抄録
The interaction between a surface protein antigen (PAc) of Streptococcus mutans and human salivary agglutinin was analyzed with a surface plasmon resonance biosensor. The major component sugars of the salivary agglutinin were galactose, fucose, mannose, N-acetylglucosamine, N-acetylgalactosamine, and N-acetylneuraminic acid. Binding of salivary agglutinin to PAc was calcium dependent and heat labile and required a pH greater than 5. Binding was significantly inhibited by N-acetylneuraminic acid and α2,6-linked sialic acid-specific lectin derived from Sambucus sieboldiana in a dose- dependent manner. Pretreatment of the salivary agglutinin with sialidase reduced the binding activity of the agglutinin to the PAc molecule. The agglutinin was dissociated into high-molecular-mass glycoprotein and secretory immunoglobulin A (sIgA) components by electrophoretic fractionation in the presence of 1% sodium dodecyl sulfate and 1% 2-mercaptoethanol. Neither of the components separated by electrophoretic fractionation, high- molecular-mass glycoprotein or sIgA, bound to the PAc molecule. Furthermore, the high-molecular-mass glycoprotein strongly inhibited the binding of the native salivary complex to PAc. These results suggest that the complex formed by the high-molecular-mass salivary glycoprotein and sIgA is essential for the binding reaction and that the sialic acid residues of the complex play an important role in the interaction between the agglutinin and PAc of S. mutans.
| 元の言語 | 英語 |
|---|---|
| ページ（範囲） | 115-121 |
| ページ数 | 7 |
| ジャーナル | Infection and Immunity |
| 巻 | 66 |
| 発行部数 | 1 |
| 出版物ステータス | 出版済み - 1998 |
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All Science Journal Classification (ASJC) codes
- Immunology
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Binding of salivary glycoprotein-secretory immunoglobulin a complex to the surface protein antigen of Streptococcus mutans. / Oho, Takahiko; Yu, Hao; Yamashita, Yoshihisa; Koga, Toshihiko.
：: Infection and Immunity, 巻 66, 番号 1, 1998, p. 115-121.研究成果: ジャーナルへの寄稿 › 記事
}
TY - JOUR
T1 - Binding of salivary glycoprotein-secretory immunoglobulin a complex to the surface protein antigen of Streptococcus mutans
AU - Oho, Takahiko
AU - Yu, Hao
AU - Yamashita, Yoshihisa
AU - Koga, Toshihiko
PY - 1998
Y1 - 1998
N2 - The interaction between a surface protein antigen (PAc) of Streptococcus mutans and human salivary agglutinin was analyzed with a surface plasmon resonance biosensor. The major component sugars of the salivary agglutinin were galactose, fucose, mannose, N-acetylglucosamine, N-acetylgalactosamine, and N-acetylneuraminic acid. Binding of salivary agglutinin to PAc was calcium dependent and heat labile and required a pH greater than 5. Binding was significantly inhibited by N-acetylneuraminic acid and α2,6-linked sialic acid-specific lectin derived from Sambucus sieboldiana in a dose- dependent manner. Pretreatment of the salivary agglutinin with sialidase reduced the binding activity of the agglutinin to the PAc molecule. The agglutinin was dissociated into high-molecular-mass glycoprotein and secretory immunoglobulin A (sIgA) components by electrophoretic fractionation in the presence of 1% sodium dodecyl sulfate and 1% 2-mercaptoethanol. Neither of the components separated by electrophoretic fractionation, high- molecular-mass glycoprotein or sIgA, bound to the PAc molecule. Furthermore, the high-molecular-mass glycoprotein strongly inhibited the binding of the native salivary complex to PAc. These results suggest that the complex formed by the high-molecular-mass salivary glycoprotein and sIgA is essential for the binding reaction and that the sialic acid residues of the complex play an important role in the interaction between the agglutinin and PAc of S. mutans.
AB - The interaction between a surface protein antigen (PAc) of Streptococcus mutans and human salivary agglutinin was analyzed with a surface plasmon resonance biosensor. The major component sugars of the salivary agglutinin were galactose, fucose, mannose, N-acetylglucosamine, N-acetylgalactosamine, and N-acetylneuraminic acid. Binding of salivary agglutinin to PAc was calcium dependent and heat labile and required a pH greater than 5. Binding was significantly inhibited by N-acetylneuraminic acid and α2,6-linked sialic acid-specific lectin derived from Sambucus sieboldiana in a dose- dependent manner. Pretreatment of the salivary agglutinin with sialidase reduced the binding activity of the agglutinin to the PAc molecule. The agglutinin was dissociated into high-molecular-mass glycoprotein and secretory immunoglobulin A (sIgA) components by electrophoretic fractionation in the presence of 1% sodium dodecyl sulfate and 1% 2-mercaptoethanol. Neither of the components separated by electrophoretic fractionation, high- molecular-mass glycoprotein or sIgA, bound to the PAc molecule. Furthermore, the high-molecular-mass glycoprotein strongly inhibited the binding of the native salivary complex to PAc. These results suggest that the complex formed by the high-molecular-mass salivary glycoprotein and sIgA is essential for the binding reaction and that the sialic acid residues of the complex play an important role in the interaction between the agglutinin and PAc of S. mutans.
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M3 - Article
C2 - 9423847
AN - SCOPUS:0031984905
VL - 66
SP - 115
EP - 121
JO - Infection and Immunity
JF - Infection and Immunity
SN - 0019-9567
IS - 1
ER -