TY - JOUR
T1 - Distribution and immunochemical specificities of fimbriae of Porphyromonas gingivalis and related bacterial species
AU - Ogawa, Tomohiko
AU - Mukai, Tetsu
AU - Yasuda, Kenji
AU - Shimauchi, Hidetoshi
AU - Toda, Yoshihisa
AU - Hamada, Shigeyuki
PY - 1991/12
Y1 - 1991/12
N2 - Rabbit polyclonal antibody (Poly‐1) and mouse monoclonal antibodies (mAbs) TO‐11, TO‐14 and TO‐M1 specific for Porphyromonas gingivalis 381 fimbriae were prepared. Poly‐1 and the 3 mAbs were screened for their reactivity with whole cells of oral and nonoral black‐pigmented bacterial species by enzyme‐linked immunosorbent assay (ELISA) and the binding experiment using [125I] Poly‐1 and [125I] mAbs. ELISA revealed that Poly‐1 definitely reacted with whole cells of all the 11 strains of P. gingivalis tested. However, 8 of 11 P. gingivalis strains reacted with mAbs TO‐11, TO‐14 and TO‐M1. These results were confirmed by the specific binding of radiolabelled Poly‐1 and mAb TO‐11 to the 8 strains. The Mr of the fimbrial summit protein (fimbrilin) isolated and purified from P. gingivalis strains 381, BH18/10, HW24D‐1, 6/26 and OMZ 314 was 41 kDa by sodium dodecylsulfate‐polyacrylamide gel electrophoresis. It was found by immunoblotting that mAbs TO‐11 and TO‐14/TO‐M1 recognized different epitopes of fimbrial protein from P. gingivalis strains. visualized similar serotype‐specific antibody bindings to the fimbriae. These results indicate that 11 strains of P. gingivalis could be divided into at least 2 separate groups based on the immunochemical specificities of the fimbriae.
AB - Rabbit polyclonal antibody (Poly‐1) and mouse monoclonal antibodies (mAbs) TO‐11, TO‐14 and TO‐M1 specific for Porphyromonas gingivalis 381 fimbriae were prepared. Poly‐1 and the 3 mAbs were screened for their reactivity with whole cells of oral and nonoral black‐pigmented bacterial species by enzyme‐linked immunosorbent assay (ELISA) and the binding experiment using [125I] Poly‐1 and [125I] mAbs. ELISA revealed that Poly‐1 definitely reacted with whole cells of all the 11 strains of P. gingivalis tested. However, 8 of 11 P. gingivalis strains reacted with mAbs TO‐11, TO‐14 and TO‐M1. These results were confirmed by the specific binding of radiolabelled Poly‐1 and mAb TO‐11 to the 8 strains. The Mr of the fimbrial summit protein (fimbrilin) isolated and purified from P. gingivalis strains 381, BH18/10, HW24D‐1, 6/26 and OMZ 314 was 41 kDa by sodium dodecylsulfate‐polyacrylamide gel electrophoresis. It was found by immunoblotting that mAbs TO‐11 and TO‐14/TO‐M1 recognized different epitopes of fimbrial protein from P. gingivalis strains. visualized similar serotype‐specific antibody bindings to the fimbriae. These results indicate that 11 strains of P. gingivalis could be divided into at least 2 separate groups based on the immunochemical specificities of the fimbriae.
KW - fimbriae
KW - immunochemistry
KW - periodontal desease
KW - porphyromonas gingivalis
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U2 - 10.1111/j.1399-302X.1991.tb00504.x
DO - 10.1111/j.1399-302X.1991.tb00504.x
M3 - Article
C2 - 1726543
AN - SCOPUS:0026289193
VL - 6
SP - 332
EP - 340
JO - Molecular Oral Microbiology
JF - Molecular Oral Microbiology
SN - 2041-1006
IS - 6
ER -