A comparative analysis on the physicochemical properties of tick-borne encephalitis virus envelope protein residues that affect its antigenic properties
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60076658%3A12310%2F17%3A43895762" target="_blank" >RIV/60076658:12310/17:43895762 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/60077344:_____/17:00478919 RIV/00027162:_____/17:N0000087
Výsledek na webu
<a href="https://ac.els-cdn.com/S0168170217301090/1-s2.0-S0168170217301090-main.pdf?_tid=9e6a6af2-f9cf-11e7-8490-00000aab0f27&acdnat=1516005757_fba3feb43dacde3e6953a9cefea0033b" target="_blank" >https://ac.els-cdn.com/S0168170217301090/1-s2.0-S0168170217301090-main.pdf?_tid=9e6a6af2-f9cf-11e7-8490-00000aab0f27&acdnat=1516005757_fba3feb43dacde3e6953a9cefea0033b</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.virusres.2017.06.006" target="_blank" >10.1016/j.virusres.2017.06.006</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
A comparative analysis on the physicochemical properties of tick-borne encephalitis virus envelope protein residues that affect its antigenic properties
Popis výsledku v původním jazyce
This work is dedicated to the study of the variability of the main antigenic envelope protein E among different strains of tick-borne encephalitis virus at the level of physical and chemical properties of the amino acid residues. E protein variants were extracted from then NCBI database. Four amino acid residues properties in the polypeptide sequences were investigated: the average volume of the amino acid residue in the protein tertiary structure, the number of amino acid residue hydrogen bond donors, the charge of amino acid residue lateral radical and the dipole moment of the amino acid residue. These physico-chemical properties are involved in antigen-antibody interactions. As a result, 103 different variants of the antigenic determinants of the tick-borne encephalitis virus E protein were found, significantly different by physical and chemical properties of the amino acid residues in their structure. This means that some strains among the natural variants of tick-borne encephalitis virus can potentially escape the immune response induced by the standard vaccine.
Název v anglickém jazyce
A comparative analysis on the physicochemical properties of tick-borne encephalitis virus envelope protein residues that affect its antigenic properties
Popis výsledku anglicky
This work is dedicated to the study of the variability of the main antigenic envelope protein E among different strains of tick-borne encephalitis virus at the level of physical and chemical properties of the amino acid residues. E protein variants were extracted from then NCBI database. Four amino acid residues properties in the polypeptide sequences were investigated: the average volume of the amino acid residue in the protein tertiary structure, the number of amino acid residue hydrogen bond donors, the charge of amino acid residue lateral radical and the dipole moment of the amino acid residue. These physico-chemical properties are involved in antigen-antibody interactions. As a result, 103 different variants of the antigenic determinants of the tick-borne encephalitis virus E protein were found, significantly different by physical and chemical properties of the amino acid residues in their structure. This means that some strains among the natural variants of tick-borne encephalitis virus can potentially escape the immune response induced by the standard vaccine.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10607 - Virology
Návaznosti výsledku
Projekt
—
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2017
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Virus Research
ISSN
0168-1702
e-ISSN
—
Svazek periodika
238
Číslo periodika v rámci svazku
JUN 15 2017
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
9
Strana od-do
124-132
Kód UT WoS článku
000408077500017
EID výsledku v databázi Scopus
—