The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody

I. K. Baykov; A. L. Matveev; L. A. Emelianova; G. B. Kaverina; S. E. Tkachev; N. V. Tikunova

doi:10.18699/VJ19.490

The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody

Переведенное название: Влияние различий в третьем домене гликопротеина Е вируса клещевого энцефалита дальневосточного, сибирского и европейского субтипов на связывание рекомбинантных белков D3 с химерным антителом

I. K. Baykov, A. L. Matveev, L. A. Emelianova, G. B. Kaverina, S. E. Tkachev, N. V. Tikunova

Результат исследования: Научные публикации в периодических изданиях › статья › рецензирование

1 Цитирования (Scopus)

Аннотация

Целью настоящей работы было исследование влияния различий аминокислотной последовательности рекомбинантных доменов D3 гликопротеина Е вируса клещевого энцефалита дальневосточного, Сибирского и европейского субтипов на связывание протективного антитела ch14D5 с этими белками. Методами вестерн-блот анализа и поверхностного плазмонного резонанса было показано, что наибольшее сродство (KD = 1.7 ± 0.5 нМ) антитело ch14D5 проявляет к домену D3 вируса клещевого энцефалита штамма «Софьин-Ru», принадлежащего к дальневосточному субтипу вируса. В то же время сродство к аналогичным белкам D3, полученным на основе штаммов «Заусаев», «1528-99» и «Абсеттаров» сибирского и европейского субтипов вируса клещевого энцефалита, оказалось заметно ниже (KD = 25 ± 4, 300 ± 50 и 250 ± 50 нМ соответственно). Кроме того, информация о пространственном расположении аминокислотных остатков, которыми отличаются полученные рекомбинантные белки, указывает на то, что узнаваемый антителом ch14D5 эпитоп находится в области бокового ребра домена D3 гликопротеина Е

Переведенное название	Влияние различий в третьем домене гликопротеина Е вируса клещевого энцефалита дальневосточного, сибирского и европейского субтипов на связывание рекомбинантных белков D3 с химерным антителом
Язык оригинала	английский
Страницы (с-по)	256-261
Число страниц	6
Журнал	Вавиловский журнал генетики и селекции
Том	23
Номер выпуска	3
DOI	https://doi.org/10.18699/VJ19.490
Состояние	Опубликовано - 1 янв 2019

Ключевые слова

Antibody
Domain D3
Epitope mapping
Glycoprotein E
Recombinant protein
Surface plasmon resonance
Tick-borne encephalitis virus

Предметные области OECD FOS+WOS

4 СЕЛЬСКОХОЗЯЙСТВЕННЫЕ НАУКИ
3 МЕДИЦИНСКИЕ НАУКИ И ЗДРАВООХРАНЕНИЕ
1.06 БИОЛОГИЧЕСКИЕ НАУКИ

ГРНТИ

34 БИОЛОГИЯ

Доступ к документу

10.18699/VJ19.490

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Подробные сведения о темах исследования «Влияние различий в третьем домене гликопротеина Е вируса клещевого энцефалита дальневосточного, сибирского и европейского субтипов на связывание рекомбинантных белков D3 с химерным антителом». Вместе они формируют уникальный семантический отпечаток (fingerprint).

Цитировать

Baykov, I. K., Matveev, A. L., Emelianova, L. A., Kaverina, G. B., Tkachev, S. E., & Tikunova, N. V. (2019). The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody. Вавиловский журнал генетики и селекции, 23(3), 256-261. https://doi.org/10.18699/VJ19.490

Baykov, I. K. ; Matveev, A. L. ; Emelianova, L. A. ; Kaverina, G. B. ; Tkachev, S. E. ; Tikunova, N. V. / The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody. В: Вавиловский журнал генетики и селекции. 2019 ; Том 23, № 3. стр. 256-261.

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title = "The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody",

abstract = "Currently, a therapeutic drug based on recombinant antibodies for the prevention and treatment of tick-borne encephalitis virus (TBEV) is developed in ICBFM SB RAS, and the chimeric antibody ch14D5 is considered as one of the key components of this drug. It was previously shown that this antibody is directed to the domain D3 of the glycoprotein E of TBEV. It was previously shown that this antibody is able to protect mice from the European subtype of TBEV, strain “Absettarov”, and the presence of virus-neutralizing activity against the Far Eastern subtype of TBEV, strain 205 was also shown for this antibody. However, it remains unclear whether this antibody exhibits selectivity for different subtypes of TBEV. The aim of this study was to investigate the effect of amino acid sequence differences of recombinant D3 domains derived from the glycoprotein E of TBEV of the Far Eastern, Siberian and European subtypes on the binding of the protective antibody ch14D5 to these proteins. Using Western blot analysis and surface plasmon resonance, it was shown that ch14D5 antibody has the highest affinity (KD = 1.7 ± 0.5 nM) for the D3 domain of the TBEV of the “Sofjin-Ru” strain belonging to the Far Eastern subtype of the virus. At the same time, the affinity of ch14D5 antibody for similar D3 proteins derived from “Zausaev”, “1528-99” and “Absettarov” strains of the Siberian and European subtypes of TBEV was noticeably lower (KD = 25 ± 4, 300 ± 50, 250 ± 50 nM, respectively). In addition, information about the spatial arrangement of amino acid residues that are different for the studied recombinant proteins indicates that the epitope recognized by the ch14D5 antibody is in close proximity to the lateral ridge of D3 domain of E glycoprotein.",

keywords = "Antibody, Domain D3, Epitope mapping, Glycoprotein E, Recombinant protein, Surface plasmon resonance, Tick-borne encephalitis virus, tick-borne encephalitis virus, glycoprotein E, domain D3, antibody, recombinant protein, surface plasmon resonance, epitope mapping, HUMANIZED MONOCLONAL-ANTIBODY, FLAVIVIRUSES",

author = "Baykov, {I. K.} and Matveev, {A. L.} and Emelianova, {L. A.} and Kaverina, {G. B.} and Tkachev, {S. E.} and Tikunova, {N. V.}",

year = "2019",

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doi = "10.18699/VJ19.490",

language = "English",

volume = "23",

pages = "256--261",

journal = "Вавиловский журнал генетики и селекции",

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number = "3",

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Baykov, IK, Matveev, AL, Emelianova, LA, Kaverina, GB, Tkachev, SE & Tikunova, NV 2019, 'The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody', Вавиловский журнал генетики и селекции, том. 23, № 3, стр. 256-261. https://doi.org/10.18699/VJ19.490

The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody. / Baykov, I. K.; Matveev, A. L.; Emelianova, L. A.; Kaverina, G. B.; Tkachev, S. E.; Tikunova, N. V.

В: Вавиловский журнал генетики и селекции, Том 23, № 3, 01.01.2019, стр. 256-261.

Результат исследования: Научные публикации в периодических изданиях › статья › рецензирование

TY - JOUR

T1 - The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody

AU - Baykov, I. K.

AU - Matveev, A. L.

AU - Emelianova, L. A.

AU - Kaverina, G. B.

AU - Tkachev, S. E.

AU - Tikunova, N. V.

PY - 2019/1/1

Y1 - 2019/1/1

N2 - Currently, a therapeutic drug based on recombinant antibodies for the prevention and treatment of tick-borne encephalitis virus (TBEV) is developed in ICBFM SB RAS, and the chimeric antibody ch14D5 is considered as one of the key components of this drug. It was previously shown that this antibody is directed to the domain D3 of the glycoprotein E of TBEV. It was previously shown that this antibody is able to protect mice from the European subtype of TBEV, strain “Absettarov”, and the presence of virus-neutralizing activity against the Far Eastern subtype of TBEV, strain 205 was also shown for this antibody. However, it remains unclear whether this antibody exhibits selectivity for different subtypes of TBEV. The aim of this study was to investigate the effect of amino acid sequence differences of recombinant D3 domains derived from the glycoprotein E of TBEV of the Far Eastern, Siberian and European subtypes on the binding of the protective antibody ch14D5 to these proteins. Using Western blot analysis and surface plasmon resonance, it was shown that ch14D5 antibody has the highest affinity (KD = 1.7 ± 0.5 nM) for the D3 domain of the TBEV of the “Sofjin-Ru” strain belonging to the Far Eastern subtype of the virus. At the same time, the affinity of ch14D5 antibody for similar D3 proteins derived from “Zausaev”, “1528-99” and “Absettarov” strains of the Siberian and European subtypes of TBEV was noticeably lower (KD = 25 ± 4, 300 ± 50, 250 ± 50 nM, respectively). In addition, information about the spatial arrangement of amino acid residues that are different for the studied recombinant proteins indicates that the epitope recognized by the ch14D5 antibody is in close proximity to the lateral ridge of D3 domain of E glycoprotein.

AB - Currently, a therapeutic drug based on recombinant antibodies for the prevention and treatment of tick-borne encephalitis virus (TBEV) is developed in ICBFM SB RAS, and the chimeric antibody ch14D5 is considered as one of the key components of this drug. It was previously shown that this antibody is directed to the domain D3 of the glycoprotein E of TBEV. It was previously shown that this antibody is able to protect mice from the European subtype of TBEV, strain “Absettarov”, and the presence of virus-neutralizing activity against the Far Eastern subtype of TBEV, strain 205 was also shown for this antibody. However, it remains unclear whether this antibody exhibits selectivity for different subtypes of TBEV. The aim of this study was to investigate the effect of amino acid sequence differences of recombinant D3 domains derived from the glycoprotein E of TBEV of the Far Eastern, Siberian and European subtypes on the binding of the protective antibody ch14D5 to these proteins. Using Western blot analysis and surface plasmon resonance, it was shown that ch14D5 antibody has the highest affinity (KD = 1.7 ± 0.5 nM) for the D3 domain of the TBEV of the “Sofjin-Ru” strain belonging to the Far Eastern subtype of the virus. At the same time, the affinity of ch14D5 antibody for similar D3 proteins derived from “Zausaev”, “1528-99” and “Absettarov” strains of the Siberian and European subtypes of TBEV was noticeably lower (KD = 25 ± 4, 300 ± 50, 250 ± 50 nM, respectively). In addition, information about the spatial arrangement of amino acid residues that are different for the studied recombinant proteins indicates that the epitope recognized by the ch14D5 antibody is in close proximity to the lateral ridge of D3 domain of E glycoprotein.

KW - Antibody

KW - Domain D3

KW - Epitope mapping

KW - Glycoprotein E

KW - Recombinant protein

KW - Surface plasmon resonance

KW - Tick-borne encephalitis virus

KW - tick-borne encephalitis virus

KW - glycoprotein E

KW - domain D3

KW - antibody

KW - recombinant protein

KW - surface plasmon resonance

KW - epitope mapping

KW - HUMANIZED MONOCLONAL-ANTIBODY

KW - FLAVIVIRUSES

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Baykov IK, Matveev AL, Emelianova LA, Kaverina GB, Tkachev SE, Tikunova NV. The effect of differences in the third domain of the glycoprotein E of tick-borne encephalitis virus of the Far Eastern, Siberian and European subtypes on the binding of recombinant D3 proteins with a chimeric antibody. Вавиловский журнал генетики и селекции. 2019 Янв. 1;23(3):256-261. https://doi.org/10.18699/VJ19.490