RETRACTED: Naturally occurring human IgM antibody that binds B7-DC and potentiates T cell stimulation by dendritic cells (Retracted article. See vol. 184, pg. 6552, 2010)

被引:50
作者
Radhakrishnan, S
Nguyen, LT
Ciric, B
Ure, DR
Zhou, B
Tamada, K
Dong, H
Tseng, SY
Shin, T
Pardoll, DM
Chen, LP
Kyle, RA
Rodriguez, M
Pease, LR
机构
[1] Mayo Clin & Mayo Grad Sch Med, Dept Immunol, Rochester, MN 55905 USA
[2] Mayo Clin & Mayo Grad Sch Med, Dept Neurol, Rochester, MN 55905 USA
[3] Mayo Clin & Mayo Grad Sch Med, Dept Internal Med, Rochester, MN 55905 USA
[4] Johns Hopkins Univ, Sch Med, Dept Oncol, Baltimore, MD 21205 USA
关键词
D O I
10.4049/jimmunol.170.4.1830
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
A human IgM Ab, serum-derived human IgM 12 (sHIgM12), is identified that binds mouse and human dendritic cells (DC), inducing dramatic immunopotentiation following treatment of the mouse DC in vitro. Competition, transfection, and knockout studies identified the ligand on mouse DC as the costimulatory molecule family member B7-DC. Potent T cell responses are stimulated by Ag-pulsed DC treated with the sHIgM12 Ab in vitro and upon adoptive transfer of Ab-treated Ag-pulsed DC into animals. The multivalent structure of pentameric IgM provides the potential for cross-linking cell surface targets, endowing the soluble Abs with biological potential not normally associated with immune, function. The ability of the sHIgM12 Ab to potentiate the immune response is dependent on the multimeric structure of IgM, as bivalent monomers do not retain this property. Furthermore, pretreatment of DC with IgM monomers blocks subsequent potentiation by intact IgM pentamers, an indication that cross-linking of B7-DC on the cell surface is critical for potentiation of Ag presentation. These findings imply that, in addition to known costimulatory roles, B7-DC can function as a receptor for signals delivered by cells expressing B7-DC ligands.
引用
收藏
页码:1830 / 1838
页数:9
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