ANALYSIS OF DOMAIN SPECIFICITY OF THE PROTECTIVE CHIMERIC ANTIBODY ch14D5a AGAINST GLYCOPROTEIN E OF TICK-BORNE ENCEPHALITIS VIRUS
A drug for the prevention and therapy of tick-borne encephalitis virus is being developed on the basis of the protective chimeric antibody ch14D5a. At the same time, the epitope recognized by this antibody on the surface of glycoprotein E has not been localized yet. The aim of this work was to ident...
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| Format: | Article |
| Language: | English |
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Siberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and Breeders
2018-07-01
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| Series: | Вавиловский журнал генетики и селекции |
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| Online Access: | https://vavilov.elpub.ru/jour/article/view/1550 |
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| author | I. K. Baykov L. A. Emelyanova L. M. Sokolova E. M. Karelina A. L. Matveev I. V. Babkin Ya. А. Khlusevich V. F. Podgornyy N. V. Tikunova |
| author_facet | I. K. Baykov L. A. Emelyanova L. M. Sokolova E. M. Karelina A. L. Matveev I. V. Babkin Ya. А. Khlusevich V. F. Podgornyy N. V. Tikunova |
| author_sort | I. K. Baykov |
| collection | DOAJ |
| description | A drug for the prevention and therapy of tick-borne encephalitis virus is being developed on the basis of the protective chimeric antibody ch14D5a. At the same time, the epitope recognized by this antibody on the surface of glycoprotein E has not been localized yet. The aim of this work was to identify the domain of glycoprotein E, to which the protective antibody ch14D5a binds. As a result, four recombinant variants of glycoprotein E were generated using the bacterial expression system: (1) the rE protein containing the domains D1, D2, and D3 of glycoprotein E; (2) the rED1+2 protein containing domains D1 and D2; (3) the rED3_301 protein, which is domain D3 of glycoprotein E, and (4) the rED3_294 protein comprising domain D3 and a hinge region connecting domains D1 and D3. The rED3_294 and rED3_301 proteins were obtained in soluble monomeric form. The rE and rED1+2 proteins were extracted from the inclusion bodies of Escherichia coli. Using Western blot analysis and surface plasmon resonance analysis, it was demonstrated that the protective chimeric antibody ch14D5a and its Fab fragment bound specifically to domain D3 of glycoprotein E. Since the antibodies recognizing epitopes on the surface of domain D3 do not tend to cause antibody-dependent enhancement of the infection as compared to antibodies directed to domains D1 and D2, the data obtained confirm the promise of using the antibody ch14D5a in the development of a therapeutic preparation against the tick-borne encephalitis virus. |
| format | Article |
| id | doaj-art-50d47b2dc19f498881a6d2e68f6af7d3 |
| institution | Kabale University |
| issn | 2500-3259 |
| language | English |
| publishDate | 2018-07-01 |
| publisher | Siberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and Breeders |
| record_format | Article |
| series | Вавиловский журнал генетики и селекции |
| spelling | doaj-art-50d47b2dc19f498881a6d2e68f6af7d32025-02-01T09:58:06ZengSiberian Branch of the Russian Academy of Sciences, Federal Research Center Institute of Cytology and Genetics, The Vavilov Society of Geneticists and BreedersВавиловский журнал генетики и селекции2500-32592018-07-0122445946710.18699/VJ18.383778ANALYSIS OF DOMAIN SPECIFICITY OF THE PROTECTIVE CHIMERIC ANTIBODY ch14D5a AGAINST GLYCOPROTEIN E OF TICK-BORNE ENCEPHALITIS VIRUSI. K. Baykov0L. A. Emelyanova1L. M. Sokolova2E. M. Karelina3A. L. Matveev4I. V. Babkin5Ya. А. Khlusevich6V. F. Podgornyy7N. V. Tikunova8Institute of Сhemical Biology аnd Fundamental Medicine SB RASInstitute of Сhemical Biology аnd Fundamental Medicine SB RAS; Novosibirsk State UniversityInstitute of Сhemical Biology аnd Fundamental Medicine SB RASInstitute of Сhemical Biology аnd Fundamental Medicine SB RAS; Novosibirsk State UniversityInstitute of Сhemical Biology аnd Fundamental Medicine SB RAS; Novosibirsk State UniversityInstitute of Сhemical Biology аnd Fundamental Medicine SB RAS; Novosibirsk State UniversityInstitute of Сhemical Biology аnd Fundamental Medicine SB RAS; Novosibirsk State UniversityInstitute of Сhemical Biology аnd Fundamental Medicine SB RASInstitute of Сhemical Biology аnd Fundamental Medicine SB RAS; Novosibirsk State UniversityA drug for the prevention and therapy of tick-borne encephalitis virus is being developed on the basis of the protective chimeric antibody ch14D5a. At the same time, the epitope recognized by this antibody on the surface of glycoprotein E has not been localized yet. The aim of this work was to identify the domain of glycoprotein E, to which the protective antibody ch14D5a binds. As a result, four recombinant variants of glycoprotein E were generated using the bacterial expression system: (1) the rE protein containing the domains D1, D2, and D3 of glycoprotein E; (2) the rED1+2 protein containing domains D1 and D2; (3) the rED3_301 protein, which is domain D3 of glycoprotein E, and (4) the rED3_294 protein comprising domain D3 and a hinge region connecting domains D1 and D3. The rED3_294 and rED3_301 proteins were obtained in soluble monomeric form. The rE and rED1+2 proteins were extracted from the inclusion bodies of Escherichia coli. Using Western blot analysis and surface plasmon resonance analysis, it was demonstrated that the protective chimeric antibody ch14D5a and its Fab fragment bound specifically to domain D3 of glycoprotein E. Since the antibodies recognizing epitopes on the surface of domain D3 do not tend to cause antibody-dependent enhancement of the infection as compared to antibodies directed to domains D1 and D2, the data obtained confirm the promise of using the antibody ch14D5a in the development of a therapeutic preparation against the tick-borne encephalitis virus.https://vavilov.elpub.ru/jour/article/view/1550tick-borne encephalitis virusglycoprotein edomain d3antibodyrecombinant proteinsurface plasmon resonanceepitope mapping |
| spellingShingle | I. K. Baykov L. A. Emelyanova L. M. Sokolova E. M. Karelina A. L. Matveev I. V. Babkin Ya. А. Khlusevich V. F. Podgornyy N. V. Tikunova ANALYSIS OF DOMAIN SPECIFICITY OF THE PROTECTIVE CHIMERIC ANTIBODY ch14D5a AGAINST GLYCOPROTEIN E OF TICK-BORNE ENCEPHALITIS VIRUS Вавиловский журнал генетики и селекции tick-borne encephalitis virus glycoprotein e domain d3 antibody recombinant protein surface plasmon resonance epitope mapping |
| title | ANALYSIS OF DOMAIN SPECIFICITY OF THE PROTECTIVE CHIMERIC ANTIBODY ch14D5a AGAINST GLYCOPROTEIN E OF TICK-BORNE ENCEPHALITIS VIRUS |
| title_full | ANALYSIS OF DOMAIN SPECIFICITY OF THE PROTECTIVE CHIMERIC ANTIBODY ch14D5a AGAINST GLYCOPROTEIN E OF TICK-BORNE ENCEPHALITIS VIRUS |
| title_fullStr | ANALYSIS OF DOMAIN SPECIFICITY OF THE PROTECTIVE CHIMERIC ANTIBODY ch14D5a AGAINST GLYCOPROTEIN E OF TICK-BORNE ENCEPHALITIS VIRUS |
| title_full_unstemmed | ANALYSIS OF DOMAIN SPECIFICITY OF THE PROTECTIVE CHIMERIC ANTIBODY ch14D5a AGAINST GLYCOPROTEIN E OF TICK-BORNE ENCEPHALITIS VIRUS |
| title_short | ANALYSIS OF DOMAIN SPECIFICITY OF THE PROTECTIVE CHIMERIC ANTIBODY ch14D5a AGAINST GLYCOPROTEIN E OF TICK-BORNE ENCEPHALITIS VIRUS |
| title_sort | analysis of domain specificity of the protective chimeric antibody ch14d5a against glycoprotein e of tick borne encephalitis virus |
| topic | tick-borne encephalitis virus glycoprotein e domain d3 antibody recombinant protein surface plasmon resonance epitope mapping |
| url | https://vavilov.elpub.ru/jour/article/view/1550 |
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