Class II-restricted IgG2ab-specific T cells recognize a signal-minus form of the V-CH3b antigen.

Abstract:

:To study the question when and where self peptides become associated with major histocompatibility complex class II molecules for tolerance induction, we recently developed a system in which the intracellular site(s) of antigen expression could be manipulated using gene cloning techniques. We previously constructed a truncated IgGa gene comprising a variable (V) domain and the CH3 domain (not including the membrane exons) from the IgG2ab heavy (H) chain. The secreted form of the V-CH3b protein was expressed at high levels under control of the Ig H chain enhancer in Ia+ B lymphoma cells and was efficiently recognized by class II-restricted IgG2ab-specific T cell hybrids. Here we describe a modified V-CH3b gene construct in which the sequences encoding the signal peptide were deleted. A strong argument can be made that the signal-less V-CH3b protein is predominantly expressed in the cytosol. We show that transfected L cell lines expressing the signal-less form of the V-CH3b protein can stimulate class II-restricted IgG2ab-specific T cells. Cell mixing experiments indicate that this response cannot be due to passive uptake of soluble antigenic peptides released into culture supernatants. These experiments demonstrate that a cytoplasmic protein having no obvious means of reaching the cell surface can be presented to class II-restricted T cells.

journal_name

Eur J Immunol

authors

Bikoff EK

doi

10.1002/eji.1830210613

subject

Has Abstract

pub_date

1991-06-01 00:00:00

pages

1411-7

issue

6

eissn

0014-2980

issn

1521-4141

journal_volume

21

pub_type

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