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1.
Front Immunol ; 15: 1359494, 2024.
Article in English | MEDLINE | ID: mdl-38947328

ABSTRACT

Sialic acids are found as terminal sugars on glycan structures on cellular surfaces. T cells carry these sialoglycans abundantly, and they are thought to serve multiple functions in cell adhesion, cell migration, and protection from complement attack. We studied the role of sialoglycans on T cells in a mouse model with a T cell-specific deletion of cytidine monophosphate-sialic acid synthase (CMAS), the enzyme that is crucial for the synthesis of sialoglycans. These mice showed a T-cell deficiency in peripheral lymphoid organs. Many T cells with an undeleted Cmas allele were found in the periphery, suggesting that they escaped the Cre-mediated deletion. The remaining peripheral T cells of T cell-specific Cmas KO mice had a memory-like phenotype. Additional depletion of the complement factor C3 could not rescue the phenotype, showing that the T-cell defect was not caused by a host complement activity. Cmas-deficient T cells showed a high level of activated caspase 3, indicating an ongoing apoptosis. In bone marrow chimeric cellular transfer experiments, we observed a strong competitive disadvantage of Cmas-deficient T cells compared to wild-type T cells. These results show that sialoglycans on the surface of T cells are crucial for T-cell survival and maintenance. This function has not been recognized before and is similar to the function of sialoglycans on B cells.


Subject(s)
Mice, Knockout , Sialic Acids , T-Lymphocytes , Animals , Mice , T-Lymphocytes/immunology , T-Lymphocytes/metabolism , Sialic Acids/metabolism , Cell Survival , Mice, Inbred C57BL , Apoptosis , Complement C3/metabolism , Complement C3/immunology , Complement C3/genetics , Mixed Function Oxygenases
2.
Front Immunol ; 15: 1402000, 2024.
Article in English | MEDLINE | ID: mdl-38827747

ABSTRACT

Sialic acids as terminal sugar residues on cell surface or secreted proteins have many functional roles. In particular, the presence or absence of α2,6-linked sialic acid residues at the immunoglobulin G (IgG) Fc fragment can switch IgG effector functions from pro- to anti-inflammatory activity. IgG glycosylation is considered to take place inside the plasma blast/plasma cell while the molecule travels through the endoplasmic reticulum and Golgi apparatus before being secreted. However, more recent studies have suggested that IgG sialylation may occur predominantly post-antibody secretion. To what extent this extracellular IgG sialylation process contributes to overall IgG sialylation remains unclear, however. By generating bone marrow chimeric mice with a B cell-specific deletion of ST6Gal1, the key enzyme required for IgG sialylation, we now show that sialylation of the IgG Fc fragment exclusively occurs within B cells pre-IgG secretion. We further demonstrate that B cells expressing ST6Gal1 have a developmental advantage over B cells lacking ST6Gal1 expression and thus dominate the plasma cell pool and the resulting serum IgG population in mouse models in which both ST6Gal1-sufficient and -deficient B cells are present.


Subject(s)
B-Lymphocytes , Immunoglobulin G , Sialyltransferases , Animals , Immunoglobulin G/immunology , Immunoglobulin G/metabolism , Mice , Sialyltransferases/metabolism , Sialyltransferases/genetics , B-Lymphocytes/immunology , B-Lymphocytes/metabolism , Mice, Knockout , Glycosylation , Mice, Inbred C57BL , Immunoglobulin Fc Fragments/immunology , Immunoglobulin Fc Fragments/metabolism , Immunoglobulin Fc Fragments/genetics , beta-D-Galactoside alpha 2-6-Sialyltransferase , Plasma Cells/immunology , Plasma Cells/metabolism , Antibody Formation
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