Analysis of domain specificity of the protective chimeric antibody ch14D5a against glycoprotein e of tick-borne encephalitis virus

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Analysis of domain specificity of the protective chimeric antibody ch14D5a against glycoprotein e of tick-borne encephalitis virus. / Baykov, I. K.; Emelyanova, L. A.; Sokolova, L. M. et al.

In: Вавиловский журнал генетики и селекции, Vol. 22, No. 4, 01.01.2018, p. 459-467.

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Author

Baykov, I. K. ; Emelyanova, L. A. ; Sokolova, L. M. et al. / Analysis of domain specificity of the protective chimeric antibody ch14D5a against glycoprotein e of tick-borne encephalitis virus. In: Вавиловский журнал генетики и селекции. 2018 ; Vol. 22, No. 4. pp. 459-467.

BibTeX

@article{6d57fa3097454f1ab6fc8eba5dfbd1a9,

title = "Analysis of domain specificity of the protective chimeric antibody ch14D5a against glycoprotein e of tick-borne encephalitis virus",

abstract = "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.",

keywords = "Antibody, Domain D3, Epitope mapping, Glycoprotein E, Recombinant protein, Surface Plasmon resonance, Tick-borne encephalitis virus, antibody, NEUTRALIZING ANTIBODIES, recombinant protein, WEST-NILE-VIRUS, glycoprotein E, domain D3, epitope mapping, ENVELOPE-PROTEIN, RESPONSES, POTENT, EPITOPE, surface plasmon resonance, STRUCTURAL BASIS, FLAVIVIRUSES, ZIKA VIRUS, tick-borne encephalitis virus",

author = "Baykov, {I. K.} and Emelyanova, {L. A.} and Sokolova, {L. M.} and Karelina, {E. M.} and Matveev, {A. L.} and Babkin, {I. V.} and Khlusevich, {Ya A.} and Podgornyy, {V. F.} and Tikunova, {N. V.}",

year = "2018",

month = jan,

day = "1",

doi = "10.18699/VJ18.383",

language = "English",

volume = "22",

pages = "459--467",

journal = "Вавиловский журнал генетики и селекции",

issn = "2500-0462",

publisher = "Institute of Cytology and Genetics of Siberian Branch of the Russian Academy of Sciences",

number = "4",

}

RIS

TY - JOUR

T1 - Analysis of domain specificity of the protective chimeric antibody ch14D5a against glycoprotein e of tick-borne encephalitis virus

AU - Baykov, I. K.

AU - Emelyanova, L. A.

AU - Sokolova, L. M.

AU - Karelina, E. M.

AU - Matveev, A. L.

AU - Babkin, I. V.

AU - Khlusevich, Ya A.

AU - Podgornyy, V. F.

AU - Tikunova, N. V.

PY - 2018/1/1

Y1 - 2018/1/1

N2 - 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.

AB - 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.

KW - Antibody

KW - Domain D3

KW - Epitope mapping

KW - Glycoprotein E

KW - Recombinant protein

KW - Surface Plasmon resonance

KW - Tick-borne encephalitis virus

KW - antibody

KW - NEUTRALIZING ANTIBODIES

KW - recombinant protein

KW - WEST-NILE-VIRUS

KW - glycoprotein E

KW - domain D3

KW - epitope mapping

KW - ENVELOPE-PROTEIN

KW - RESPONSES

KW - POTENT

KW - EPITOPE

KW - surface plasmon resonance

KW - STRUCTURAL BASIS

KW - FLAVIVIRUSES

KW - ZIKA VIRUS

KW - tick-borne encephalitis virus

UR - http://www.scopus.com/inward/record.url?scp=85049400318&partnerID=8YFLogxK

U2 - 10.18699/VJ18.383

DO - 10.18699/VJ18.383

M3 - Article

AN - SCOPUS:85049400318

VL - 22

SP - 459

EP - 467

JO - Вавиловский журнал генетики и селекции

JF - Вавиловский журнал генетики и селекции

SN - 2500-0462

IS - 4

ER -

ID: 14882548