Involvement of the Zn-binding region of tetanus toxin in B and T recognition. Influence of Zn fixation.
Tetanus toxin contains a metal-binding site for zinc, located in its light chain. The sequence accounting for Zn fixation is part of a predicted amphipathic helical secondary structure and corresponds to a putative T cell epitope according to Rothbard and Taylor (EMBO J. 7, 93-100, 1988). In this paper, we analyse the antigenic properties of two synthetic peptides (233-248 = P12 and 225-243 = P13) containing the Zn binding sequence. Our results show that peptide P13 contains a B and T epitope. The B epitope seems to be immuno-dominant whether the T epitope is at least DR2 restricted. Zn binding on P13 leads to a decrease in its recognition by both antibodies and T lymphocytes.
Villiers
M B
MB
Laboratoire d'Immunochimie, DBMS/ICH-INSERM U238, Grenoble, France.
Gabert
F M
FM
Jacquier
M R
MR
Villiers
C L
CL
Colomb
M G
MG
D000595:Amino Acid Sequence; D001402:B-Lymphocytes / Q000276:immunology*; D001665:Binding Sites; D001667:Binding, Competitive; D000939:Epitopes / Q000737:chemistry / Q000276:immunology; D015802:HLA-DR2 Antigen; D006639:Histidine / Q000276:immunology; D006801:Humans; D008969:Molecular Sequence Data; D013601:T-Lymphocytes / Q000276:immunology*; D013744:Tetanus Toxin / Q000276:immunology*; D015032:Zinc / Q000276:immunology*
D000939:Epitopes; D015802:HLA-DR2 Antigen; D013744:Tetanus Toxin; D006639:Histidine; D015032:Zinc