International Immunology Advance Access published online on March 29, 2004
International Immunology, doi:10.1093/intimm/dxh068
© 2004 by The Japanese Society for Immunology
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1 Institute for Virology and Immunobiology, University of Würzburg, Würzburg 97078, Germany
* To whom correspondence should be addressed. E-mail: herrmann-t{at}vim.uni-wuerzburg.de.
In experimental autoimmune encephalomyelitis (EAE) of LEW rats, BV8S2+ (V Keywords:
Keywords: autoimmunity, experimental autoimmune encephalomyelitis, LEW, T cell repertoire
Accepted February 3, 2004
Article
Contrasting contributions of complementarity-determining region 2 and hypervariable region 4 of rat BV8S2+ (V
8.2) TCR to the recognition of myelin basic protein and different types of bacterial superantigens
2 Institute of Virology, University of Dresden, Dresden 01307, Germany
3 Department of Microbiology and Immunology, Tokyo Women’s Medical University School of Medicine, Tokyo 162-8666, Japan
4 Institute of Immunology, University Hospital, RWTH-Aachen, Aachen 52074, Germany
5 Institute of Infectious Diseases and Immunology, University of Utrecht, Utrecht 3584 CL, The Netherlands
6 Institute for Virology and Immunobiology, University of Würzburg, Würzburg 97078, Germany; Institute for Virology and Immunobiology, Versbacherstrasse 7, Würzburg 97078, Germany
Abstract 
8.2) T cells dominate the RT1Bl-restricted response to guinea pig myelin basic protein (gpMBP), and respond to the superantigens (SAg) Staphylococcus enterotoxin C1 (SEC1), Mycoplasma arthritidis SAg (MAS) and Yersinia pseudotuberculosis mitogen (YPM). T cells expressing the closely related BV8S4 differ from BV8S2 T cells in their response to gpMBP, and the SAg SEC1 and MAS, but not in their response to YPM. The functional differences between BV8S2 and BV8S4, which vary in complementarity-determining/hypervariable region 4 (CDR4/HV4) and CDR2, were analyzed by cloning and mutating a TCR with features typical for gpMBP-specific BV8S2+ TCR. The wild-type BV8S2 receptor and the BV8S4-like CDR2 + 4 double mutant of BV8S2 showed the same differences in ligand specificity as polyclonal BV8S2+ and BV8S4+ lymphocyte populations. The CDR2 mutant lost its reactivity for SEC1 and gpMBP68-88, but the CDR4/HV4 mutation abolished only activation by SEC1. Thus, CDR2 and HV4 contribute not only differently to recognition of peptide antigens, but also to recognition of different types of bacterial SAg.
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