Aptamer-Hytac Chimeras for Targeted Degradation of SARS-CoV-2 Spike-1

The development of novel tools to tackle viral processes has become a central focus in global health, during the COVID-19 pandemic. The spike protein is currently one of the main SARS-CoV-2 targets, owing to its key roles in infectivity and virion formation. In this context, exploring innovative str...

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Main Authors: Carme Fàbrega, Núria Gallisà-Suñé, Alice Zuin, Juan Sebastián Ruíz, Bernat Coll-Martínez, Gemma Fabriàs, Ramon Eritja, Bernat Crosas
Format: Article
Language:English
Published: MDPI AG 2024-10-01
Series:Cells
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Online Access:https://www.mdpi.com/2073-4409/13/21/1767
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author Carme Fàbrega
Núria Gallisà-Suñé
Alice Zuin
Juan Sebastián Ruíz
Bernat Coll-Martínez
Gemma Fabriàs
Ramon Eritja
Bernat Crosas
author_facet Carme Fàbrega
Núria Gallisà-Suñé
Alice Zuin
Juan Sebastián Ruíz
Bernat Coll-Martínez
Gemma Fabriàs
Ramon Eritja
Bernat Crosas
author_sort Carme Fàbrega
collection DOAJ
description The development of novel tools to tackle viral processes has become a central focus in global health, during the COVID-19 pandemic. The spike protein is currently one of the main SARS-CoV-2 targets, owing to its key roles in infectivity and virion formation. In this context, exploring innovative strategies to block the activity of essential factors of SARS-CoV-2, such as spike proteins, will strengthen the capacity to respond to current and future threats. In the present work, we developed and tested novel bispecific molecules that encompass: (i) oligonucleotide aptamers S901 and S702, which bind to the spike protein through its S1 domain, and (ii) hydrophobic tags, such as adamantane and tert-butyl-carbamate-based ligands. Hydrophobic tags have the capacity to trigger the degradation of targets recruited in the context of a proteolytic chimera by activating quality control pathways. We observed that S901-adamantyl conjugates promote the degradation of the S1 spike domain, stably expressed in human cells by genomic insertion. These results highlight the suitability of aptamers as target-recognition molecules and the robustness of protein quality control pathways triggered by hydrophobic signals, and place aptamer-Hytacs as promising tools for counteracting coronavirus progression in human cells.
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institution Kabale University
issn 2073-4409
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publishDate 2024-10-01
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spelling doaj-art-00d1b154c83841d2a3310f94588a1da22024-11-08T14:34:26ZengMDPI AGCells2073-44092024-10-011321176710.3390/cells13211767Aptamer-Hytac Chimeras for Targeted Degradation of SARS-CoV-2 Spike-1Carme Fàbrega0Núria Gallisà-Suñé1Alice Zuin2Juan Sebastián Ruíz3Bernat Coll-Martínez4Gemma Fabriàs5Ramon Eritja6Bernat Crosas7Department of Surfactants and Nanobiotechnology, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Jordi Girona 18, 08034 Barcelona, SpainProteasome Regulation Lab, Department of Cells and Tissues, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri i Reixac 4, 08028 Barcelona, SpainProteasome Regulation Lab, Department of Cells and Tissues, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri i Reixac 4, 08028 Barcelona, SpainLincbiotech SL, Avenida do Mestre Mateo, 2, 15706 Santiago de Compostela, SpainProteasome Regulation Lab, Department of Cells and Tissues, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri i Reixac 4, 08028 Barcelona, SpainDepartment of Biological Chemistry, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Jordi Girona 18, 08034 Barcelona, SpainDepartment of Surfactants and Nanobiotechnology, Institute for Advanced Chemistry of Catalonia (IQAC-CSIC), Jordi Girona 18, 08034 Barcelona, SpainProteasome Regulation Lab, Department of Cells and Tissues, Molecular Biology Institute of Barcelona (IBMB-CSIC), Baldiri i Reixac 4, 08028 Barcelona, SpainThe development of novel tools to tackle viral processes has become a central focus in global health, during the COVID-19 pandemic. The spike protein is currently one of the main SARS-CoV-2 targets, owing to its key roles in infectivity and virion formation. In this context, exploring innovative strategies to block the activity of essential factors of SARS-CoV-2, such as spike proteins, will strengthen the capacity to respond to current and future threats. In the present work, we developed and tested novel bispecific molecules that encompass: (i) oligonucleotide aptamers S901 and S702, which bind to the spike protein through its S1 domain, and (ii) hydrophobic tags, such as adamantane and tert-butyl-carbamate-based ligands. Hydrophobic tags have the capacity to trigger the degradation of targets recruited in the context of a proteolytic chimera by activating quality control pathways. We observed that S901-adamantyl conjugates promote the degradation of the S1 spike domain, stably expressed in human cells by genomic insertion. These results highlight the suitability of aptamers as target-recognition molecules and the robustness of protein quality control pathways triggered by hydrophobic signals, and place aptamer-Hytacs as promising tools for counteracting coronavirus progression in human cells.https://www.mdpi.com/2073-4409/13/21/1767coronavirusSARS-CoV-2spike proteinaptameroligonucleotideadamantyl
spellingShingle Carme Fàbrega
Núria Gallisà-Suñé
Alice Zuin
Juan Sebastián Ruíz
Bernat Coll-Martínez
Gemma Fabriàs
Ramon Eritja
Bernat Crosas
Aptamer-Hytac Chimeras for Targeted Degradation of SARS-CoV-2 Spike-1
Cells
coronavirus
SARS-CoV-2
spike protein
aptamer
oligonucleotide
adamantyl
title Aptamer-Hytac Chimeras for Targeted Degradation of SARS-CoV-2 Spike-1
title_full Aptamer-Hytac Chimeras for Targeted Degradation of SARS-CoV-2 Spike-1
title_fullStr Aptamer-Hytac Chimeras for Targeted Degradation of SARS-CoV-2 Spike-1
title_full_unstemmed Aptamer-Hytac Chimeras for Targeted Degradation of SARS-CoV-2 Spike-1
title_short Aptamer-Hytac Chimeras for Targeted Degradation of SARS-CoV-2 Spike-1
title_sort aptamer hytac chimeras for targeted degradation of sars cov 2 spike 1
topic coronavirus
SARS-CoV-2
spike protein
aptamer
oligonucleotide
adamantyl
url https://www.mdpi.com/2073-4409/13/21/1767
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