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A comparative analysis on the physicochemical properties of tick-borne encephalitis virus envelope protein residues that affect its antigenic properties

YS. Bukin, YP. Dzhioev, SE. Tkachev, IV. Kozlova, AI. Paramonov, D. Ruzek, Z. Qu, VI. Zlobin,

. 2017 ; 238 (-) : 124-132. [pub] 20170615

Jazyk angličtina Země Nizozemsko

Typ dokumentu časopisecké články, práce podpořená grantem

Perzistentní odkaz   https://www.medvik.cz/link/bmc18024925

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.

Citace poskytuje Crossref.org

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$a Bukin, Yu S $u Limnological Institute of the Siberian Branch of the Russian Academy of Sciences, Ulan- Batorskaya Str., 3, 664033 Irkutsk, Russia; Irkutsk National Research Technical University, Lermontov Str., 83, 664074 Irkutsk, Russia. Electronic address: bukinyura@mail.ru.
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$a 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.
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$a Dzhioev, Yu P $u Irkutsk State Medical University, Institute of Biomedical Technology, Irkutsk, Russia; Science Center of Family Health Problems and Human Reproduction, Irkutsk, Russia.
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$a Tkachev, S E $u Institute of Chemical Biology and Fundamental Medicine SB RAS, Novosibirsk, Russia.
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$a Kozlova, I V $u Science Center of Family Health Problems and Human Reproduction, Irkutsk, Russia.
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$a Růžek, Daniel, $u Faculty of Science, University of South Bohemia and Biology Centre, Institute of Parasitology, Czech Academy of Sciences, Branisovska 31, České Budějovice (Budweis) 37005, Czech Republic; Veterinary Research Institute, Hudcova 70, Brno 62100, Czech Republic. $d 1981- $7 stk2008441707
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$a Qu, Z $u Department of Microbiology, School of Public Health, Harbin Medical University, China; Department of Natural Focus Disease Control, Institute of Environment-Associated Disease, Sino-Russia Joint Medical Research Center, Harbin Medical University, China.
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