Immunosuppression in Vivo by a Soluble Form of the CTLA-4 T Cell Activation Molecule
Peter S. Linsley(Bristol-Myers Squibb (United States)), Philip M. Wallace(Bristol-Myers Squibb (United States)), Jennifer Johnson(Bristol-Myers Squibb (United States)), Marylou G. Gibson(Bristol-Myers Squibb (United States)), JoAnne L. Greene(Bristol-Myers Squibb (United States)), Jeffrey A. Ledbetter(Bristol-Myers Squibb (United States)), Cherry Singh(Bristol-Myers Squibb (United States)), Mark A. Tepper(Bristol-Myers Squibb (United States))
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Abstract
In vitro, when the B7 molecule on the surface of antigen-presenting cells binds to the T cell surface molecules CD28 and CTLA-4, a costimulatory signal for T cell activation is generated. CTLA4Ig is a soluble form of the extracellular domain of CTLA-4 and binds B7 with high avidity. CTLA4Ig treatment in vivo suppressed T cell-dependent antibody responses to sheep erythrocytes or keyhole limpet hemocyanin. Large doses of CTLA4Ig suppressed responses to a second immunization. Thus, costimulation by B7 is important for humoral immune responses in vivo, and interference with costimulation may be useful for treatment of antibody-mediated autoimmune disease.
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