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No sweet deal : the antibody-mediated immune response to malaria. / Hviid, Lars; Lopez-Perez, Mary; Larsen, Mads Delbo et al.

In: Trends in parasitology, Vol. 38, No. 6, 06.2022, p. 428-434.

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Harvard

Hviid, L, Lopez-Perez, M, Larsen, MD & Vidarsson, G 2022, 'No sweet deal: the antibody-mediated immune response to malaria', Trends in parasitology, vol. 38, no. 6, pp. 428-434. https://doi.org/10.1016/j.pt.2022.02.008

APA

Vancouver

Hviid L, Lopez-Perez M, Larsen MD, Vidarsson G. No sweet deal: the antibody-mediated immune response to malaria. Trends in parasitology. 2022 Jun;38(6):428-434. Epub 2022. doi: 10.1016/j.pt.2022.02.008

Author

Hviid, Lars ; Lopez-Perez, Mary ; Larsen, Mads Delbo et al. / No sweet deal : the antibody-mediated immune response to malaria. In: Trends in parasitology. 2022 ; Vol. 38, No. 6. pp. 428-434.

BibTeX

@article{b1df8c0b7e394ba98c13b64d2653ac64,
title = "No sweet deal: the antibody-mediated immune response to malaria",
abstract = "IgG antibodies are key effector molecules in acquired immunity to Plasmodium falciparum malaria, and the PfEMP1 adhesins expressed on the surface of the infected erythrocytes are crucial immunological targets. The antigen specificity of these antibodies has therefore been a major research focus. However, we recently reported that the Fc domain of naturally induced PfEMP1-specific IgG1 is selectively modified by post-translational omission of fucose from the conserved Fc glycan. The resulting afucosylated IgG has increased affinity for the IgG-Fc-receptor III family (FcγRIII), found on natural killer cells and on subsets of other cells in the immune system. We discuss the implications of these findings for the basic understanding of antimalarial immunity and for the design of improved vaccines against the disease.",
keywords = "Fc region, Fcγ receptors, Plasmodium falciparum malaria, acquired immunity, antibody effector function, fucosylation",
author = "Lars Hviid and Mary Lopez-Perez and Larsen, {Mads Delbo} and Gestur Vidarsson",
note = "Funding Information: The work in the authors{\textquoteright} laboratories discussed in this article is supported by the Danish International Development Agency [grants 17-02-KU and BSU3-UG ] (L.H.), Danish Medical Research Council [grant 013400123B ] (M.L.P. and L.H.), and Landsteiner Foundation for Blood Transfusion Research (LSBR) [grant 1721 ] (G.V.). Publisher Copyright: {\textcopyright} 2022 Elsevier Ltd",
year = "2022",
month = jun,
doi = "10.1016/j.pt.2022.02.008",
language = "English",
volume = "38",
pages = "428--434",
journal = "Trends in parasitology",
issn = "1471-4922",
publisher = "Elsevier Limited",
number = "6",

}

RIS

TY - JOUR

T1 - No sweet deal

T2 - the antibody-mediated immune response to malaria

AU - Hviid, Lars

AU - Lopez-Perez, Mary

AU - Larsen, Mads Delbo

AU - Vidarsson, Gestur

N1 - Funding Information: The work in the authors’ laboratories discussed in this article is supported by the Danish International Development Agency [grants 17-02-KU and BSU3-UG ] (L.H.), Danish Medical Research Council [grant 013400123B ] (M.L.P. and L.H.), and Landsteiner Foundation for Blood Transfusion Research (LSBR) [grant 1721 ] (G.V.). Publisher Copyright: © 2022 Elsevier Ltd

PY - 2022/6

Y1 - 2022/6

N2 - IgG antibodies are key effector molecules in acquired immunity to Plasmodium falciparum malaria, and the PfEMP1 adhesins expressed on the surface of the infected erythrocytes are crucial immunological targets. The antigen specificity of these antibodies has therefore been a major research focus. However, we recently reported that the Fc domain of naturally induced PfEMP1-specific IgG1 is selectively modified by post-translational omission of fucose from the conserved Fc glycan. The resulting afucosylated IgG has increased affinity for the IgG-Fc-receptor III family (FcγRIII), found on natural killer cells and on subsets of other cells in the immune system. We discuss the implications of these findings for the basic understanding of antimalarial immunity and for the design of improved vaccines against the disease.

AB - IgG antibodies are key effector molecules in acquired immunity to Plasmodium falciparum malaria, and the PfEMP1 adhesins expressed on the surface of the infected erythrocytes are crucial immunological targets. The antigen specificity of these antibodies has therefore been a major research focus. However, we recently reported that the Fc domain of naturally induced PfEMP1-specific IgG1 is selectively modified by post-translational omission of fucose from the conserved Fc glycan. The resulting afucosylated IgG has increased affinity for the IgG-Fc-receptor III family (FcγRIII), found on natural killer cells and on subsets of other cells in the immune system. We discuss the implications of these findings for the basic understanding of antimalarial immunity and for the design of improved vaccines against the disease.

KW - Fc region

KW - Fcγ receptors

KW - Plasmodium falciparum malaria

KW - acquired immunity

KW - antibody effector function

KW - fucosylation

UR - http://www.scopus.com/inward/record.url?scp=85126087569&partnerID=8YFLogxK

U2 - 10.1016/j.pt.2022.02.008

DO - 10.1016/j.pt.2022.02.008

M3 - Review article

C2 - 35279381

VL - 38

SP - 428

EP - 434

JO - Trends in parasitology

JF - Trends in parasitology

SN - 1471-4922

IS - 6

ER -

ID: 22154752