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Autoantibodies to heat shock protein 60, 70, and 90 are not altered in the anti-SARS-CoV-2 IgG-seropositive humans without or with mild symptoms
Cell Stress and Chaperones ( IF 3.8 ) Pub Date : 2021-06-02 , DOI: 10.1007/s12192-021-01215-3
Jagoda Mantej 1 , Marta Bednarek 1 , Krzysztof Sitko 1 , Marta Świętoń 1 , Stefan Tukaj 1
Affiliation  

Highly conserved heat shock proteins (Hsps) are localized in the cytoplasm and cellular organelles, and act as molecular chaperones or proteases. Members of Hsp families are released into the extracellular milieu under both normal and stress conditions. It is hypothesized that the severe acute respiratory syndrome corona virus 2 (SARS-CoV-2) has the potential to elicit autoimmunity due to molecular mimicry between human extracellular Hsps and immunogenic proteins of the virus. To confirm the above hypothesis, levels of circulating autoantibodies directed to the key human chaperones i.e., Hsp60, Hsp70, and Hsp90 in the anti-SARS-CoV-2 IgG-seropositive participants have been evaluated. Twenty-six healthy volunteers who got two doses of the mRNA vaccine encoding the viral spike protein, anti-SARS-CoV-2 IgG-positive participants (n = 15), and healthy naïve (anti-SARS-CoV-2 IgG-negative) volunteers (n = 51) have been included in this study. We found that the serum levels of anti-Hsp60, anti-Hsp70, and anti-Hsp90 autoantibodies of the IgG, IgM, or IgA isotype remained unchanged in either the anti-COVID-19-immunized humans or the anti-SARS-CoV-2 IgG-positive participants when compared to healthy naïve volunteers, as measured by enzyme-linked immunosorbent assay. Our results showing that the humoral immune response to SARS-CoV-2 did not include the production of anti-SARS-CoV-2 antibodies that also recognized extracellular heat shock protein 60, 70, and 90 represent a partial evaluation of the autoimmunity hypothesis stated above. Further testing for cell-based immunity will be necessary to fully evaluate this hypothesis.



中文翻译:

在没有或有轻微症状的抗 SARS-CoV-2 IgG 血清阳性人类中,针对热休克蛋白 60、70 和 90 的自身抗体没有改变

高度保守的热休克蛋白 (Hsps) 位于细胞质和细胞器中,充当分子伴侣或蛋白酶。Hsp 家族的成员在正常和压力条件下都会被释放到细胞外环境中。假设严重急性呼吸系统综合症冠状病毒 2 (SARS-CoV-2) 由于人类细胞外 Hsps 和病毒免疫原性蛋白之间的分子模拟,有可能引发自身免疫。为了证实上述假设,我们评估了抗 SARS-CoV-2 IgG 血清阳性参与者中针对关键人类伴侣蛋白(即 Hsp60、Hsp70 和 Hsp90)的循环自身抗体的水平。26 名健康志愿者接种了两剂编码病毒刺突蛋白的 mRNA 疫苗,抗 SARS-CoV-2 IgG 阳性参与者(n = 15),本研究包括健康的天真(抗 SARS-CoV-2 IgG 阴性)志愿者(n = 51)。我们发现 IgG、IgM 或 IgA 同种型的抗 Hsp60、抗 Hsp70 和抗 Hsp90 自身抗体的血清水平在抗 COVID-19 免疫的人或抗 SARS-CoV 中保持不变。 2 IgG 阳性参与者与健康的幼稚志愿者相比,通过酶联免疫吸附测定进行测量。我们的结果表明,对 SARS-CoV-2 的体液免疫反应不包括抗 SARS-CoV-2 抗体的产生,这些抗体也识别细胞外热休克蛋白 60、70 和 90,这代表了对自身免疫假说的部分评估。以上。需要进一步测试基于细胞的免疫力,以充分评估这一假设。

更新日期:2021-06-03
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