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

Abstract

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.

Receptor Binding Domain (RBD) Structural Susceptibility in the SARS-CoV-2 Virus Spike Protein Exposed to a Pulsed Electric Field

“…Theoretical reports have suggested that electric field intensities of at least 0.10 Vnm -1 can cause subtle movements of atoms within proteins and promote conformational changes [16]. Moreover, in previous work, we used 1.0 Vnm -1 to induce structural variations in other viral proteins [17]. Based on the previous statements, we initially disturbed RBD with stimulus 1, and after that, we used a second stimulus E 0 = 2.9 Vnm -1 with twice the intensity: ω = 300 ps -1 ( Table 1).…”