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首页> 外文期刊>Infection and immunity >Anti-Gal binds to pili of Neisseria meningitidis: the immunoglobulin A isotype blocks complement-mediated killing.
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Anti-Gal binds to pili of Neisseria meningitidis: the immunoglobulin A isotype blocks complement-mediated killing.

机译：抗-Gal与脑膜炎奈瑟氏菌的菌毛结合：免疫球蛋白A同种型阻断补体介导的杀伤。

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alpha 1,3-Galactosyl antibodies (anti-Gal) are ubiquitous natural human serum and secretory polyclonal antibodies that bind to terminal galactose-alpha 1,3-galactose (alpha-galactosyl) residues. Serum immunoglobulin G (IgG) anti-Gal can block alternative complement pathway-mediated lysis of representative gram-negative enteric bacteria that bind it to lipopolysaccharide alpha-galactosyl structures, thereby promoting survival of such bacteria in the nonimmune host. We wanted to know whether anti-Gal also could bind to the lipooligosaccharides (LOS) of Neisseria meningitidis. To our surprise, we found that serum and secretory anti-Gal bound to pili but not to LOS of certain strains. This suggested the presence of an immunogenic pilus carbohydrate epitope. Mild periodate oxidation of sodium dodecyl sulfate-polyacrylamide gel electrophoresis-separated outer membrane preparations from strains that bound anti-Gal followed by labeling of the neoaldehyde groups resulted in the labeling of bands that corresponded to pilin and LOS, confirming that pilin contains carbohydrate structures. A Bandeiraea simplicifolia lectin that also binds terminal alpha 1,3-galactosyl residues also bound to pilin. Serum IgG, IgA, and IgM anti-Gal as well as colostral secretory IgA anti-Gal bound to pilin, as judged by immunoblotting, and to the pili of intact piliated organisms, as judged by immunoelectron microscopy. Total serum anti-Gal (IgG, IgA, and IgM) and purified serum IgA1 anti-Gal, but not its purified IgG isotype, blocked complement-mediated lysis of a piliated meningococcal strain that bound anti-Gal to its pili. Colostral anti-Gal secretory IgA blocked killing of the same strain. Thus, anti-Gal IgA may promote disease when it binds to the pili of N. meningitidis strains.
机译：α1,3-半乳糖基抗体（抗Gal）是普遍存在的天然人血清和分泌性多克隆抗体，可与末端半乳糖-α1,3-半乳糖（α-半乳糖基）残基结合。血清免疫球蛋白G（IgG）抗Gal可以阻断替代性补体途径介导的代表性革兰氏阴性肠细菌的裂解，使之与脂多糖α-半乳糖基结构结合，从而促进此类细菌在非免疫宿主中的存活。我们想知道抗-Gal是否也可以与脑膜炎奈瑟氏球菌的脂寡糖（LOS）结合。令我们惊讶的是，我们发现血清和分泌型抗Gal结合菌毛，但不结合某些菌株的LOS。这表明存在免疫原性菌毛碳水化合物表位。十二烷基硫酸钠-聚丙烯酰胺凝胶电泳分离的结合抗-Gal菌株的外膜制剂的轻度高碘酸氧化，然后标记新醛基，导致对应于菌毛蛋白和LOS的条带被标记，证实菌毛蛋白含有碳水化合物结构。一个Bandeiraea simplicifolia凝集素也结合也与菌毛素结合的末端α1,3-半乳糖基残基。血清IgG，IgA和IgM抗-Gal以及初乳分泌型IgA抗-Gal通过免疫印迹判断与菌毛蛋白结合，并通过免疫电子显微镜判断与完整的毛细血管生物的菌毛结合。总血清抗-Gal（IgG，IgA和IgM）和纯化的血清IgA1抗-Gal，但不是其纯化的IgG同种型，阻断了将抗-Gal与其菌毛结合的纤毛型脑膜炎球菌菌株的补体介导裂解。鼻腔抗Gal分泌型IgA阻止了同一菌株的杀死。因此，抗Gal IgA当与脑膜炎奈瑟氏球菌菌株的菌毛结合时可能会促进疾病。

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