エンド‐Ｎ‐アセチルムラミダーゼ（Ｍ‐１酵素）を用いて分離したＳｔｒｅｐｔｏｃｏｃｃｕｓ　ｐｙｏｇｅｎｅｓ　Ｍ３型株のＭたんぱく質の免疫・生物学的性状，特にオプソニン抗体生成能について

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  • Biological and immunological properties of native Streptococcal M protein isolated by use of endo-N-acetylmuramidase, especially production of opsonic antibody.
  • エンド N アセチルムラミダーゼ M-1 コウソ オ モチイテ ブンリシタ S

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1. The M protein of Streptococcus pyogenes (type 3, strain Sv) was solubilized by treatment of a cell envelope fraction with endo-N-acetylmuramidase (the M-1 enzyme). It was concentrated by salting out at 30-80% saturation of ammonium sulfate and fractionated on a QAE-Sephadex column by elution with a linear gradient of sodium chloride concentration.<br>2. The M protein thus isolated (mur M3) was shown to be practically a homogeneous protein with a molecular weight of 150, 000-160, 000 daltones and an isoelectric point of 5.9 in SDS-polyacrylamide gradient gel electrophoresis (PAGE) and PAGE, respectively, and to give essentially a single precipitin line with anti-Sv whole cell rabbit serum and anti-mur M3 guinea-pig serum in Ouchterlony's agar gel precipitin reaction.<br>3. Mur M3 composed almost exclusively of amino acids, contained neither muramic acid nor glucosamine, but contained trace amounts of rhamnose and organic phosphorus.<br>4. Mur M3 exhibited a distinct type-specific, opsonin-neutralizing activity which was susceptible to trypsin but resistant to boiling in 0.2N HCl.<br>5. Mur M3 was mitogenic on murine thymocytes, but not on murine splenocyte, and activated the human complement system via the classical as well as an alternate pathway.<br>6. Mur M3 was immunogenic to guinea pigs, rabbits and mice, especially to guinea pigs. Two intra-footpad injections of 10μg amounts of mur M3 into guinea pigs without any adjuvant stimulated a distinct and long-lasting production of anti-M3 opsonizing and protective antibody.<br>The results described in this report suggest that mur M3 is a more native M protein than those so far obtained by other researchers.

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