Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization

The recent coronavirus disease 2019 (COVID-19) pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has spurred intense research efforts to develop new materials with antiviral activity. In this study, we genetically engineered amyloid-based nanofibrils for capturing a...

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Autores: Behbahanipour, Molood|||0000-0002-7889-6105, Navarro, Susanna|||0000-0001-8160-9536, Bárcenas, Oriol|||0000-0002-8439-4005, Garcia-Pardo, Javier|||0000-0001-9179-6371, Ventura, Salvador|||0000-0002-9652-6351
Formato: artículo
Fecha de publicación:2024
País:España
Recursos:Universitat Autònoma de Barcelona
Repositorio:Dipòsit Digital de Documents de la UAB
Idioma:inglés
OAI Identifier:oai:ddd.uab.cat:302294
Acesso em linha:https://ddd.uab.cat/record/302294
https://dx.doi.org/urn:doi:10.1016/j.jcis.2024.06.175
Access Level:acceso abierto
Palavra-chave:Amyloid Fibrils
Antiviral Biomaterials
Functional Polymers
SARS-CoV-2
Supramolecular Assemblies
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spelling Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralizationBehbahanipour, Molood|||0000-0002-7889-6105Navarro, Susanna|||0000-0001-8160-9536Bárcenas, Oriol|||0000-0002-8439-4005Garcia-Pardo, Javier|||0000-0001-9179-6371Ventura, Salvador|||0000-0002-9652-6351Amyloid FibrilsAntiviral BiomaterialsFunctional PolymersSARS-CoV-2Supramolecular AssembliesThe recent coronavirus disease 2019 (COVID-19) pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has spurred intense research efforts to develop new materials with antiviral activity. In this study, we genetically engineered amyloid-based nanofibrils for capturing and neutralizing SARS-CoV-2. Building upon the amyloid properties of a short Sup35 yeast prion sequence, we fused it to SARS-CoV-2 receptor-binding domain (RBD) capturing proteins, LCB1 and LCB3. By tuning the reaction conditions, we achieved the spontaneous self-assembly of the Sup35-LCB1 fusion protein into a highly homogeneous and well-dispersed amyloid-like fibrillar material. These nanofibrils exhibited high affinity for the SARS-CoV-2 RBD, effectively inhibiting its interaction with the angiotensin-converting enzyme 2 (ACE2) receptor, the primary entry point for the virus into host cells. We further demonstrate that this functional nanomaterial entraps and neutralizes SARS-CoV-2 virus-like particles (VLPs), with a potency comparable to that of therapeutic antibodies. As a proof of concept, we successfully fabricated patterned surfaces that selectively capture SARS-CoV-2 RBD protein on wet environments. Collectively, these findings suggest that these protein-only nanofibrils hold promise as disinfecting coatings endowed with selective SARS-CoV-2 neutralizing properties to combat viral spread or in the development of sensitive viral sampling and diagnostic tools. 22024-01-0120242024-01-01Articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://ddd.uab.cat/record/302294https://dx.doi.org/urn:doi:10.1016/j.jcis.2024.06.175reponame:Dipòsit Digital de Documents de la UABinstname:Universitat Autònoma de BarcelonaInglésengAgencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2022-137963OB-I00Ministerio de Ciencia e Innovación https://doi.org/10.13039/501100004837 IJC2019-041039-IMinisterio de Ciencia e Innovación https://doi.org/10.13039/501100004837 PRE2020-092634Ministerio de Ciencia, Innovación y Universidades https://doi.org/10.13039/100014440 FPU22/03656open accesshttp://purl.org/coar/access_right/c_abf2Aquest document està subjecte a una llicència d'ús Creative Commons. Es permet la reproducció total o parcial, la distribució, la comunicació pública de l'obra i la creació d'obres derivades, sempre que no sigui amb finalitats comercials, i sempre que es reconegui l'autoria de l'obra original.https://creativecommons.org/licenses/by-nc/4.0/info:eu-repo/semantics/openAccessoai:ddd.uab.cat:3022942026-06-06T12:50:31Z
dc.title.none.fl_str_mv Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
title Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
spellingShingle Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
Behbahanipour, Molood|||0000-0002-7889-6105
Amyloid Fibrils
Antiviral Biomaterials
Functional Polymers
SARS-CoV-2
Supramolecular Assemblies
title_short Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
title_full Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
title_fullStr Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
title_full_unstemmed Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
title_sort Bioengineered self-assembled nanofibrils for high-affinity SARS-CoV-2 capture and neutralization
dc.creator.none.fl_str_mv Behbahanipour, Molood|||0000-0002-7889-6105
Navarro, Susanna|||0000-0001-8160-9536
Bárcenas, Oriol|||0000-0002-8439-4005
Garcia-Pardo, Javier|||0000-0001-9179-6371
Ventura, Salvador|||0000-0002-9652-6351
author Behbahanipour, Molood|||0000-0002-7889-6105
author_facet Behbahanipour, Molood|||0000-0002-7889-6105
Navarro, Susanna|||0000-0001-8160-9536
Bárcenas, Oriol|||0000-0002-8439-4005
Garcia-Pardo, Javier|||0000-0001-9179-6371
Ventura, Salvador|||0000-0002-9652-6351
author_role author
author2 Navarro, Susanna|||0000-0001-8160-9536
Bárcenas, Oriol|||0000-0002-8439-4005
Garcia-Pardo, Javier|||0000-0001-9179-6371
Ventura, Salvador|||0000-0002-9652-6351
author2_role author
author
author
author
dc.subject.none.fl_str_mv Amyloid Fibrils
Antiviral Biomaterials
Functional Polymers
SARS-CoV-2
Supramolecular Assemblies
topic Amyloid Fibrils
Antiviral Biomaterials
Functional Polymers
SARS-CoV-2
Supramolecular Assemblies
description The recent coronavirus disease 2019 (COVID-19) pandemic caused by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) has spurred intense research efforts to develop new materials with antiviral activity. In this study, we genetically engineered amyloid-based nanofibrils for capturing and neutralizing SARS-CoV-2. Building upon the amyloid properties of a short Sup35 yeast prion sequence, we fused it to SARS-CoV-2 receptor-binding domain (RBD) capturing proteins, LCB1 and LCB3. By tuning the reaction conditions, we achieved the spontaneous self-assembly of the Sup35-LCB1 fusion protein into a highly homogeneous and well-dispersed amyloid-like fibrillar material. These nanofibrils exhibited high affinity for the SARS-CoV-2 RBD, effectively inhibiting its interaction with the angiotensin-converting enzyme 2 (ACE2) receptor, the primary entry point for the virus into host cells. We further demonstrate that this functional nanomaterial entraps and neutralizes SARS-CoV-2 virus-like particles (VLPs), with a potency comparable to that of therapeutic antibodies. As a proof of concept, we successfully fabricated patterned surfaces that selectively capture SARS-CoV-2 RBD protein on wet environments. Collectively, these findings suggest that these protein-only nanofibrils hold promise as disinfecting coatings endowed with selective SARS-CoV-2 neutralizing properties to combat viral spread or in the development of sensitive viral sampling and diagnostic tools.
publishDate 2024
dc.date.none.fl_str_mv 2
2024-01-01
2024
2024-01-01
dc.type.none.fl_str_mv Article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://ddd.uab.cat/record/302294
https://dx.doi.org/urn:doi:10.1016/j.jcis.2024.06.175
url https://ddd.uab.cat/record/302294
https://dx.doi.org/urn:doi:10.1016/j.jcis.2024.06.175
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Agencia Estatal de Investigación https://doi.org/10.13039/501100011033 PID2022-137963OB-I00
Ministerio de Ciencia e Innovación https://doi.org/10.13039/501100004837 IJC2019-041039-I
Ministerio de Ciencia e Innovación https://doi.org/10.13039/501100004837 PRE2020-092634
Ministerio de Ciencia, Innovación y Universidades https://doi.org/10.13039/100014440 FPU22/03656
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by-nc/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
https://creativecommons.org/licenses/by-nc/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.source.none.fl_str_mv reponame:Dipòsit Digital de Documents de la UAB
instname:Universitat Autònoma de Barcelona
instname_str Universitat Autònoma de Barcelona
reponame_str Dipòsit Digital de Documents de la UAB
collection Dipòsit Digital de Documents de la UAB
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repository.mail.fl_str_mv
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