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Characterization of the structural modifications accompanying the loss of HBsAg particle immunogenicity

机译：伴随HBsAg颗粒免疫原性丧失的结构修饰的表征

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摘要

The aim of this work was to further understand the relationship between the immunogenicity and the structure of Hepatitis B surface antigen (HBsAg) particles used in Hepatitis B vaccines. To reach this aim, we compared by using a large range of techniques, the structure and properties of untreated particles with those of particles stored for 3 weeks at +60 degrees C, a treatment which resulted in a loss of HBsAg antigenicity (toward RF-1 mAb) and immunogenicity (in mice). While untreated particles imaged by electron microscopy and atomic force microscopy appeared as isolated nanoparticles of 20 nm, heated particles appeared as long chains of particle aggregates with a partial loss of their protein protrusions. Moreover, infrared spectroscopy and circular dichroism revealed that the secondary structure of the S proteins was significantly affected, with a loss of 10% of their a-helix content. Steady-state and time-resolved fluorescence data further revealed strong modifications of the most emitting Trp residues at the particle surface, confirming significant changes in the conformation of the S proteins. Moreover, modifications in the organization of both the lipid core and lipid membrane surface of the heated particles were evidenced by environment-sensitive 3-hydroxyflavone probes. Taken together, our data evidenced a clear relationship between the bona fide S protein structure and lipid organization notably at the particle surface and the particle immunogenicity
机译：这项工作的目的是进一步了解用于乙型肝炎疫苗的乙型肝炎表面抗原（HBsAg）颗粒的免疫原性与结构之间的关系。为了达到这个目标，我们使用了多种技术，将未经处理的颗粒的结构和性质与在+60摄氏度下储存3周的颗粒的结构和性质进行了比较，这种处理导致HBsAg抗原性降低（朝RF- 1 mAb）和免疫原性（小鼠）。通过电子显微镜和原子力显微镜成像的未处理颗粒表现为20 nm的分离纳米颗粒，而受热颗粒则表现为颗粒聚集体的长链，其蛋白质突出部分丢失。此外，红外光谱和圆二色性表明S蛋白的二级结构受到显着影响，其α-螺旋含量损失了10％。稳态和时间分辨的荧光数据进一步揭示了颗粒表面最发射Trp残基的强烈修饰，证实了S蛋白构象的重大变化。此外，通过环境敏感的3-羟基黄酮探针证明了加热颗粒的脂质核和脂质膜表面的组织都发生了改变。综上所述，我们的数据证明了真正的S蛋白结构与脂质组织之间存在明显的关系，尤其是在颗粒表面与颗粒免疫原性之间。

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