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

Ohmi, Yuhsuke  ,  Ise, Wataru  ,  Harazono, Akira  ,  Takakura, Daisuke  ,  Fukuyama, Hidehiro  ,  Baba, Yoshihiro  ,  Narazaki, Masashi  ,  Shoda, Hirofumi  ,  Takahashi, Nobunori  ,  Ohkawa, Yuki  ,  Ji, Shuting  ,  Sugiyama, Fumihiro  ,  Fujio, Keishi  ,  Kumanogoh, Atsushi  ,  Yamamoto, Kazuhiko  ,  Kawasaki, Nana  ,  Kurosaki, Tomohiro  ,  Takahashi, Yoshimasa  ,  Furukawa, Koichi

7p.11205 , 2016-01 , Nature Publishing Group
ISSN:2041-1723
Description
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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