Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1

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Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1. / Rajan Raghavan, Sai Sundar; Turner, Louise; Jensen, Rasmus W.; Johansen, Nicolai Tidemand; Jensen, Daniel Skjold; Gourdon, Pontus; Zhang, Jinqiu; Wang, Yong; Theander, Thor Grundtvig; Wang, Kaituo; Lavstsen, Thomas.

I: Structure, Bind 31, Nr. 10, 2023, s. 1174-1183.e4.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

Rajan Raghavan, SS, Turner, L, Jensen, RW, Johansen, NT, Jensen, DS, Gourdon, P, Zhang, J, Wang, Y, Theander, TG, Wang, K & Lavstsen, T 2023, 'Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1', Structure, bind 31, nr. 10, s. 1174-1183.e4. https://doi.org/10.1016/j.str.2023.07.011

APA

Rajan Raghavan, S. S., Turner, L., Jensen, R. W., Johansen, N. T., Jensen, D. S., Gourdon, P., Zhang, J., Wang, Y., Theander, T. G., Wang, K., & Lavstsen, T. (2023). Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1. Structure, 31(10), 1174-1183.e4. https://doi.org/10.1016/j.str.2023.07.011

Vancouver

Rajan Raghavan SS, Turner L, Jensen RW, Johansen NT, Jensen DS, Gourdon P o.a. Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1. Structure. 2023;31(10):1174-1183.e4. https://doi.org/10.1016/j.str.2023.07.011

Author

Rajan Raghavan, Sai Sundar ; Turner, Louise ; Jensen, Rasmus W. ; Johansen, Nicolai Tidemand ; Jensen, Daniel Skjold ; Gourdon, Pontus ; Zhang, Jinqiu ; Wang, Yong ; Theander, Thor Grundtvig ; Wang, Kaituo ; Lavstsen, Thomas. / Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1. I: Structure. 2023 ; Bind 31, Nr. 10. s. 1174-1183.e4.

Bibtex

@article{ab6dd5a8b21b460eb6f4cf444cb08b88,
title = "Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1",
abstract = "Severe Plasmodium falciparum malaria infections are caused by microvascular sequestration of parasites binding to the human endothelial protein C receptor (EPCR) via the multi-domain P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesion ligands. Using cryogenic electron microscopy (Cryo-EM) and PfEMP1 sequence diversity analysis, we found that group A PfEMP1 CIDRα1 domains interact with the adjacent DBLα1 domain through central, conserved residues of the EPCR-binding site to adopt a compact conformation. Upon EPCR binding, the DBLα1 domain is displaced, and the EPCR-binding helix of CIDRα1 is turned, kinked, and twisted to reach a rearranged, stable EPCR-bound conformation. The unbound conformation and the required transition to the EPCR-bound conformation may represent a conformational masking mechanism of immune evasion for the PfEMP1 family.",
author = "{Rajan Raghavan}, {Sai Sundar} and Louise Turner and Jensen, {Rasmus W.} and Johansen, {Nicolai Tidemand} and Jensen, {Daniel Skjold} and Pontus Gourdon and Jinqiu Zhang and Yong Wang and Theander, {Thor Grundtvig} and Kaituo Wang and Thomas Lavstsen",
note = "Publisher Copyright: {\textcopyright} 2023 Elsevier Ltd",
year = "2023",
doi = "10.1016/j.str.2023.07.011",
language = "English",
volume = "31",
pages = "1174--1183.e4",
journal = "Structure",
issn = "0969-2126",
publisher = "Cell Press",
number = "10",

}

RIS

TY - JOUR

T1 - Endothelial protein C receptor binding induces conformational changes to severe malaria-associated group A PfEMP1

AU - Rajan Raghavan, Sai Sundar

AU - Turner, Louise

AU - Jensen, Rasmus W.

AU - Johansen, Nicolai Tidemand

AU - Jensen, Daniel Skjold

AU - Gourdon, Pontus

AU - Zhang, Jinqiu

AU - Wang, Yong

AU - Theander, Thor Grundtvig

AU - Wang, Kaituo

AU - Lavstsen, Thomas

N1 - Publisher Copyright: © 2023 Elsevier Ltd

PY - 2023

Y1 - 2023

N2 - Severe Plasmodium falciparum malaria infections are caused by microvascular sequestration of parasites binding to the human endothelial protein C receptor (EPCR) via the multi-domain P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesion ligands. Using cryogenic electron microscopy (Cryo-EM) and PfEMP1 sequence diversity analysis, we found that group A PfEMP1 CIDRα1 domains interact with the adjacent DBLα1 domain through central, conserved residues of the EPCR-binding site to adopt a compact conformation. Upon EPCR binding, the DBLα1 domain is displaced, and the EPCR-binding helix of CIDRα1 is turned, kinked, and twisted to reach a rearranged, stable EPCR-bound conformation. The unbound conformation and the required transition to the EPCR-bound conformation may represent a conformational masking mechanism of immune evasion for the PfEMP1 family.

AB - Severe Plasmodium falciparum malaria infections are caused by microvascular sequestration of parasites binding to the human endothelial protein C receptor (EPCR) via the multi-domain P. falciparum erythrocyte membrane protein 1 (PfEMP1) adhesion ligands. Using cryogenic electron microscopy (Cryo-EM) and PfEMP1 sequence diversity analysis, we found that group A PfEMP1 CIDRα1 domains interact with the adjacent DBLα1 domain through central, conserved residues of the EPCR-binding site to adopt a compact conformation. Upon EPCR binding, the DBLα1 domain is displaced, and the EPCR-binding helix of CIDRα1 is turned, kinked, and twisted to reach a rearranged, stable EPCR-bound conformation. The unbound conformation and the required transition to the EPCR-bound conformation may represent a conformational masking mechanism of immune evasion for the PfEMP1 family.

U2 - 10.1016/j.str.2023.07.011

DO - 10.1016/j.str.2023.07.011

M3 - Journal article

C2 - 37582356

AN - SCOPUS:85172200717

VL - 31

SP - 1174-1183.e4

JO - Structure

JF - Structure

SN - 0969-2126

IS - 10

ER -

ID: 370487236