No sweet deal - Resultat

No sweet deal: the antibody-mediated immune response to malaria

Publikation: Bidrag til tidsskrift › Review › fagfællebedømt

Standard

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

I: Trends in Parasitology, Bind 38, Nr. 6, 2022, s. 428-434.

Publikation: Bidrag til tidsskrift › Review › fagfællebedømt

Harvard

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

APA

Hviid, L., Lopez-Perez, M., Larsen, M. D., & Vidarsson, G. (2022). No sweet deal: the antibody-mediated immune response to malaria. Trends in Parasitology, 38(6), 428-434. https://doi.org/10.1016/j.pt.2022.02.008

Vancouver

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

Author

Hviid, Lars ; Lopez-Perez, Mary ; Larsen, Mads Delbo ; Vidarsson, Gestur. / No sweet deal : the antibody-mediated immune response to malaria. I: Trends in Parasitology. 2022 ; Bind 38, Nr. 6. s. 428-434.

Bibtex

@article{fb5d4edf5b61466cabd2e8135a624530,

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 = "acquired immunity, antibody effector function, Fc region, Fcγ receptors, fucosylation, Plasmodium falciparum malaria",

author = "Lars Hviid and Mary Lopez-Perez and Larsen, {Mads Delbo} and Gestur Vidarsson",

note = "Publisher Copyright: {\textcopyright} 2022 Elsevier Ltd",

year = "2022",

doi = "10.1016/j.pt.2022.02.008",

language = "English",

volume = "38",

pages = "428--434",

journal = "Trends in Parasitology",

issn = "1471-4922",

publisher = "Elsevier Ltd. * Trends Journals",

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

PY - 2022

Y1 - 2022

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 - acquired immunity

KW - antibody effector function

KW - Fc region

KW - Fcγ receptors

KW - fucosylation

KW - Plasmodium falciparum malaria

U2 - 10.1016/j.pt.2022.02.008

DO - 10.1016/j.pt.2022.02.008

M3 - Review

C2 - 35279381

AN - SCOPUS:85126087569

VL - 38

SP - 428

EP - 434

JO - Trends in Parasitology

JF - Trends in Parasitology

SN - 1471-4922

IS - 6

ER -

ID: 305715662

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