A B cell-, T cell-linked epitope located on the adhesin of Mycoplasma pneumoniae.

The identification of specific T cell and B cell epitopes of the P1 protein, which functions as an adhesin and as a major antigen of Mycoplasma pneumoniae, has become of central interest for the design of synthetic vaccines. Here we report the isolation from guinea pigs infected intranasally with M. pneumoniae of hilar and bronchial T lymphocytes which proliferated after in vitro stimulation with sonicated M. pneumoniae whole-cell antigen and with the isolated P1 protein. For more detailed information on T cell epitopes, a 51-amino-acid region (histidine 821 to glycine 871; numbered from the NH2-terminal end) of the P1 protein was analyzed for a T cell epitope. An octapeptide, S-G-S-R-S-F-L-P (starting at amino acid 845), stimulated in vitro lymphocytes of bronchial washings and of hilar lymph nodes. Furthermore, this T cell-stimulating amino acid sequence was located at the C-terminal end of a B cell epitope with the sequence T-N-T (starting at amino acid 842).