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携带风疹病毒E1糖蛋白主要表位的乙型肝炎病毒核心颗粒嵌合衍生物。

Chimeric derivatives of hepatitis B virus core particles carrying major epitopes of the rubella virus E1 glycoprotein.

作者信息

Skrastina Dace, Petrovskis Ivars, Petraityte Rasa, Sominskaya Irina, Ose Velta, Lieknina Ilva, Bogans Janis, Sasnauskas Kestutis, Pumpens Paul

机构信息

Latvian Biomedical Research and Study Centre, Riga, Latvia.

出版信息

Clin Vaccine Immunol. 2013 Nov;20(11):1719-28. doi: 10.1128/CVI.00533-13. Epub 2013 Sep 4.

DOI:10.1128/CVI.00533-13
PMID:24006140
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC3837786/
Abstract

Three variants of the major rubella virus (RV) E1 protein virus-neutralizing epitope from position 214 to 285 were exposed on the hepatitis B virus (HBV) C-terminally truncated core (HBcΔ) in a virus-like particle (VLP) vector and were produced in Escherichia coli. All three chimeras demonstrated VLPs in bacterial cell lysates, but only HBcΔ-E1(245-285) demonstrated the correct VLP structure after purification. The other chimeras, HBcΔ-E1(214-285) and HBcΔ-E1(214-240), appeared after purification as non-VLP aggregates of 100 to 900 nm in diameter according to dynamic light scattering data. All three variants possessed the intrinsic antigenic activity of RV E1, since they were recognized by natural human anti-RV E1 antibodies and induced an anti-RV E1 response in mice. HBcΔ-E1(214-240) and HBcΔ-E1(245-285) can be regarded as prototypes for a putative RV vaccine because they were able to induce antibodies recognizing natural RV E1 protein in RV diagnostic kits.

摘要

风疹病毒（RV）E1蛋白病毒中和表位214至285位的三个变体在乙型肝炎病毒（HBV）C端截短的核心（HBcΔ）上，以病毒样颗粒（VLP）载体形式呈现，并在大肠杆菌中产生。所有这三种嵌合体在细菌细胞裂解物中均显示出VLP，但只有HBcΔ-E1(245-285)在纯化后显示出正确的VLP结构。根据动态光散射数据，其他嵌合体HBcΔ-E1(214-285)和HBcΔ-E1(214-240)在纯化后呈现为直径100至900nm的非VLP聚集体。所有这三个变体都具有RV E1的固有抗原活性，因为它们能被天然人抗RV E1抗体识别，并在小鼠中诱导抗RV E1反应。HBcΔ-E1(214-240)和HBcΔ-E1(245-285)可被视为一种假定的RV疫苗的原型，因为它们能够诱导识别RV诊断试剂盒中天然RV E1蛋白的抗体。

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