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.
Originalsprog | Engelsk |
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Tidsskrift | Trends in Parasitology |
Vol/bind | 38 |
Udgave nummer | 6 |
Sider (fra-til) | 428-434 |
ISSN | 1471-4922 |
DOI | |
Status | Udgivet - 2022 |
Bibliografisk note
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.).
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