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Immunosuppression in Vivo by a Soluble Form of the CTLA-4 T Cell Activation Molecule

Peter S. Linsley, Philip M. Wallace, Jennifer Johnson, Marylou G. Gibson, JoAnne L. Greene, Jeffrey A. Ledbetter, Cherry Singh and Mark A. Tepper
Science
New Series, Vol. 257, No. 5071 (Aug. 7, 1992), pp. 792-795
Stable URL: http://www.jstor.org/stable/2877673
Page Count: 4
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Immunosuppression in Vivo by a Soluble Form of the CTLA-4 T Cell Activation Molecule
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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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