Enhancement of antigen presentation of influenza virus hemagglutinin by the natural human anti-Gal antibody
Enhancement of antigen presentation of influenza virus hemagglutinin by the natural human anti-Gal antibody
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DOI：
10.1016/0264-410x(95)00189-8
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发表时间：
1996-03-01
期刊：
影响因子：
5.5
通讯作者：
Gerhard, W
中科院分区：
文献类型：
--
作者：
Galili, U;Repik, PM;Gerhard, W
灭活病毒或亚病毒疫苗的免疫原性可以通过与IgG抗体复合来增强。这种抗体将通过抗体-疫苗复合物与巨噬细胞和其他APC上的Fc受体的粘附来增加抗原呈递细胞（APC）对疫苗抗原的摄取、加工和呈递。通常可用于此目的的人体天然抗体是天然抗Gal抗体。该抗体在人类和旧世界灵长类动物中普遍产生为循环IgG的1%，并且其与碳水化合物表位Gal α 1-3 Gal β 1-4GlcNAc-R（称为α-半乳糖基表位）特异性相互作用。该表位在非灵长类哺乳动物和新世界猴的细胞中通过糖基化酶α 1，3半乳糖基转移酶大量合成。在这里，我们描述了在体外研究的能力，抗半乳糖苷结合α-半乳糖基表位的流感病毒在哺乳动物细胞中繁殖，并增强介绍APC的病毒血凝素抗原决定簇的特异性辅助T细胞克隆。讨论了在病毒粒子和亚病毒疫苗上表达α-半乳糖基表位的各种方法。版权所有（C）1996 Elsevier Science Ltd.
Immunogenicity of inactivated virus or subviral vaccines may be enhanced by complexing with an IgG antibody. Such antibody would increase the uptake, processing and presentation of the vaccine's antigens by antigen presenting cells (APC), via the adhesion of the antibody-vaccine complex to Fc-receptors on macrophages and other APC. A natural antibody in humans, which may be generally exploited for this purpose, is the natural anti-Gal antibody, This antibody is ubiquitously produced as 1% of circulating IgG in humans and Old World primates, and it interacts specifically with the carbohydrate epitope Gal alpha 1-3 Gal beta 1-4GlcNAc-R (termed the alpha-galactosyl epitope). This epitope is synthesized in large amounts in cells of nonprimate mammals and New World monkeys by the glycosylation enzyme alpha 1,3 galactosyltransferase. Here we describe in vitro studies on the ability of anti-Gal to bind to alpha-galactosyl epitopes on influenza virus propagated in mammalian cells, and to enhance presentation by APC of viral hemagglutinin antigenic determinants to specific helper T cell clones. The various approaches for achieving alpha-galactosyl epitope expression on virion and subviral vaccines ave discussed. Copyright (C) 1996 Elsevier Science Ltd.