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变形链球菌血清型h碳水化合物抗原的免疫化学特性

Immunochemical characteristics of Streptococcus mutans serotype h carbohydrate antigen.

作者信息

Okahashi N, Nishida Y, Koga T, Hamada S

出版信息

Microbiol Immunol. 1984;28(4):407-13. doi: 10.1111/j.1348-0421.1984.tb00692.x.

DOI:10.1111/j.1348-0421.1984.tb00692.x
PMID:6748966
Abstract

Serotype h carbohydrate antigen was prepared from cell walls of Streptococcus mutans strain MFe28 of monkey origin. The h antigen was extracted from the cell walls with 5% trichloracetic acid at 4 C, and purified by DEAE-Sephadex A-25 ion exchange chromatography followed by Sephacryl S-300 gel filtration. The purified antigen was composed of galactose (75%), glucose (16%), and rhamnose (3%). Although the antiserum against whole cells of S. mutans MFe28 gave a strong cross reaction with serotype d S. mutans, serotype h-specific antiserum could be obtained by adequate adsorption. The precipitin reactions and hapten inhibition test using serotype h-specific antiserum showed that galactose, glucose, and their derivative sugars were markedly potent inhibitors. It was concluded that the serotype h antigen is immunologically distinguishable from the known serotypes of S. mutans, although it is closely related to serotype d antigen of S. mutans.

摘要

血清型h碳水化合物抗原是从源自猴子的变形链球菌MFe28菌株的细胞壁制备的。h抗原在4℃下用5%三氯乙酸从细胞壁中提取,并通过DEAE-葡聚糖A-25离子交换色谱,随后进行Sephacryl S-300凝胶过滤进行纯化。纯化的抗原由半乳糖(75%)、葡萄糖(16%)和鼠李糖(3%)组成。尽管抗变形链球菌MFe28全细胞的抗血清与血清型d变形链球菌有强烈的交叉反应,但通过适当吸附可获得血清型h特异性抗血清。使用血清型h特异性抗血清的沉淀反应和半抗原抑制试验表明,半乳糖、葡萄糖及其衍生糖是明显有效的抑制剂。得出的结论是,血清型h抗原在免疫上与变形链球菌的已知血清型不同,尽管它与变形链球菌的血清型d抗原密切相关。

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Infect Immun. 2000 Feb;68(2):725-31. doi: 10.1128/IAI.68.2.725-731.2000.
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Cloning and expression of two Streptococcus mutans glucosyltransferases in Escherichia coli K-12.变形链球菌两种葡糖基转移酶在大肠杆菌K-12中的克隆与表达
Infect Immun. 1985 Aug;49(2):414-6. doi: 10.1128/iai.49.2.414-416.1985.
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Immunological study of cross-reactive polysaccharide antigens (types a, d, and h) of oral Streptococcus spp. with monoclonal antibodies.
口腔链球菌属交叉反应性多糖抗原(a、d和h型)与单克隆抗体的免疫学研究。
Infect Immun. 1987 Jan;55(1):266-8. doi: 10.1128/iai.55.1.266-268.1987.