The Journal of Experimental Medicine
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J. Exp. Med.
© The Rockefeller University Press
0022-1007/96/12/2439/06 $2.00
Volume 184 December 1996 2439-2444

BRIEF DEFINITIVE REPORT:
CD8beta Increases CD8 Coreceptor Function and Participation in TCR-Ligand Binding

By Valery Renard,* Pedro Romero,Dagger Eric Vivier,* Bernard Malissen,* and Immanuel F. LuescherDagger

From the * Centre d'Immunologie Institut National de la Santé et de la Recherche Médicale, Centre National de la Recherche Scientifique de Marseille-Luminy, Case 906, 13288 Marseille, Cedex 09, France; and Dagger  Ludwig Institute for Cancer Research, Lausanne Branch, University of Lausanne, 1066 Epalinges, Switzerland

To study the role of CD8beta in T cell function, we derived a CD8alpha /beta - (CD8-/-) T cell hybridoma of the H-2Kd-restricted N9 cytotoxic T lymphocyte clone specific for a photoreactive derivative of the Plasmodium berghei circumsporozoite peptide PbCS 252-260. This hybridoma was transfected either with CD8alpha alone or together with CD8beta . All three hybridomas released interleukin 2 upon incubation with L cells expressing Kd-peptide derivative complexes, though CD8alpha /beta cells did so more efficiently than CD8alpha /alpha and especially CD8-/- cells. More strikingly, only CD8alpha /beta cells were able to recognize a weak agonist peptide derivative variant. This recognition was abolished by Fab' fragments of the anti-Kd alpha 3 monoclonal antibody SF11.1.1 or substitution of Kd D-227 with K, both conditions known to impair CD8 coreceptor function. T cell receptor (TCR) photoaffinity labeling indicated that TCR-ligand binding on CD8alpha /beta cells was ~5- and 20-fold more avid than on CD8alpha /a and CD8-/- cells, respectively. SF1-1.1.1 Fab' or Kd mutation D227K reduced the TCR photoaffinity labeling on CD8alpha /beta cells to approximately the same low levels observed on CD8-/- cells. These results indicate that CD8alpha /beta is a more efficient coreceptor than CD8alpha /alpha , because it more avidly strengthens TCR-ligand binding.


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