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首页> 外文期刊>BMC Immunology >Boosting immune response with the invariant chain segments via association with non-peptide binding region of major histocompatibility complex class II molecules
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Boosting immune response with the invariant chain segments via association with non-peptide binding region of major histocompatibility complex class II molecules

机译：通过与主要组织相容性复合体II类分子的非肽结合区缔合来增强恒定链段的免疫反应

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Background Based on binding of invariant chain (Ii) to major histocompatibility complex (MHC) class II molecules to form complexes, Ii-segment hybrids, Ii-key structure linking an epitope, or Ii class II-associated invariant chain peptide (CLIP) replaced with an epitope were used to increase immune response. It is currently unknown whether the Ii-segment cytosolic and transmembrane domains bind to the MHC non-peptide binding region (PBR) and consequently influence immune response. To investigate the potential role of Ii-segments in the immune response via MHC II/peptide complexes, a few hybrids containing Ii-segments and a multiepitope (F306) from Newcastle disease virus fusion protein (F) were constructed, and their binding effects on MHC II molecules and specific antibody production were compared using confocal microscopy, immunoprecipitation, western blotting and animal experiments. Results One of the Ii-segment/F306 hybrids, containing ND (Asn–Asp) outside the F306 in the Ii-key structure (Ii-key/F306/ND), neither co-localized with MHC II molecules on plasma membrane nor bound to MHC II molecules to form complexes. However, stimulation of mice with the structure produced 4-fold higher antibody titers compared with F306 alone. The two other Ii-segment/F306 hybrids, in which the transmembrane and cytosolic domains of Ii were linked to this structure (Cyt/TM/Ii-key/F306/ND), partially co-localized on plasma membrane with MHC class II molecules and weakly bound MHC II molecules to form complexes. They induced mice to produce approximately 9-fold higher antibody titers compared with F306 alone. Furthermore, an Ii/F306 hybrid (F306 substituting CLIP) co-localized well with MHC II molecules on the membrane to form complexes, although it increased antibody titer about 3-fold relative to F306 alone. Conclusions These results suggest that Ii-segments improve specific immune response by binding to the non-PBR on MHC class II molecules and enabling membrane co-localization with MHC II molecules, resulting in the formation of relatively stable MHC II/peptide complexes on the plasma membrane, and signal transduction.
机译：背景技术基于不变链（Ii）与主要组织相容性复合物（MHC）II类分子的结合形成复合物，Ii段杂种，连接表位的Ii-关键结构或与IIi类相关的不变链肽（CLIP）取代具有表位的抗原被用于增加免疫反应。目前尚不清楚II片段的胞质和跨膜结构域是否结合至MHC非肽结合区（PBR）并因此影响免疫应答。为了研究Ii片段在通过MHC II /肽复合物的免疫反应中的潜在作用，构建了一些包含Ii片段和来自新城疫病毒融合蛋白（F）的多表位（F306）的杂种，并结合了它们对使用共聚焦显微镜，免疫沉淀，蛋白质印迹和动物实验比较了MHC II分子和特异性抗体的产生。结果一种Ii段/ F306杂种，在Ii键结构（Ii-key / F306 / ND）中在F306外包含ND（Asn–Asp），既不与质膜上的MHC II分子共定位也不结合与MHC II分子形成复合物。但是，与单独的F306相比，用该结构刺激小鼠产生的抗体滴度高4倍。其他两个Ii段/ F306杂种，其中Ii的跨膜结构域和胞质结构域与该结构（Cyt / TM / Ii-key / F306 / ND）连接，与MHC II类分子部分共定位在质膜上和弱结合的MHC II分子形成复合物。他们诱导小鼠产生的抗体效价比单独的F306高约9倍。此外，尽管Ii / F306杂合体（取代CLIP的F306）与MHC II分子在膜上很好地共定位以形成复合物，但相对于单独的F306，它的抗体效价提高了约3倍。结论这些结果表明，II片段通过结合II类MHC分子上的非PBR并使膜与MHC II分子共定位，从而改善了特异性免疫反应，从而在血浆上形成了相对稳定的MHC II /肽复合物。膜和信号转导。

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