggesting that PHIST proteins might be optimized for subsets of PfEMP1 variants. PFE1605w does not play a role in PfEMP1 transport, but it directly interacts with both the intracellular segment of PfEMP1 and with cytoskeletal components. This is the first report of a PHIST protein interacting with key molecules of the cytoadherence complex and the host cytoskeleton, and this functional role seems to play an essential role in the pathology of P. falciparum.

U2 - 10.1111/cmi.12583

DO - 10.1111/cmi.12583

M3 - Journal article

C2 - 26916885

VL - 18

SP - 1415

EP - 1428

JO - Cellular Microbiology

JF - Cellular Microbiology

SN - 1462-5814

IS - 10

ER -

ID: 165851576