Plasmodium falciparum-CD36 structure-function relationships defined by ortholog scanning mutagenesis

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

Standard

Plasmodium falciparum-CD36 structure-function relationships defined by ortholog scanning mutagenesis. / Cabrera, Ana; Neculai, Dante; Tran, Vanessa; Lavstsen, Thomas; Turner, Louise; Kain, Kevin C.

In: The Journal of Infectious Diseases, Vol. 219, No. 6, 2019, p. 945-954.

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

Harvard

Cabrera, A, Neculai, D, Tran, V, Lavstsen, T, Turner, L & Kain, KC 2019, 'Plasmodium falciparum-CD36 structure-function relationships defined by ortholog scanning mutagenesis', The Journal of Infectious Diseases, vol. 219, no. 6, pp. 945-954. https://doi.org/10.1093/infdis/jiy607

APA

Cabrera, A., Neculai, D., Tran, V., Lavstsen, T., Turner, L., & Kain, K. C. (2019). Plasmodium falciparum-CD36 structure-function relationships defined by ortholog scanning mutagenesis. The Journal of Infectious Diseases, 219(6), 945-954. https://doi.org/10.1093/infdis/jiy607

Vancouver

Cabrera A, Neculai D, Tran V, Lavstsen T, Turner L, Kain KC. Plasmodium falciparum-CD36 structure-function relationships defined by ortholog scanning mutagenesis. The Journal of Infectious Diseases. 2019;219(6):945-954. https://doi.org/10.1093/infdis/jiy607

Author

Cabrera, Ana ; Neculai, Dante ; Tran, Vanessa ; Lavstsen, Thomas ; Turner, Louise ; Kain, Kevin C. / Plasmodium falciparum-CD36 structure-function relationships defined by ortholog scanning mutagenesis. In: The Journal of Infectious Diseases. 2019 ; Vol. 219, No. 6. pp. 945-954.

Bibtex

@article{0f1ecdab0e4f4cce8672dfa57e4dfca2,
title = "Plasmodium falciparum-CD36 structure-function relationships defined by ortholog scanning mutagenesis",
abstract = "BACKGROUND: The interaction of Plasmodium falciparum-infected erythrocytes (IEs) with the host receptor CD36 is among the most studied host-parasite interfaces. CD36 is a scavenger receptor that binds numerous ligands including the cysteine-rich interdomain region (CIDR)α domains of the erythrocyte membrane protein 1 family (PfEMP1) expressed on the surface of IEs. CD36 is conserved across species, but orthologs display differential binding of IEs.METHODS: In this study, we exploited these differences, combined with the recent crystal structure and 3-dimensional modeling of CD36, to investigate malaria-CD36 structure-function relationships and further define IE-CD36 binding interactions.RESULTS: We show that a charged surface in the membrane-distal region of CD36 is necessary for IE binding. Moreover, IE interaction with this binding surface is influenced by additional CD36 domains, both proximal to and at a distance from this site.CONCLUSIONS: Our data indicate that subtle sequence and spatial differences in these domains modify receptor conformation and regulate the ability of CD36 to selectively interact with its diverse ligands.",
author = "Ana Cabrera and Dante Neculai and Vanessa Tran and Thomas Lavstsen and Louise Turner and Kain, {Kevin C}",
note = "{\textcopyright} The Author(s) 2018. Published by Oxford University Press for the Infectious Diseases Society of America. All rights reserved. For permissions, e-mail: journals.permissions@oup.com.",
year = "2019",
doi = "10.1093/infdis/jiy607",
language = "English",
volume = "219",
pages = "945--954",
journal = "Journal of Infectious Diseases",
issn = "0022-1899",
publisher = "Oxford University Press",
number = "6",

}

RIS

TY - JOUR

T1 - Plasmodium falciparum-CD36 structure-function relationships defined by ortholog scanning mutagenesis

AU - Cabrera, Ana

AU - Neculai, Dante

AU - Tran, Vanessa

AU - Lavstsen, Thomas

AU - Turner, Louise

AU - Kain, Kevin C

N1 - © The Author(s) 2018. Published by Oxford University Press for the Infectious Diseases Society of America. All rights reserved. For permissions, e-mail: journals.permissions@oup.com.

PY - 2019

Y1 - 2019

N2 - BACKGROUND: The interaction of Plasmodium falciparum-infected erythrocytes (IEs) with the host receptor CD36 is among the most studied host-parasite interfaces. CD36 is a scavenger receptor that binds numerous ligands including the cysteine-rich interdomain region (CIDR)α domains of the erythrocyte membrane protein 1 family (PfEMP1) expressed on the surface of IEs. CD36 is conserved across species, but orthologs display differential binding of IEs.METHODS: In this study, we exploited these differences, combined with the recent crystal structure and 3-dimensional modeling of CD36, to investigate malaria-CD36 structure-function relationships and further define IE-CD36 binding interactions.RESULTS: We show that a charged surface in the membrane-distal region of CD36 is necessary for IE binding. Moreover, IE interaction with this binding surface is influenced by additional CD36 domains, both proximal to and at a distance from this site.CONCLUSIONS: Our data indicate that subtle sequence and spatial differences in these domains modify receptor conformation and regulate the ability of CD36 to selectively interact with its diverse ligands.

AB - BACKGROUND: The interaction of Plasmodium falciparum-infected erythrocytes (IEs) with the host receptor CD36 is among the most studied host-parasite interfaces. CD36 is a scavenger receptor that binds numerous ligands including the cysteine-rich interdomain region (CIDR)α domains of the erythrocyte membrane protein 1 family (PfEMP1) expressed on the surface of IEs. CD36 is conserved across species, but orthologs display differential binding of IEs.METHODS: In this study, we exploited these differences, combined with the recent crystal structure and 3-dimensional modeling of CD36, to investigate malaria-CD36 structure-function relationships and further define IE-CD36 binding interactions.RESULTS: We show that a charged surface in the membrane-distal region of CD36 is necessary for IE binding. Moreover, IE interaction with this binding surface is influenced by additional CD36 domains, both proximal to and at a distance from this site.CONCLUSIONS: Our data indicate that subtle sequence and spatial differences in these domains modify receptor conformation and regulate the ability of CD36 to selectively interact with its diverse ligands.

U2 - 10.1093/infdis/jiy607

DO - 10.1093/infdis/jiy607

M3 - Journal article

C2 - 30335152

VL - 219

SP - 945

EP - 954

JO - Journal of Infectious Diseases

JF - Journal of Infectious Diseases

SN - 0022-1899

IS - 6

ER -

ID: 213826887