International Immunology, Vol 9, 805-813, Copyright © 1997 by Oxford University Press
P Rennert, K Furlong, C Jellis, E Greenfield, GJ Freeman, Y Ueda, B Levine, CH June and GS Gray
B7-1 (CD80) and B7-2 (CD86) are genetically and structurally related
molecules expressed on antigen-presenting cells. Both bind CD28 to co-
stimulate T lymphocytes, resulting in proliferation and cytokine
production. The extracellular portions of B7-1 and B7-2 which bind to CD28
and CTLA-4 are related to Ig variable (V) and Ig constant (C) domain
sequences. Recent reports have described splice variant forms of B7
proteins which occur in vivo and are of unknown function. Here we describe
soluble recombinant forms of B7-1 and B7-2 containing either both of the
Ig-like extracellular domains or the individual IgV or IgC domains coupled
to an Ig Fc tail. Soluble B7-1 and B7-2 bind to CD28 and CTLA-4, and
effectively co-stimulate T lymphocytes resulting in their proliferation and
the secretion of cytokines. Furthermore, the IgV domain of B7-2 binds CD28
and CTLA-4, competes with B7-1 and B7-2 for binding to these receptors, and
co-stimulates T lymphocytes. Cross- linked soluble B7-2v was the most
potent co-stimulatory molecule tested and was active at a concentration
approximately 100-fold lower than cross-linked soluble B7-1 or B7-2
proteins. When bound to tosyl- activated beads, B7-2v was capable of
sustaining multiple rounds of T cell expansion. These data complement the
description of naturally occurring variants to suggest that T cell
co-stimulation in vivo may be regulated by soluble or truncated forms of B7
proteins.
ARTICLES
The IgV domain of human B7-2 (CD86) is sufficient to co-stimulate T lymphocytes and induce cytokine secretion
Department of Molecular Biology, Repligen Corp., Cambridge, MA 02139, USA.
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