Abstract
Recent structure-function studies of ours and others indicating that regions of the TCR other than Vβ are involved in the TCR-superantigen (SAg)-MHC class II trimolecular interaction were correlative; thus, while the conclusions were persuasive, they were not unequivocal. The transfecfion experiments described in this report show that 1) responsiveness to staphylococcal enterotoxin B in Vβ6 T cells was transferred by a Vα4- but not by Vα8- and Vα10-containing α-chain cDNA constructs, 2) responsiveness was not transferred by a chimeric α-chain construct containing the N and J regions from a responsive T hybrid clone and the Vα10 Vα region from a nonresponsive clone, and 3) responsiveness was transferred by a chimeric α-chain construct in which most of the Vα region (from the N terminus to the C-terminal end of the complementarity-determining region 2) was derived from the Vα4 α-chain of a responsive T hybrid and the rest (framework 3, N, and J) from the Vα8 α-chain of a nonresponsive T hybrid. Thus, these data provide the first direct evidence for a specific SAg response facilitating activity in a defined Vα segment and map this activity N-terminal of framework region 3. Furthermore, the diversity in the α- and β-chain functional regions of a panel of staphylococcal enterotoxin B-responsive Vβ6 T hybrid clones excludes a stringent corequirement for a oarticular iunctional region for the Vα4 segment to mediate its facilitating activity. Finally, a model postulating a universal role for Vα elements in TCR recognition of SAg is presented.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5229-5236 |
| Number of pages | 8 |
| Journal | Journal of Immunology |
| Volume | 158 |
| Issue number | 11 |
| State | Published - 1997 |
| Externally published | Yes |
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ASJC Scopus subject areas
- Immunology
Cite this
Gene transfer directly demonstrates a role for TCR Vα elements in superantigen recognition. / Donson, David; Borrero, Heriberto; Rutman, Matthew; Pergolizzi, Robert; Malhado-Chang, Norika O; Macphail, Stuart.
In: Journal of Immunology, Vol. 158, No. 11, 1997, p. 5229-5236.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Gene transfer directly demonstrates a role for TCR Vα elements in superantigen recognition
AU - Donson, David
AU - Borrero, Heriberto
AU - Rutman, Matthew
AU - Pergolizzi, Robert
AU - Malhado-Chang, Norika O
AU - Macphail, Stuart
PY - 1997
Y1 - 1997
N2 - Recent structure-function studies of ours and others indicating that regions of the TCR other than Vβ are involved in the TCR-superantigen (SAg)-MHC class II trimolecular interaction were correlative; thus, while the conclusions were persuasive, they were not unequivocal. The transfecfion experiments described in this report show that 1) responsiveness to staphylococcal enterotoxin B in Vβ6 T cells was transferred by a Vα4- but not by Vα8- and Vα10-containing α-chain cDNA constructs, 2) responsiveness was not transferred by a chimeric α-chain construct containing the N and J regions from a responsive T hybrid clone and the Vα10 Vα region from a nonresponsive clone, and 3) responsiveness was transferred by a chimeric α-chain construct in which most of the Vα region (from the N terminus to the C-terminal end of the complementarity-determining region 2) was derived from the Vα4 α-chain of a responsive T hybrid and the rest (framework 3, N, and J) from the Vα8 α-chain of a nonresponsive T hybrid. Thus, these data provide the first direct evidence for a specific SAg response facilitating activity in a defined Vα segment and map this activity N-terminal of framework region 3. Furthermore, the diversity in the α- and β-chain functional regions of a panel of staphylococcal enterotoxin B-responsive Vβ6 T hybrid clones excludes a stringent corequirement for a oarticular iunctional region for the Vα4 segment to mediate its facilitating activity. Finally, a model postulating a universal role for Vα elements in TCR recognition of SAg is presented.
AB - Recent structure-function studies of ours and others indicating that regions of the TCR other than Vβ are involved in the TCR-superantigen (SAg)-MHC class II trimolecular interaction were correlative; thus, while the conclusions were persuasive, they were not unequivocal. The transfecfion experiments described in this report show that 1) responsiveness to staphylococcal enterotoxin B in Vβ6 T cells was transferred by a Vα4- but not by Vα8- and Vα10-containing α-chain cDNA constructs, 2) responsiveness was not transferred by a chimeric α-chain construct containing the N and J regions from a responsive T hybrid clone and the Vα10 Vα region from a nonresponsive clone, and 3) responsiveness was transferred by a chimeric α-chain construct in which most of the Vα region (from the N terminus to the C-terminal end of the complementarity-determining region 2) was derived from the Vα4 α-chain of a responsive T hybrid and the rest (framework 3, N, and J) from the Vα8 α-chain of a nonresponsive T hybrid. Thus, these data provide the first direct evidence for a specific SAg response facilitating activity in a defined Vα segment and map this activity N-terminal of framework region 3. Furthermore, the diversity in the α- and β-chain functional regions of a panel of staphylococcal enterotoxin B-responsive Vβ6 T hybrid clones excludes a stringent corequirement for a oarticular iunctional region for the Vα4 segment to mediate its facilitating activity. Finally, a model postulating a universal role for Vα elements in TCR recognition of SAg is presented.
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UR - http://www.scopus.com/inward/citedby.url?scp=0031157107&partnerID=8YFLogxK
M3 - Article
C2 - 9164940
AN - SCOPUS:0031157107
VL - 158
SP - 5229
EP - 5236
JO - Journal of Immunology
JF - Journal of Immunology
SN - 0022-1767
IS - 11
ER -