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首页> 外文期刊>Journal of Nuclear Physics, Material Sciences, Radiation and Applications >Structural Variations Induced by Temperature Changes in Rotavirus VP6 Protein Immersed in an Electric Field and Their Effects on Epitopes of The Region 300-396
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Structural Variations Induced by Temperature Changes in Rotavirus VP6 Protein Immersed in an Electric Field and Their Effects on Epitopes of The Region 300-396

机译：轮状病毒VP6蛋白浸入电场中温度变化引起的结构变异及其对300-396区表位的影响

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Rotavirus diarrhea is an infectious intestinal disease that causes about 215 thousand deaths annually in infants under five years old. This virus is formed by three layers of concentric proteins that envelop its genome, from which VP6 structural protein is the most conserved among rotavirus serotypes and an excellent vaccine candidate. Recent studies have shown that structural proteins are susceptible to losing their biological function when their conformation is modified by moderate temperature increments, and in the case of VP6, its antigen efficiency decreases. We performed an in silicoanalysis to identify the structural variations in the epitopes 301-315, 357-366, and 376-384 of the rotavirus VP6 protein -in a hydrated medium- when the temperature is increased from 310 K to 322 K. In the latter state, we applied an electric field equivalent to a low energy laser pulse and calculated the fluctuations per amino acid residue. We identified that the region 301-315 has greater flexibility and density of negative electrical charge; nevertheless, at 322 K it experiences a sudden change of secondary structure that could decrease its efficiency as an antigenic determinant. The applied electric field induces electrical neutrality in the region 357-366, whereas in 376-384 inverts the charge, implying that temperature changes in the range 310 K-322 K are a factor that promotes thermoelectric effects in the VP6 protein epitopes in the region 300-396.
机译：轮状病毒腹泻是一种传染性肠道疾病，每年在5岁以下的婴儿中造成约215,000例死亡。该病毒由包裹其基因组的三层同心蛋白形成，在轮状病毒血清型中，VP6结构蛋白是其中最保守的，并且是优秀的候选疫苗。最近的研究表明，结构蛋白通过适度的温度升高对其构象进行修饰时，很容易丧失其生物学功能，而在VP6的情况下，其抗原效率会降低。当温度从310 K升高到322 K时，我们进行了计算机分析，以鉴定轮状病毒VP6蛋白的表位301-315、357-366和376-384（在水合介质中）的结构变异。在后一种状态下，我们施加了等效于低能量激光脉冲的电场，并计算了每个氨基酸残基的波动。我们发现，区域301-315具有更大的柔性和负电荷密度。然而，在322 K时，它经历了二级结构的突然变化，这可能会降低其作为抗原决定簇的效率。施加的电场在区域357-366中感应出电中性，而在376-384中则使电荷反转，这意味着温度在310 K-322 K范围内变化是促进该区域VP6蛋白表位热电效应的因素。 300-396。

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