Interactions Between Two Antigens Governed by the Poly-L-lysine Gene: Failure of One to Inhibit Competitively an in Vitro Response to the Other

Dunham, Edward K.; Schlossman, Stuart F.; Benacerraf, Baruj

doi:10.3181/00379727-145-37847

Cited by 1 publication

(2 citation statements)

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“…Current information on the extent of T cell cross-reactivity presents a paradox; there is evidence that T cells are broadly cross-reactive (1)(2)(3)(4), but other data show narrow specificities (5)(6)(7)(8)(9)(10)(11). The balance achieved between these opposing characteristics is particularly pertinent to antiviral immunity, where antigenic variation may result in poor T cell recognition and profoundly affect the outcome of an infection (12).…”

Section: Introductionmentioning

confidence: 99%

“…In some cases, the antigens were closely related to self (5)(6)(7), so tolerance to the self epitopes might have preselected T cells that react to only very limited epitope variants. Similarly, T cells responding to peptide immunogens (8) could show restricted specificity because the antigen is suboptimal. However, three studies of human CD8 ϩ T cell responses to natural viral antigens (9)(10)(11) show that immunodominant CD8 ϩ T cells are finely restricted in epitope specificity.…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

T Cell Cross-Reactivity and Conformational Changes during TCR Engagement

Lee

Stewart-Jones

Dong

et al. 2004

The Journal of Experimental Medicine

149

141

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All thymically selected T cells are inherently cross-reactive, yet many data indicate a fine specificity in antigen recognition, which enables virus escape from immune control by mutation in infections such as the human immunodeficiency virus (HIV). To address this paradox, we analyzed the fine specificity of T cells recognizing a human histocompatibility leukocyte antigen (HLA)-A2-restricted, strongly immunodominant, HIV gag epitope (SLFNTVATL). The majority of 171 variant peptides tested bound HLA-A2, but only one third were recognized. Surprisingly, one recognized variant (SLYNTVATL) showed marked differences in structure when bound to HLA-A2. T cell receptor (TCR) recognition of variants of these two peptides implied that they adopted the same conformation in the TCR-peptide-major histocompatibility complex (MHC) complex. However, the on-rate kinetics of TCR binding were identical, implying that conformational changes at the TCR-peptide-MHC binding interface occur after an initial permissive antigen contact. These findings have implications for the rational design of vaccines targeting viruses with unstable genomes.

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