Sialylation converts arthritogenic IgG into inhibitors of collagen-induced arthritis

• Published in: Nature Communications Vol. 7; no. 7; p. 11205
• Main Authors: 杉山 文博, 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
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group 05.04.2016; Nature Publishing Group UK; Nature Portfolio
• Subjects: 631/250/249/1313/498; 631/250/251; 64; 64/110; 64/60; 692/308; 692/420/2780; 82; 82/1; 82/51; 82/58; 82/83; Amino Acid Sequence; Animals; Arthritis, Experimental - immunology; Arthritis, Experimental - metabolism; Arthritis, Experimental - pathology; Arthritis, Rheumatoid - immunology; Arthritis, Rheumatoid - metabolism; Arthritis, Rheumatoid - pathology; Autoantibodies - chemistry; Autoantibodies - immunology; Autoantibodies - metabolism; Carbohydrate Sequence; Collagen Type II - immunology; Collagen Type II - metabolism; Humanities and Social Sciences; Humans; Immunoglobulin G - chemistry; Immunoglobulin G - immunology; Immunoglobulin G - metabolism; Immunotherapy; Mice; Mice, Inbred C57BL; Mice, Inbred DBA; Mice, Transgenic; Molecular Sequence Data; multidisciplinary; Protein Processing, Post-Translational; Rheumatoid arthritis; Science; Science (multidisciplinary); Sialic Acids - immunology; Sialic Acids - metabolism

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...