| First Author | Ohmi Y | Year | 2016 |
| Journal | Nat Commun | Volume | 7 |
| Pages | 11205 | PubMed ID | 27046227 |
| Mgi Jnum | J:236903 | Mgi Id | MGI:5810059 |
| Doi | 10.1038/ncomms11205 | Citation | Ohmi Y, et al. (2016) Sialylation converts arthritogenic IgG into inhibitors of collagen-induced arthritis. Nat Commun 7:11205 |
| abstractText | 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. |
