Purification and Characterization of Membrane Protein (90 kDa) from Mycoplasma salivarium, Which Binds Immunoglobulin (Ig) G Fc Fragment

Yoshihiko Sawa, Ken Ichiro Shibata, Mamoru Noda, Tsuguo Watanabe

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

A 90 kDa protein of Mycoplasma salivarium was released from cell membranes of the organism with Triton X-100 and purified by ion-exchange chromatography and chromatofocusing. The protein was eluted at pH 5.5 by chromatofocusing. The protein was shown to react with the Fc fragments of IgG from human and nine different animal species and did not distinguish between IgG from different species, while protein A, tested for comparative purposes, displayed a strong specificity for human and swine IgG. Furthermore, the protein reacted with antigen specific goat IgG (specific for gamma chains of human IgG), sheep red blood cells (SRBC) sensitized with rabbit antiserum to SRBC, that is, the Fc part of rabbit IgG, and concanavalin A as well. These findings may suggest that the protein is a lectin which binds the carbohydrate moiety of the Fc part of IgG.

Original languageEnglish
Pages (from-to)257-262
Number of pages6
JournalMICROBIOLOGY and IMMUNOLOGY
Volume38
Issue number4
DOIs
Publication statusPublished - Jan 1 1994
Externally publishedYes

Keywords

  • IgG Fc-binding protein
  • Mycoplasma salivarium

ASJC Scopus subject areas

  • Microbiology
  • Immunology
  • Virology

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