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将表面暴露的结构环鉴定为杯状病毒衍生的病毒样颗粒平台中用于递送外源抗原的插入位点。

Characterization of surface-exposed structural loops as insertion sites for foreign antigen delivery in calicivirus-derived VLP platform.

作者信息

Panasiuk Mirosława, Chraniuk Milena, Zimmer Karolina, Hovhannisyan Lilit, Krapchev Vasil, Peszyńska-Sularz Grażyna, Narajczyk Magdalena, Węsławski Jan, Konopacka Agnieszka, Gromadzka Beata

机构信息

Department of In Vitro Studies, Institute of Biotechnology and Molecular Medicine, Gdańsk, Poland.

Nano Expo Sp z.o.o, Gdańsk, Poland.

出版信息

Front Microbiol. 2023 Feb 27;14:1111947. doi: 10.3389/fmicb.2023.1111947. eCollection 2023.

DOI:10.3389/fmicb.2023.1111947
PMID:36922971
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10010390/
Abstract

Chimeric virus-like particles (cVLPs) show great potential in improving public health as they are safe and effective vaccine candidates. The capsid protein of caliciviruses has been described previously as a self-assembling, highly immunogenic delivery platform. The ability to significantly induce cellular and humoral immunity can be used to boost the immune response to low immunogenic foreign antigens displayed on the surface of VLPs. Capsid proteins of caliciviruses despite sequence differences share similar architecture with structural loops that can be genetically modified to present foreign epitopes on the surface of cVLPs. Here, based on the VP1 protein of norovirus (NoV), we investigated the impact of the localization of the epitope in different structural loops of the P domain on the immunogenicity of the presented epitope. In this study, three distinct loops of NoV VP1 protein were genetically modified to present a multivalent influenza virus epitope consisting of a tandem repeat of M2/NP epitopes. cVLPs presenting influenza virus-conserved epitopes in different localizations were produced in the insect cells and used to immunize BALB/c mice. Specific reaction to influenza epitopes was compared in sera from vaccinated mice to determine whether the localization of the foreign epitope has an impact on the immunogenicity.

摘要

嵌合病毒样颗粒（cVLPs）作为安全有效的候选疫苗，在改善公共卫生方面显示出巨大潜力。杯状病毒的衣壳蛋白此前已被描述为一种能自我组装、具有高度免疫原性的递送平台。其显著诱导细胞免疫和体液免疫的能力可用于增强对展示在病毒样颗粒表面的低免疫原性外来抗原的免疫反应。尽管杯状病毒的衣壳蛋白序列存在差异，但它们具有相似的结构，带有可经基因改造以在cVLPs表面呈现外来表位的结构环。在此，基于诺如病毒（NoV）的VP1蛋白，我们研究了表位在P结构域不同结构环中的定位对所呈现表位免疫原性的影响。在本研究中，对NoV VP1蛋白的三个不同环进行了基因改造，以呈现由M2/NP表位串联重复组成的多价流感病毒表位。在昆虫细胞中产生了在不同定位呈现流感病毒保守表位的cVLPs，并用于免疫BALB/c小鼠。比较了接种疫苗小鼠血清中对流感表位的特异性反应，以确定外来表位的定位是否对免疫原性有影响。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/852ba0939131/fmicb-14-1111947-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/3b7bd1b1d4c5/fmicb-14-1111947-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/986a2ede04aa/fmicb-14-1111947-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/9d16c405c60d/fmicb-14-1111947-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/f0daddbfd895/fmicb-14-1111947-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/5b2e7480d8bb/fmicb-14-1111947-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/b0b30017ced9/fmicb-14-1111947-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/c8b9c4b85669/fmicb-14-1111947-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/852ba0939131/fmicb-14-1111947-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/3b7bd1b1d4c5/fmicb-14-1111947-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/986a2ede04aa/fmicb-14-1111947-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/9d16c405c60d/fmicb-14-1111947-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/f0daddbfd895/fmicb-14-1111947-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/5b2e7480d8bb/fmicb-14-1111947-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/b0b30017ced9/fmicb-14-1111947-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/c8b9c4b85669/fmicb-14-1111947-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/823b/10010390/852ba0939131/fmicb-14-1111947-g008.jpg

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