Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers
Nucleic acid aptamers specific to S-protein and its receptor binding domain (RBD) of SARS-CoV-2 (severe acute respiratory syndrome-related coronavirus 2) virions are of high interest as potential inhibitors of viral infection and recognizing elements in biosensors. Development of specific therapy an...
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| Format: | Article |
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MDPI AG
2022-01-01
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| Series: | International Journal of Molecular Sciences |
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| Online Access: | https://www.mdpi.com/1422-0067/23/1/557 |
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| author | Fedor Grabovenko Liudmila Nikiforova Bogdan Yanenko Andrey Ulitin Eugene Loktyushov Timofei Zatsepin Elena Zavyalova Maria Zvereva |
| author_facet | Fedor Grabovenko Liudmila Nikiforova Bogdan Yanenko Andrey Ulitin Eugene Loktyushov Timofei Zatsepin Elena Zavyalova Maria Zvereva |
| author_sort | Fedor Grabovenko |
| collection | DOAJ |
| description | Nucleic acid aptamers specific to S-protein and its receptor binding domain (RBD) of SARS-CoV-2 (severe acute respiratory syndrome-related coronavirus 2) virions are of high interest as potential inhibitors of viral infection and recognizing elements in biosensors. Development of specific therapy and biosensors is complicated by an emergence of new viral strains bearing amino acid substitutions and probable differences in glycosylation sites. Here, we studied affinity of a set of aptamers to two Wuhan-type RBD of S-protein expressed in Chinese hamster ovary cell line and <i>Pichia pastoris</i> that differ in glycosylation patterns. The expression system for the RBD protein has significant effects, both on values of dissociation constants and relative efficacy of the aptamer binding. We propose glycosylation of the RBD as the main force for observed differences. Moreover, affinity of a several aptamers was affected by a site of biotinylation. Thus, the robustness of modified aptamers toward new virus variants should be carefully tested. |
| first_indexed | 2024-03-10T03:37:17Z |
| format | Article |
| id | doaj.art-0beeea96d3e74047a5b2dd2a1e32cf00 |
| institution | Directory Open Access Journal |
| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-10T03:37:17Z |
| publishDate | 2022-01-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | International Journal of Molecular Sciences |
| spelling | doaj.art-0beeea96d3e74047a5b2dd2a1e32cf002023-11-23T11:41:49ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672022-01-0123155710.3390/ijms23010557Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA AptamersFedor Grabovenko0Liudmila Nikiforova1Bogdan Yanenko2Andrey Ulitin3Eugene Loktyushov4Timofei Zatsepin5Elena Zavyalova6Maria Zvereva7Chemistry Department, Moscow State University, 119991 Moscow, RussiaChemistry Department, Moscow State University, 119991 Moscow, RussiaBiogenec Joint-Stock Company, Moscow Region, 142290 Pushchino, RussiaBiogenec Joint-Stock Company, Moscow Region, 142290 Pushchino, RussiaBiogenec Joint-Stock Company, Moscow Region, 142290 Pushchino, RussiaChemistry Department, Moscow State University, 119991 Moscow, RussiaChemistry Department, Moscow State University, 119991 Moscow, RussiaChemistry Department, Moscow State University, 119991 Moscow, RussiaNucleic acid aptamers specific to S-protein and its receptor binding domain (RBD) of SARS-CoV-2 (severe acute respiratory syndrome-related coronavirus 2) virions are of high interest as potential inhibitors of viral infection and recognizing elements in biosensors. Development of specific therapy and biosensors is complicated by an emergence of new viral strains bearing amino acid substitutions and probable differences in glycosylation sites. Here, we studied affinity of a set of aptamers to two Wuhan-type RBD of S-protein expressed in Chinese hamster ovary cell line and <i>Pichia pastoris</i> that differ in glycosylation patterns. The expression system for the RBD protein has significant effects, both on values of dissociation constants and relative efficacy of the aptamer binding. We propose glycosylation of the RBD as the main force for observed differences. Moreover, affinity of a several aptamers was affected by a site of biotinylation. Thus, the robustness of modified aptamers toward new virus variants should be carefully tested.https://www.mdpi.com/1422-0067/23/1/557coronavirusSARS-CoV-2aptamersreceptor-binding domainspike glycoproteinbiolayer interferometry |
| spellingShingle | Fedor Grabovenko Liudmila Nikiforova Bogdan Yanenko Andrey Ulitin Eugene Loktyushov Timofei Zatsepin Elena Zavyalova Maria Zvereva Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers International Journal of Molecular Sciences coronavirus SARS-CoV-2 aptamers receptor-binding domain spike glycoprotein biolayer interferometry |
| title | Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers |
| title_full | Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers |
| title_fullStr | Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers |
| title_full_unstemmed | Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers |
| title_short | Glycosylation of Receptor Binding Domain of SARS-CoV-2 S-Protein Influences on Binding to Immobilized DNA Aptamers |
| title_sort | glycosylation of receptor binding domain of sars cov 2 s protein influences on binding to immobilized dna aptamers |
| topic | coronavirus SARS-CoV-2 aptamers receptor-binding domain spike glycoprotein biolayer interferometry |
| url | https://www.mdpi.com/1422-0067/23/1/557 |
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