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. 1983 Feb;39(2):762–766. doi: 10.1128/iai.39.2.762-766.1983

Immunochemical Properties of Glucosyltransferases from Streptococcus mutans

Kazuhiro Fukui 1, Susumu Kokeguchi 1, Keijiro Kato 1, Yoichiro Miyake 2, Ryuzo Nogami 2, Takafumi Moriyama 3
PMCID: PMC348015  PMID: 6187685

Abstract

Antiserum against purified mutansynthetase (EC 2.4.1.?) of Streptococcus mutans 6715 (serotype g), which is responsible for the synthesis of water-insoluble glucan (ISG) in the presence of both sucrose and water-soluble glucan, was prepared. The specificity of the antiserum was tested by using crude enzyme preparations (CEPs) of S. mutans strains of various serotypes. On immunodiffusion, the antiserum cross-reacted with CEPs from strains of serotypes a (HS-6 and AHT), d (OMZ176), and g (OMZ65 and KIR), but not with those from strains of serotypes b (BHT and FA-1) and c (GS-5 and Ingbritt). The antiserum inhibited the synthesis of ISG by crude or purified mutansynthetase of S. mutans 6715. The activities of ISG synthesis by CEPs from the strains antigenically related in the foregoing immunodiffusion were inhibited by the antiserum against strain 6715 mutansynthetase. The antiserum, however, also inhibited the enzyme activity of the strains of serotype b. The finding that the antiserum against purified dextransucrase of S. mutans HS-6 inhibited ISG synthesis by a CEP of strain HS-6 and also by CEPs of antigenically related strains suggested that dextransucrase activity is involved in ISG synthesis.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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