Structural and Functional Aspects of G-Quadruplex Aptamers Which Bind a Broad Range of Influenza A Viruses

Novoseltseva, A.A.; Ivanov, N.M.; Novikov, R.A.; Tkachev, Y.V.; Bunin, D.A.; Gambaryan, A.S.; Tashlitsky, V.N.; Arutyunyan, A.M.; Kopylov, A.M.; Zavyalova, E.G.

Статья опубликована в высокорейтинговом журнале

Информация о цитировании статьи получена из Web of Science, Scopus
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 11 мая 2021 г.

Авторы: Novoseltseva Anastasia A., Ivanov Nikita M., Novikov Roman A., Tkachev Yaroslav V., Bunin Dmitry A., Gambaryan Alexandra S., Tashlitsky Vadim N., Arutyunyan Alexander M., Kopylov Alexey M., Zavyalova Elena G.
Журнал: Biomolecules
Том: 10
Номер: 1
Год издания: 2020
Издательство: MDPI
Местоположение издательства: Basel, Switzerland
Первая страница: 119
DOI: 10.3390/biom10010119
Аннотация: An aptamer is a synthetic oligonucleotide with a unique spatial structure that provides specific binding to a target. To date, several aptamers to hemagglutinin of the influenza A virus have been described, which vary in affinity and strain specificity. Among them, the DNA aptamer RHA0385 is able to recognize influenza hemagglutinins with highly variable sequences. In this paper, the structure of RHA0385 was studied by circular dichroism spectroscopy, nuclear magnetic resonance, and size‐exclusion chromatography, demonstrating the formation of a parallel G-quadruplex structure. Three derivatives of RHA0385 were designed in order to determine the contribution of the major loop to affinity. Shortening of the major loop from seven to three nucleotides led to stabilization of the scaffold. The affinities of the derivatives were studied by surface plasmon resonance and an enzyme‐linked aptamer assay on recombinant hemagglutinins and viral particles, respectively. The alterations in the loop affected the binding to influenza hemagglutinin, but did not abolish it. Contrary to aptamer RHA0385, two of the designed aptamers were shown to be conformationally homogeneous, retaining high affinities and broad binding abilities for both recombinant hemagglutinins and whole influenza A viruses.
Добавил в систему: Бизяева Анастасия Александровна

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Structural and Functional Aspects of G-Quadruplex Aptamers Which Bind a Broad Range of Influenza A Virusesстатья Исследовательская статья

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