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人轮状病毒 VP6 特异性抗体通过与转录孔中的四级结构结合介导细胞内中和。

Human rotavirus VP6-specific antibodies mediate intracellular neutralization by binding to a quaternary structure in the transcriptional pore.

机构信息

Department of Pathology, Microbiology and Immunology, Vanderbilt Medical Center, Nashville, Tennessee, USA.

出版信息

PLoS One. 2013 May 9;8(5):e61101. doi: 10.1371/journal.pone.0061101. Print 2013.

DOI:10.1371/journal.pone.0061101
PMID:23671563
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3650007/
Abstract

Several live attenuated rotavirus (RV) vaccines have been licensed, but the mechanisms of protective immunity are still poorly understood. The most frequent human B cell response is directed to the internal protein VP6 on the surface of double-layered particles, which is normally exposed only in the intracellular environment. Here, we show that the canonical VP6 antibodies secreted by humans bind to such particles and inhibit viral transcription. Polymeric IgA RV antibodies mediated an inhibitory effect against virus replication inside cells during IgA transcytosis. We defined the recognition site on VP6 as a quaternary epitope containing a high density of charged residues. RV human mAbs appear to bind to a negatively-charged patch on the surface of the Type I channel in the transcriptionally active particle, and they sterically block the channel. This unique mucosal mechanism of viral neutralization, which is not apparent from conventional immunoassays, may contribute significantly to human immunity to RV.

摘要

几种减毒轮状病毒 (RV) 疫苗已获得许可，但保护免疫的机制仍知之甚少。人类最常见的 B 细胞反应是针对双层颗粒表面的内部蛋白 VP6，该蛋白通常仅在细胞内环境中暴露。在这里，我们表明，人类分泌的典型 VP6 抗体与这些颗粒结合并抑制病毒转录。聚合 IgA RV 抗体在 IgA 穿越细胞时介导针对细胞内病毒复制的抑制作用。我们将 VP6 上的识别位点定义为包含高密度带电荷残基的四级表位。RV 人源单抗似乎与转录活跃颗粒中 I 型通道表面的带负电荷的斑块结合，并在空间上阻断该通道。这种独特的黏膜中和病毒的机制在常规免疫测定中并不明显，可能对人类对 RV 的免疫力有重要贡献。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/6b5022e82203/pone.0061101.g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/431daf804b33/pone.0061101.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/1bb81aa93042/pone.0061101.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/d84ab1ee78b9/pone.0061101.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/c18e14cbc389/pone.0061101.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/a4851344a868/pone.0061101.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/435491705f8b/pone.0061101.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/6b5022e82203/pone.0061101.g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/431daf804b33/pone.0061101.g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/1bb81aa93042/pone.0061101.g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/d84ab1ee78b9/pone.0061101.g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/c18e14cbc389/pone.0061101.g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/a4851344a868/pone.0061101.g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/435491705f8b/pone.0061101.g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/7bb4/3650007/6b5022e82203/pone.0061101.g007.jpg

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