A common idiotope on human rheumatoid factors identified by a hybridoma antibody.
A common idiotope on human rheumatoid factors identified by a hybridoma antibody.
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由杂交瘤抗体鉴定出的人类类风湿因子的常见独特位。
DOI:
10.1016/0161-5890(83)90116-5
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发表时间:
1983
影响因子:
3.6
通讯作者:
Fong,S
中科院分区:
文献类型:
--
作者:
Carson,DA;Fong,S
Human monoclonal and polyclonal anti-IgG autoantibodies [rheumatoid factors (RFs)] are composed primarily of kappa light chains, and may display cross-reactive idiotypes. However, the nature of the shared idiotope (s) has remained unclear. We have prepared a murine hybridoma antibody (17–109) that recognizes an idiotope present on 30%(3 10) of human IgM-RF paraproteins, and absent on immunoglobulins without RF activity. The idiotope was measurable on isolated, intact kappa light chains, but not on light-chain tryptic peptides, nor on isolated heavy chains. A comparison of the binding to 17–109 of five IgM-RF paraproteins, with known kappa chain amino acid sequences, suggested a relationship between the idiotope recognized by the hybridoma and the complementarity-determining regions. The serum of patients with rheumatoid arthritis contained idiotope positive material that bound specifically to a 17–109 immunoadsorbent column. Moreover, the 17–109 anti-idiotope antibody partially inhibited the binding to IgG of IgM-RF and IgA-RF in serum, but did not effect the binding to antigen of IgM and IgA anti-tetanus toxoid antibodies. These results suggest that a significant proportion of IgM-RF paraproteins share an idiotope located at or near the complementarity-determining regions of the kappa light chain. Human serum RFs include a kappa light chain family that is idiotopically related to the kappa chains on IgM-RF paraproteins.