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Sialylation converts arthritogenic IgG into inhibitors of collagen-induced arthritis.

Article scientifique 2016 Anglais

Résumé

Rheumatoid arthritis (RA)-associated IgG antibodies such as anti-citrullinated protein antibodies (ACPAs) have diverse glycosylation variants; however, key sugar chains modulating the arthritogenic activity of IgG remain to be clarified.Here, we show that reduced sialylation is a common feature of RA-associated IgG in humans and in mouse models of arthritis.Genetically blocking sialylation in activated B cells results in exacerbation of joint inflammation in a collagen-induced arthritis (CIA) model.On the other hand, artificial sialylation of anti-type II collagen antibodies, including ACPAs, not only attenuates arthritogenic activity, but also suppresses the development of CIA in the antibody-infused mice, whereas sialylation of other IgG does not prevent CIA.Thus, our data demonstrate that sialylation levels control the arthritogenicity of RA-associated IgG, presenting a potential target for antigen-specific immunotherapy.

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Import, S. (2016). Sialylation converts arthritogenic IgG into inhibitors of collagen-induced arthritis..

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