TY - JOUR
T1 - Immunodominance of conformation-dependent B-cell epitopes of protein antigens
AU - Ito, Hiro O.
AU - Nakashima, Toshihiro
AU - So, Takanori
AU - Hirata, Masato
AU - Inoue, Masakazu
N1 - Funding Information:
We thank Drs. Tadashi Ueda, Toshihiko Koga, Koji Nakayama, and Tetsuhiro Moriya for the donation of biological materials and helpful suggestions, Drs. Fuminobu Yoshimura and Toshitaka Koga for valuable discussions and continuous encouragement, and Ms. Mariko Ohara for critical reading of the manuscript. This work was supported in part by Grants-in-Aid for Scientific Research from the Ministry of Education, Science, Sports and Culture of Japan (Nos. 09671924 and 12557188).
PY - 2003/9/5
Y1 - 2003/9/5
N2 - Immunodominance of conformational epitopes over linear ones in four proteins was quantified making use of the B-cell hybridoma technology. The proteins were immunized in their native forms into BALB/c mice, and clonal frequencies of B-cell hybridomas that produce antibodies to the native and denatured forms were determined, using ELISA and immunoblotting. All 16 monoclonal antibodies (mAbs) to Porphyromonas gingivalis fimbria were suggested to recognize conformational epitopes expressed by the oligomer. Ten out of 14 mAbs to Serratia marcescens fimbria and 13 of 15 mAbs to hen lysozyme were also specific to their conformational epitopes. In contrast, all 18 mAbs to a surface protein of Streptococcus mutans, termed PAc, reacted to both the native and denatured forms, thereby indicating the immunodominance of linear epitopes in this protein. The results suggest that B-cell epitopes of proteins possessing stable tertiary or quaternary structures are predominantly expressed by the higher-order structures.
AB - Immunodominance of conformational epitopes over linear ones in four proteins was quantified making use of the B-cell hybridoma technology. The proteins were immunized in their native forms into BALB/c mice, and clonal frequencies of B-cell hybridomas that produce antibodies to the native and denatured forms were determined, using ELISA and immunoblotting. All 16 monoclonal antibodies (mAbs) to Porphyromonas gingivalis fimbria were suggested to recognize conformational epitopes expressed by the oligomer. Ten out of 14 mAbs to Serratia marcescens fimbria and 13 of 15 mAbs to hen lysozyme were also specific to their conformational epitopes. In contrast, all 18 mAbs to a surface protein of Streptococcus mutans, termed PAc, reacted to both the native and denatured forms, thereby indicating the immunodominance of linear epitopes in this protein. The results suggest that B-cell epitopes of proteins possessing stable tertiary or quaternary structures are predominantly expressed by the higher-order structures.
KW - B-cell epitope
KW - Hen-egg lysozyme
KW - Higher-order structure
KW - Immunodominance
KW - Monoclonal antibodies
KW - Porphyromonas gingivalis
KW - Protein antigens
KW - Serratia marcescens
KW - Streptococcus mutans
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U2 - 10.1016/S0006-291X(03)01466-9
DO - 10.1016/S0006-291X(03)01466-9
M3 - Article
C2 - 12927785
AN - SCOPUS:0042160142
VL - 308
SP - 770
EP - 776
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 4
ER -