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International Immunology, Vol. 12, No. 11, 1579-1591, November 2000
© 2000 Japanese Society for Immunology

Identification of a novel pre-TCR isoform in which the accessibility of the TCRß subunit is determined by occupancy of the `missing' V domain of pre-T{alpha}

Marc A. Berger1,5, Michael Carleton1, Michele Rhodes1, J. Michael Sauder2, Sébastien Trop3, Roland L. Dunbrack2, Patrice Hugo4 and David L. Wiest1

1 Immunobiology Working Group, and
2 Biomolecular Structure and Function Working Group, Fox Chase Cancer Center, Philadelphia, PA 19111, USA
3 Department of Medicine, Division of Experimental Medicine, McGill University, Montréal, Québec H3A 1A3, Canada
4 PROCREA BioSciences, Inc., Montreal, Québec H4P 2R2, Canada

Correspondence to: D. L. Wiest

We have identified a novel pre-TCR isoform that is structurally distinct from conventional pre-TCR complexes and whose TCRß chains are inaccessible to anti-TCRß antibodies. We term this pre-TCR isoform the MB (masked ß)-pre-TCR. Pre-T{alpha} (pT{alpha}) subunits of MB-pre-TCR complexes have a larger apparent mol. wt due to extensive modification with O-linked carbohydrates; however, preventing addition of O-glycans does not restore antibody recognition of the TCRß subunits of MB-pre-TCR complexes. Importantly, accessibility of TCRß chains in MB-pre-TCR complexes is restored by filling in the `missing' variable (V) domain of pT{alpha} with a V domain from TCR{alpha}. Moreover, the proportion of pre-TCR complexes in which the TCRß subunits are accessible to anti-TCRß antibody varies with the cellular context, suggesting that TCRß accessibility is controlled by a trans-acting factor. The way in which this factor might control TCRß accessibility as well as the physiologic relevance of TCRß masking for pre-TCR function are discussed.

Keywords: pre-TCR, pT{alpha}, structural model, thymocyte development, Vpre-T

Transmitting editor: A. Singer

5 Present address: Purdue BioPharma, LP, 201 College Road East, Princeton, NJ 08540, USA


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