Резюме. Вакцинопрофилактика эпидемического паротита в РФ проводится с 1981 г. Иммунизация населения позволила в более чем в 600 раз снизить заболеваемость по сравнению с довакцинальным периодом, облегчить течение болезни, ликвидировать смертность. Иммунизация населения России осуществляется отечественной моно-и дивакциной из штамма Л-3. Вакцинация и ревакцинация против эпидемического паротита безопасна и высоко эффективна.
Polyelectrolytes currently play an increasingly important role in antivirus therapy. Antiviral activity towards influenza virus, measles virus, herpes simplex virus type 1, and cytomegalovirus was demonstrated for the 6000 Da polyelectrolyte polyallylamine. A nontoxic polyallylamine concentration of 30 μM at which the compound retains its antiviral effect towards measles and influenza viruses but lacks any toxic effect on human cells was previously determined. It is well known, at the same time, that simultaneous virus exposure to physical environmental factors and chemical substances causes a more significant decrease in virus infectivity. Temperature is among these physical factors since thermal exposure causes virus inactivation. Analysis of virus thermal inactivation parameters is of high practical importance when it comes to the development of vaccines against influenza virus and to the study of how virus particles infectivity decreases on various surfaces. In this view, the study of kinetic and thermodynamical characteristics of influenza virus thermal inactivation in the presence of the antiviral preparation polyallylanime is of particular interest. The paper reports that thermal inactivation of influenza virus in the temperature range of 38-60°C in the presence of polyallylamine follows the first-order reaction kinetics. Thermodynamic parameters of influenza virus thermal inactivation evidence that influenza virus surface proteins are involved in the inactivation process as a result of their interaction with polyallylamine. The obtained results show that polyallylamine may be used to accelerate thermal inactivation of the influenza virus.
The study of interaction between surface viral proteins and model phospholipids is important for learning more details about the mechanisms of viral penetration into cells during infection. In this context, liposomes represent suitable systems for modeling a cell membrane. The binding of hemagglutinin (HA) of influenza virus with phosphatidylcholine liposomes was studied by equilibrium adsorption. It was interesting elucidate changes occurring in the structure of a protein during its translocation from the surface into the interior part of the membrane. In this work, we have studied characteristics of the protein-lipid interaction during HA complex formation with phospholipids including adsorption of HA on a phospholipid bilayer. Using the Scatchard equation and the Gibbs-Helmholtz equation at pH 4.0 and pH 6.0 thermodynamic parameters were determined. The results concluded the hydrophobic type of interaction between viral protein and liposomes. The additional confirmation of hydrophobic protein-lipid interaction presence was determination of HA distribution constants in two-phase systems: dextran-polyethylene glycol (K1) and dextran-polyethylene glycol esterified with palmitic acid (K2). The presence of hydrophobic interaction between HA and the liposome membrane was also confirmed using the quenching method of intrinsic protein fluorescence by a neutral quencher with acrylamide. At pH 4.0, an increase in the Stern-Volmer quenching constant was observed for the HA+liposome from phosphatidylcholine system, which is caused by structural changes in HA upon incorporation into the liposome bilayer. The fluorescence quenching rate constants calculated using the Stern-Volmer equation indicate a static quenching mechanism in which the quencher interacts with fluophors of a stationary protein molecule. The obtained results are interesting for not only studying virus and cell fusion theoretically, but also have practical applications. Using values of the protein-bilayer binding constant and free energy constant, it is possible to select the optimal phospholipid composition of liposomes or virosomes to obtain a stronger complex with various viral proteins. With two-phase systems, it is possible to determine the presence of hydrophobic sites on the viral protein surface, which can be used for evaluation both protein-lipid and protein-protein interaction.
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