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Type-specific antigens of group A Neisseria meningitidis: lipopolysaccharide and heat-modifiable outer membrane proteins.

机译:A组脑膜炎奈瑟氏球菌的类型特异性抗原:脂多糖和可热修饰的外膜蛋白。

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摘要

The solid-phase radioimmunoassay inhibition method was used to analyze the noncapsular surface antigens of group A Neisseria meningitidis for type specificity. By use of antisera prepared against group A strains, three serologically distinct lipopolysaccharide antigens and five outer membrane protein antigens were identified among group A strains from a variety of geographical origins. Two of the lipopolysaccharide antigens were unique to group A strains while the third was similar to those on strains of other meningococcal serogroups. Fractionation of outer membrane proteins in the presence of 2% sodium deoxycholate followed by quantitative inhibition of the typing reactions with the subfractions revealed that the protein responsible for type specificity was not the principal outer membrane protein, but, most likely, the 31,000-dalton, heat-modifiable outer membrane protein. Thus, although group A strains may share a common principal outer membrane protein, typing is feasible using other surface antigens. In a survey of 82 group A strains, 93% were typable with respect to outer membrane proteins.
机译:固相放射免疫分析抑制方法用于分析A组脑膜炎奈瑟氏球菌的非荚膜表面抗原的类型特异性。通过使用针对A组毒株制备的抗血清,在来自各种地理起源的A组毒株中鉴定出3种血清学上不同的脂多糖抗原和5种外膜蛋白抗原。脂多糖抗原中的两种是A组菌株独有的,而第三种则与其他脑膜炎球菌血清群的相似。在2%脱氧胆酸钠存在下分级分离外膜蛋白,然后对亚型的打字反应进行定量抑制,发现负责类型特异性的蛋白不是主要的外膜蛋白,最有可能是31,000道尔顿,可热修饰的外膜蛋白。因此,尽管A组菌株可能共享一个共同的主要外膜蛋白,但使用其他表面抗原进行分型是可行的。在对82个A组菌株的调查中,有93%的菌株具有外膜蛋白分型。

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