Membrane proteins with molecular masses of 88, 90 and 150 kDa are responsible for binding of human immunoglobulin G Fc fragment to the native cells of Mycoplasma salivarium

Ken ichiro Shibata, Yoshihiko Sawa, Satoshi Inoue, Mamoru Noda, Tsuguo Watanabe

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

Mycoplasma salivarium cells bound the Fc fragment of human immunoglobulin G. The activity was remarkablu enhanced by Mn+, but not by Mg2+ and Ca2+; significantly inhibited by D-mannose; and reduced by pronase treatment of the cells. About 90% of the cells treated with pronase were not disrupted. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins of the cells treated with pronase indicated that proteins with molecular masses of 88, 90 and 150 kDa (88 kp, 90 kp and 150 kp) were specifically digested. The results presented suggest that 88 kp, 90 kp and 150 kp, located in the outer surface of the cell membrane, are responsible for the activity of the M. salivarium cells and interact with a carbohydrate-containing moiety (D-mannose) of the Fc fragment in a Mn2+-dependent manner.

Original languageEnglish
Pages (from-to)305-309
Number of pages5
JournalFEMS Microbiology Letters
Volume123
Issue number3
Publication statusPublished - Nov 1 1994
Externally publishedYes

Fingerprint

Mycoplasma salivarium
Immunoglobulin Fc Fragments
Membrane Proteins
Immunoglobulin G
Pronase
Mannose
Sodium Dodecyl Sulfate
Polyacrylamide Gel Electrophoresis
Proteins
Carbohydrates
Cell Membrane

Keywords

  • Fc fragment binding activity
  • Mycoplasma salivarium
  • Pronase

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics

Cite this

Membrane proteins with molecular masses of 88, 90 and 150 kDa are responsible for binding of human immunoglobulin G Fc fragment to the native cells of Mycoplasma salivarium. / Shibata, Ken ichiro; Sawa, Yoshihiko; Inoue, Satoshi; Noda, Mamoru; Watanabe, Tsuguo.

In: FEMS Microbiology Letters, Vol. 123, No. 3, 01.11.1994, p. 305-309.

Research output: Contribution to journalArticle

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AU - Sawa, Yoshihiko

AU - Inoue, Satoshi

AU - Noda, Mamoru

AU - Watanabe, Tsuguo

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AB - Mycoplasma salivarium cells bound the Fc fragment of human immunoglobulin G. The activity was remarkablu enhanced by Mn+, but not by Mg2+ and Ca2+; significantly inhibited by D-mannose; and reduced by pronase treatment of the cells. About 90% of the cells treated with pronase were not disrupted. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of proteins of the cells treated with pronase indicated that proteins with molecular masses of 88, 90 and 150 kDa (88 kp, 90 kp and 150 kp) were specifically digested. The results presented suggest that 88 kp, 90 kp and 150 kp, located in the outer surface of the cell membrane, are responsible for the activity of the M. salivarium cells and interact with a carbohydrate-containing moiety (D-mannose) of the Fc fragment in a Mn2+-dependent manner.

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