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首页> 外文期刊>BMC Biotechnology >Antigen vehiculization particles based on the Z protein of Junin virus
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Antigen vehiculization particles based on the Z protein of Junin virus

机译：基于Junin病毒Z蛋白的抗原载体化颗粒。

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Background Arenavirus matrix protein Z plays an important role in virus budding and is able to generate enveloped virus-like-particles (VLPs) in absence of any other viral proteins. In these VLPs, Z protein is associated to the plasma membrane inner surface by its myristoyl residue. Budding induction and vesicle formation properties can be exploited to generate enveloped VLPs platform. These structures can be designed to carry specific antigen in the inner side or on the surface of VLPs. Vaccines based on VLPs are a highly effective type of subunit vaccines that mimic the overall structure of virus particles in absence of viral nucleic acid, being noninfectious. In this work we assayed the capacity of Junin Z protein to produce VLPs carrying the green fluorescent protein (eGFP), as a model antigen. Results In this report the Junin Z protein ability to produce VLPs from 293T cells and its capacity to deliver a specific antigen (eGFP) fused to Z was evaluated. Confocal microscopy showed a particular membrane bending in cells expressing Z and a spot welded distribution in the cytoplasm. VLPs were detected by TEM (transmission electron microscopy) and were purified from cell supernatant. The proteinase protection assay demonstrated the VLPs integrity and the absence of degradation of the fused antigen, thus indicating its internal localization. Finally, immunization of mice with purified VLPs produced high titres of anti-eGFP antibodies compared to the controls. Conclusions It was proved that VLPs can be generated from cells transfected with a fusion Junin virus Z-eGFP protein in absence of any other viral protein, and the capacity of Z protein to support fusions at the C-terminal, without impairing its budding activity, allowing vehiculization of specific antigens into VLPs.
机译：背景竞技场病毒基质蛋白Z在病毒萌发中起着重要作用，并且能够在不存在任何其他病毒蛋白的情况下产生包膜的病毒样颗粒（VLP）。在这些VLP中，Z蛋白通过肉豆蔻酰基残基与质膜内表面结合。可以利用萌芽诱导和囊泡形成特性来产生包膜的VLP平台。可设计这些结构以在VLP的内侧或表面携带特定抗原。基于VLP的疫苗是一种非常有效的亚单位疫苗，可在无病毒核酸的情况下模拟病毒颗粒的整体结构，具有非传染性。在这项工作中，我们分析了Junin Z蛋白生产带有绿色荧光蛋白（eGFP）作为模型抗原的VLP的能力。结果在本报告中，对Junin Z蛋白从293T细胞产生VLP的能力及其传递与Z融合的特异性抗原（eGFP）的能力进行了评估。共聚焦显微镜显示表达Z的细胞发生特定的膜弯曲，并在细胞质中出现点焊分布。通过TEM（透射电子显微镜）检测VLP，并从细胞上清液中纯化。蛋白酶保护试验证明了VLP的完整性和融合抗原的降解，因此表明其内部定位。最后，与对照相比，用纯化的VLP免疫小鼠可产生高滴度的抗eGFP抗体。结论已证明，在不存在任何其他病毒蛋白的情况下，可以通过用融合的Junin病毒Z-eGFP蛋白转染的细胞产生VLP，并且Z蛋白在C端支持融合的能力不损害其萌发活性，允许将特定抗原囊化为VLP。

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