Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif
- Autores
- Lorenzo Lopez, Juan Ramiro; Defelipe, Lucas Alfredo; Aliperti Car, Lucio; Niebling, Stephan; Custódio, Tânia F.; Löw, Christian; Schwarz, Jennifer J.; Remans, Kim; Craig, Patricio Oliver; Otero, Lisandro Horacio; Klinke, Sebastian; García Alai, María; Sánchez Miguel, Ignacio Enrique; Alonso, Leonardo Gabriel
- Año de publicación
- 2021
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- The spike protein is the main protein component of the SARS-CoV-2 virion surface. The spike receptor-binding motif mediates recognition of the human angiotensin-converting enzyme 2 (hACE2) receptor, a critical step in infection, and is the preferential target for spikeneutralizing antibodies. Post-translational modifications of the spike receptor-binding motif have been shown to modulate viral infectivity and host immune response, but these modifications are still being explored. Here we studied asparagine deamidation of the spike protein, a spontaneous event that leads to the appearance of aspartic and isoaspartic residues, which affect both the protein backbone and its charge. We used computational prediction and biochemical experiments to identify five deamidation hotspots in the SARS-CoV-2 spike protein. Asparagine residues 481 and 501 in the receptor-binding motif deamidate with a half-life of 16.5 and 123 days at 37°C, respectively. Deamidation is significantly slowed at 4°C, indicating a strong dependence of spike protein molecular aging on environmental conditions. Deamidation of the spike receptor-binding motif decreases the equilibrium constant for binding to the hACE2 receptor more than 3.5-fold, yet its high conservation pattern suggests some positive effect on viral fitness. We propose a model for deamidation of the full SARS-CoV-2 virion illustrating how deamidation of the spike receptor-binding motif could lead to the accumulation on the virion surface of a nonnegligible chemically diverse spike population in a timescale of days. Our findings provide a potential mechanism for molecular aging of the spike protein with significant consequences for understanding virus infectivity and vaccine development.
Fil: Lorenzo Lopez, Juan Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina
Fil: Defelipe, Lucas Alfredo. European Molecular Biology Laboratory; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Aliperti Car, Lucio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Niebling, Stephan. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania
Fil: Custódio, Tânia F.. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania
Fil: Löw, Christian. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania
Fil: Schwarz, Jennifer J.. European Molecular Biology Laboratory; Alemania
Fil: Remans, Kim. European Molecular Biology Laboratory; Alemania
Fil: Craig, Patricio Oliver. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina
Fil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina
Fil: García Alai, María. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania
Fil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina
Fil: Alonso, Leonardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina - Materia
-
SARS-COV-2
RECEPTOR-BINDING
SPIKE
MOLECULAR AGING
PROTEIN DEAMIDATION
RNA VIRUS
PROTEIN EVOLUTION
PROTEIN-PROTEIN INTERACTION
RECEPTOR STRUCTURE-FUNCTION
COVID-19 - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
.jpg)
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/149752
Ver los metadatos del registro completo
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Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motifLorenzo Lopez, Juan RamiroDefelipe, Lucas AlfredoAliperti Car, LucioNiebling, StephanCustódio, Tânia F.Löw, ChristianSchwarz, Jennifer J.Remans, KimCraig, Patricio OliverOtero, Lisandro HoracioKlinke, SebastianGarcía Alai, MaríaSánchez Miguel, Ignacio EnriqueAlonso, Leonardo GabrielSARS-COV-2RECEPTOR-BINDINGSPIKEMOLECULAR AGINGPROTEIN DEAMIDATIONRNA VIRUSPROTEIN EVOLUTIONPROTEIN-PROTEIN INTERACTIONRECEPTOR STRUCTURE-FUNCTIONCOVID-19https://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1The spike protein is the main protein component of the SARS-CoV-2 virion surface. The spike receptor-binding motif mediates recognition of the human angiotensin-converting enzyme 2 (hACE2) receptor, a critical step in infection, and is the preferential target for spikeneutralizing antibodies. Post-translational modifications of the spike receptor-binding motif have been shown to modulate viral infectivity and host immune response, but these modifications are still being explored. Here we studied asparagine deamidation of the spike protein, a spontaneous event that leads to the appearance of aspartic and isoaspartic residues, which affect both the protein backbone and its charge. We used computational prediction and biochemical experiments to identify five deamidation hotspots in the SARS-CoV-2 spike protein. Asparagine residues 481 and 501 in the receptor-binding motif deamidate with a half-life of 16.5 and 123 days at 37°C, respectively. Deamidation is significantly slowed at 4°C, indicating a strong dependence of spike protein molecular aging on environmental conditions. Deamidation of the spike receptor-binding motif decreases the equilibrium constant for binding to the hACE2 receptor more than 3.5-fold, yet its high conservation pattern suggests some positive effect on viral fitness. We propose a model for deamidation of the full SARS-CoV-2 virion illustrating how deamidation of the spike receptor-binding motif could lead to the accumulation on the virion surface of a nonnegligible chemically diverse spike population in a timescale of days. Our findings provide a potential mechanism for molecular aging of the spike protein with significant consequences for understanding virus infectivity and vaccine development.Fil: Lorenzo Lopez, Juan Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; ArgentinaFil: Defelipe, Lucas Alfredo. European Molecular Biology Laboratory; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Aliperti Car, Lucio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Niebling, Stephan. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; AlemaniaFil: Custódio, Tânia F.. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; AlemaniaFil: Löw, Christian. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; AlemaniaFil: Schwarz, Jennifer J.. European Molecular Biology Laboratory; AlemaniaFil: Remans, Kim. European Molecular Biology Laboratory; AlemaniaFil: Craig, Patricio Oliver. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; ArgentinaFil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; ArgentinaFil: García Alai, María. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; AlemaniaFil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; ArgentinaFil: Alonso, Leonardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; ArgentinaAmerican Society for Biochemistry and Molecular Biology2021-09info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/149752Lorenzo Lopez, Juan Ramiro; Defelipe, Lucas Alfredo; Aliperti Car, Lucio; Niebling, Stephan; Custódio, Tânia F.; et al.; Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 4; 9-2021; 1-250021-9258CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbc.2021.101175info:eu-repo/semantics/altIdentifier/url/https://www.jbc.org/article/S0021-9258(21)00977-7/fulltextinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:01:20Zoai:ri.conicet.gov.ar:11336/149752instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 10:01:20.25CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
| dc.title.none.fl_str_mv |
Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif |
| title |
Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif |
| spellingShingle |
Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif Lorenzo Lopez, Juan Ramiro SARS-COV-2 RECEPTOR-BINDING SPIKE MOLECULAR AGING PROTEIN DEAMIDATION RNA VIRUS PROTEIN EVOLUTION PROTEIN-PROTEIN INTERACTION RECEPTOR STRUCTURE-FUNCTION COVID-19 |
| title_short |
Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif |
| title_full |
Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif |
| title_fullStr |
Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif |
| title_full_unstemmed |
Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif |
| title_sort |
Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif |
| dc.creator.none.fl_str_mv |
Lorenzo Lopez, Juan Ramiro Defelipe, Lucas Alfredo Aliperti Car, Lucio Niebling, Stephan Custódio, Tânia F. Löw, Christian Schwarz, Jennifer J. Remans, Kim Craig, Patricio Oliver Otero, Lisandro Horacio Klinke, Sebastian García Alai, María Sánchez Miguel, Ignacio Enrique Alonso, Leonardo Gabriel |
| author |
Lorenzo Lopez, Juan Ramiro |
| author_facet |
Lorenzo Lopez, Juan Ramiro Defelipe, Lucas Alfredo Aliperti Car, Lucio Niebling, Stephan Custódio, Tânia F. Löw, Christian Schwarz, Jennifer J. Remans, Kim Craig, Patricio Oliver Otero, Lisandro Horacio Klinke, Sebastian García Alai, María Sánchez Miguel, Ignacio Enrique Alonso, Leonardo Gabriel |
| author_role |
author |
| author2 |
Defelipe, Lucas Alfredo Aliperti Car, Lucio Niebling, Stephan Custódio, Tânia F. Löw, Christian Schwarz, Jennifer J. Remans, Kim Craig, Patricio Oliver Otero, Lisandro Horacio Klinke, Sebastian García Alai, María Sánchez Miguel, Ignacio Enrique Alonso, Leonardo Gabriel |
| author2_role |
author author author author author author author author author author author author author |
| dc.subject.none.fl_str_mv |
SARS-COV-2 RECEPTOR-BINDING SPIKE MOLECULAR AGING PROTEIN DEAMIDATION RNA VIRUS PROTEIN EVOLUTION PROTEIN-PROTEIN INTERACTION RECEPTOR STRUCTURE-FUNCTION COVID-19 |
| topic |
SARS-COV-2 RECEPTOR-BINDING SPIKE MOLECULAR AGING PROTEIN DEAMIDATION RNA VIRUS PROTEIN EVOLUTION PROTEIN-PROTEIN INTERACTION RECEPTOR STRUCTURE-FUNCTION COVID-19 |
| purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
| dc.description.none.fl_txt_mv |
The spike protein is the main protein component of the SARS-CoV-2 virion surface. The spike receptor-binding motif mediates recognition of the human angiotensin-converting enzyme 2 (hACE2) receptor, a critical step in infection, and is the preferential target for spikeneutralizing antibodies. Post-translational modifications of the spike receptor-binding motif have been shown to modulate viral infectivity and host immune response, but these modifications are still being explored. Here we studied asparagine deamidation of the spike protein, a spontaneous event that leads to the appearance of aspartic and isoaspartic residues, which affect both the protein backbone and its charge. We used computational prediction and biochemical experiments to identify five deamidation hotspots in the SARS-CoV-2 spike protein. Asparagine residues 481 and 501 in the receptor-binding motif deamidate with a half-life of 16.5 and 123 days at 37°C, respectively. Deamidation is significantly slowed at 4°C, indicating a strong dependence of spike protein molecular aging on environmental conditions. Deamidation of the spike receptor-binding motif decreases the equilibrium constant for binding to the hACE2 receptor more than 3.5-fold, yet its high conservation pattern suggests some positive effect on viral fitness. We propose a model for deamidation of the full SARS-CoV-2 virion illustrating how deamidation of the spike receptor-binding motif could lead to the accumulation on the virion surface of a nonnegligible chemically diverse spike population in a timescale of days. Our findings provide a potential mechanism for molecular aging of the spike protein with significant consequences for understanding virus infectivity and vaccine development. Fil: Lorenzo Lopez, Juan Ramiro. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Tandil. Centro de Investigación Veterinaria de Tandil. Universidad Nacional del Centro de la Provincia de Buenos Aires. Centro de Investigación Veterinaria de Tandil. Provincia de Buenos Aires. Gobernación. Comision de Investigaciones Científicas. Centro de Investigación Veterinaria de Tandil; Argentina Fil: Defelipe, Lucas Alfredo. European Molecular Biology Laboratory; Alemania. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Aliperti Car, Lucio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Niebling, Stephan. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania Fil: Custódio, Tânia F.. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania Fil: Löw, Christian. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania Fil: Schwarz, Jennifer J.. European Molecular Biology Laboratory; Alemania Fil: Remans, Kim. European Molecular Biology Laboratory; Alemania Fil: Craig, Patricio Oliver. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Departamento de Química Biológica; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina Fil: Otero, Lisandro Horacio. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: Klinke, Sebastian. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Parque Centenario. Instituto de Investigaciones Bioquímicas de Buenos Aires. Fundación Instituto Leloir. Instituto de Investigaciones Bioquímicas de Buenos Aires; Argentina Fil: García Alai, María. European Molecular Biology Laboratory; Alemania. Centre for Structural Systems Biology; Alemania Fil: Sánchez Miguel, Ignacio Enrique. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Ciudad Universitaria. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales. Instituto de Química Biológica de la Facultad de Ciencias Exactas y Naturales; Argentina Fil: Alonso, Leonardo Gabriel. Consejo Nacional de Investigaciones Científicas y Técnicas. Oficina de Coordinación Administrativa Houssay. Instituto de Nanobiotecnología. Universidad de Buenos Aires. Facultad de Farmacia y Bioquímica. Instituto de Nanobiotecnología; Argentina |
| description |
The spike protein is the main protein component of the SARS-CoV-2 virion surface. The spike receptor-binding motif mediates recognition of the human angiotensin-converting enzyme 2 (hACE2) receptor, a critical step in infection, and is the preferential target for spikeneutralizing antibodies. Post-translational modifications of the spike receptor-binding motif have been shown to modulate viral infectivity and host immune response, but these modifications are still being explored. Here we studied asparagine deamidation of the spike protein, a spontaneous event that leads to the appearance of aspartic and isoaspartic residues, which affect both the protein backbone and its charge. We used computational prediction and biochemical experiments to identify five deamidation hotspots in the SARS-CoV-2 spike protein. Asparagine residues 481 and 501 in the receptor-binding motif deamidate with a half-life of 16.5 and 123 days at 37°C, respectively. Deamidation is significantly slowed at 4°C, indicating a strong dependence of spike protein molecular aging on environmental conditions. Deamidation of the spike receptor-binding motif decreases the equilibrium constant for binding to the hACE2 receptor more than 3.5-fold, yet its high conservation pattern suggests some positive effect on viral fitness. We propose a model for deamidation of the full SARS-CoV-2 virion illustrating how deamidation of the spike receptor-binding motif could lead to the accumulation on the virion surface of a nonnegligible chemically diverse spike population in a timescale of days. Our findings provide a potential mechanism for molecular aging of the spike protein with significant consequences for understanding virus infectivity and vaccine development. |
| publishDate |
2021 |
| dc.date.none.fl_str_mv |
2021-09 |
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info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
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article |
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http://hdl.handle.net/11336/149752 Lorenzo Lopez, Juan Ramiro; Defelipe, Lucas Alfredo; Aliperti Car, Lucio; Niebling, Stephan; Custódio, Tânia F.; et al.; Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 4; 9-2021; 1-25 0021-9258 CONICET Digital CONICET |
| url |
http://hdl.handle.net/11336/149752 |
| identifier_str_mv |
Lorenzo Lopez, Juan Ramiro; Defelipe, Lucas Alfredo; Aliperti Car, Lucio; Niebling, Stephan; Custódio, Tânia F.; et al.; Deamidation drives molecular aging of the SARS-CoV-2 spike protein receptor-binding motif; American Society for Biochemistry and Molecular Biology; Journal of Biological Chemistry (online); 279; 4; 9-2021; 1-25 0021-9258 CONICET Digital CONICET |
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eng |
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eng |
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info:eu-repo/semantics/altIdentifier/doi/10.1016/j.jbc.2021.101175 info:eu-repo/semantics/altIdentifier/url/https://www.jbc.org/article/S0021-9258(21)00977-7/fulltext |
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American Society for Biochemistry and Molecular Biology |
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American Society for Biochemistry and Molecular Biology |
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