THE STUDY OF INFLUENZA VIRUS NEURAMINIDASE HYDRATION DEGREE
It is known that the functioning of many proteins and enzymes depends on the degree of hydration of their surfaces. In our studies, neuraminidase (NA) of influenza virus was selected as a model for surface antigenic viral protein. The Brunauer–Emmett–Teller (BET) model of adsorption was used to calc...
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| Format: | Article |
| Language: | Russian |
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Sankt-Peterburg : NIIÈM imeni Pastera
2018-01-01
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| Series: | Инфекция и иммунитет |
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| Online Access: | https://www.iimmun.ru/iimm/article/view/598 |
| _version_ | 1797972507410563072 |
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| author | N. S. Grebenkina N. A. Kontarov N. V. Yuminova |
| author_facet | N. S. Grebenkina N. A. Kontarov N. V. Yuminova |
| author_sort | N. S. Grebenkina |
| collection | DOAJ |
| description | It is known that the functioning of many proteins and enzymes depends on the degree of hydration of their surfaces. In our studies, neuraminidase (NA) of influenza virus was selected as a model for surface antigenic viral protein. The Brunauer–Emmett–Teller (BET) model of adsorption was used to calculate the values of water monolayer (am) at different values of water vapor pressure. The obtained BET isotherms allow for concluding that hysteresis takes place manifested by the difference between the monolayer am values for sorption and desorption of water from the surface of the enzyme, which is probably associated with a high degree of cooperation of the hydration shell formed. The maximum binding of water molecules was observed for the vapor pressure p/ps value of 0.65 and was am = 224 water molecules per a molecule of the enzyme. Basing on the calculated surface area of a NA tetramer (S = 256 nm2 ) and the maximum projection area of water molecule, it may be concluded that the entire surface of the enzyme is completely covered with a water monolayer. For said am value the maximum activity of NA was observed, whereas the minimum enzyme activity corresponded to the am value of 98 water molecules per a molecule of the enzyme, which corresponded to the water vapor pressure p/pS value of 0.38. Thus, for the influenza virus NA protein a dependency of the enzymatic activity on the degree of hydration of the surface of the enzyme is demonstrated. The dependence of immunogenicity of influenza virus from the extent of hydration of NA. |
| first_indexed | 2024-04-11T03:49:34Z |
| format | Article |
| id | doaj.art-42b22de4702e44b69734416c6b5d2560 |
| institution | Directory Open Access Journal |
| issn | 2220-7619 2313-7398 |
| language | Russian |
| last_indexed | 2024-04-11T03:49:34Z |
| publishDate | 2018-01-01 |
| publisher | Sankt-Peterburg : NIIÈM imeni Pastera |
| record_format | Article |
| series | Инфекция и иммунитет |
| spelling | doaj.art-42b22de4702e44b69734416c6b5d25602023-01-02T02:14:11ZrusSankt-Peterburg : NIIÈM imeni PasteraИнфекция и иммунитет2220-76192313-73982018-01-017440540810.15789/2220-7619-2017-4-405-408361THE STUDY OF INFLUENZA VIRUS NEURAMINIDASE HYDRATION DEGREEN. S. Grebenkina0N. A. Kontarov1N. V. Yuminova2I.I. Mechnikov Research Institute of Vaccines and Sera, MoscowI.I. Mechnikov Research Institute of Vaccines and Sera, MoscowI.I. Mechnikov Research Institute of Vaccines and Sera, MoscowIt is known that the functioning of many proteins and enzymes depends on the degree of hydration of their surfaces. In our studies, neuraminidase (NA) of influenza virus was selected as a model for surface antigenic viral protein. The Brunauer–Emmett–Teller (BET) model of adsorption was used to calculate the values of water monolayer (am) at different values of water vapor pressure. The obtained BET isotherms allow for concluding that hysteresis takes place manifested by the difference between the monolayer am values for sorption and desorption of water from the surface of the enzyme, which is probably associated with a high degree of cooperation of the hydration shell formed. The maximum binding of water molecules was observed for the vapor pressure p/ps value of 0.65 and was am = 224 water molecules per a molecule of the enzyme. Basing on the calculated surface area of a NA tetramer (S = 256 nm2 ) and the maximum projection area of water molecule, it may be concluded that the entire surface of the enzyme is completely covered with a water monolayer. For said am value the maximum activity of NA was observed, whereas the minimum enzyme activity corresponded to the am value of 98 water molecules per a molecule of the enzyme, which corresponded to the water vapor pressure p/pS value of 0.38. Thus, for the influenza virus NA protein a dependency of the enzymatic activity on the degree of hydration of the surface of the enzyme is demonstrated. The dependence of immunogenicity of influenza virus from the extent of hydration of NA.https://www.iimmun.ru/iimm/article/view/598hydration degreeneuraminidasebrunauer–emmett–teller adsorption modelimmunogenicity of influenza virus |
| spellingShingle | N. S. Grebenkina N. A. Kontarov N. V. Yuminova THE STUDY OF INFLUENZA VIRUS NEURAMINIDASE HYDRATION DEGREE Инфекция и иммунитет hydration degree neuraminidase brunauer–emmett–teller adsorption model immunogenicity of influenza virus |
| title | THE STUDY OF INFLUENZA VIRUS NEURAMINIDASE HYDRATION DEGREE |
| title_full | THE STUDY OF INFLUENZA VIRUS NEURAMINIDASE HYDRATION DEGREE |
| title_fullStr | THE STUDY OF INFLUENZA VIRUS NEURAMINIDASE HYDRATION DEGREE |
| title_full_unstemmed | THE STUDY OF INFLUENZA VIRUS NEURAMINIDASE HYDRATION DEGREE |
| title_short | THE STUDY OF INFLUENZA VIRUS NEURAMINIDASE HYDRATION DEGREE |
| title_sort | study of influenza virus neuraminidase hydration degree |
| topic | hydration degree neuraminidase brunauer–emmett–teller adsorption model immunogenicity of influenza virus |
| url | https://www.iimmun.ru/iimm/article/view/598 |
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