Rook G A, Steele J, Rademacher T
Department of Medical Microbiology, University College, London.
Ann Rheum Dis. 1988 Mar;47(3):247-50. doi: 10.1136/ard.47.3.247.
It was shown recently that the IgG of patients with rheumatoid arthritis tends to lack the terminal galactose normally present on the conserved N-linked oligosaccharide situated on the CH2 domain. This results in the exposure of a terminal N-acetylglucosamine linked beta 1-2 to mannose. It is reported here that mice immunised with the peptidoglycan/polysaccharide complex of group A streptococci can be used as a source of monoclonal antibodies binding to this epitope. It may be significant that the organism responsible for rheumatic fever evokes antibodies binding to an abnormality of IgG found in rheumatoid arthritis.
最近研究表明,类风湿性关节炎患者的IgG往往缺少正常情况下存在于CH2结构域保守N - 连接寡糖上的末端半乳糖。这导致一个与甘露糖以β 1 - 2连接的末端N - 乙酰葡糖胺暴露出来。本文报道,用A组链球菌的肽聚糖/多糖复合物免疫的小鼠可作为结合该表位的单克隆抗体的来源。风湿热的致病生物体诱发与类风湿性关节炎中发现的IgG异常相结合的抗体,这可能具有重要意义。