Binding of salivary glycoprotein-secretory immunoglobulin a complex to the surface protein antigen of Streptococcus mutans

Takahiko Oho, Hao Yu, Yoshihisa Yamashita, Toshihiko Koga

研究成果: ジャーナルへの寄稿記事

75 引用 (Scopus)

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
66
発行部数1
出版物ステータス出版済み - 1998

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Streptococcus mutans
Agglutinins
Surface Antigens
Immunoglobulins
Glycoproteins
Membrane Proteins
N-Acetylneuraminic Acid
Secretory Immunoglobulin A
Acetylgalactosamine
Fucose
Acetylglucosamine
Surface Plasmon Resonance
Mercaptoethanol
Neuraminidase
Biosensing Techniques
Mannose
Galactose
Sodium Dodecyl Sulfate
Hot Temperature
Calcium

All Science Journal Classification (ASJC) codes

  • Immunology

これを引用

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

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abstract = "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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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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