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3. Atypical N-glycosylation of SARS-CoV-2 impairs the efficient binding of Spike-RBM to the human-host receptor hACE2

Author

Interconexión Eléctrica, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Gámez, Gustavo [0000-0002-5957-9163], Hermoso, Juan A. [0000-0002-1862-8950], Carrasco-López, César [0000-0002-3853-8776], Gómez-Mejia, Alejandro [0000-0002-7313-7169], Muskus, Carlos E. [0000-0003-4280-5627], Hammerschmidt, Sven [0000-0002-6382-6681], Gámez, Gustavo, Hermoso, Juan A., Carrasco-López, César, Gómez-Mejia, Alejandro, Muskus, Carlos E., Hammerschmidt, Sven, Interconexión Eléctrica, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Gámez, Gustavo [0000-0002-5957-9163], Hermoso, Juan A. [0000-0002-1862-8950], Carrasco-López, César [0000-0002-3853-8776], Gómez-Mejia, Alejandro [0000-0002-7313-7169], Muskus, Carlos E. [0000-0003-4280-5627], Hammerschmidt, Sven [0000-0002-6382-6681], Gámez, Gustavo, Hermoso, Juan A., Carrasco-López, César, Gómez-Mejia, Alejandro, Muskus, Carlos E., and Hammerschmidt, Sven

Abstract

SARS-CoV-2 internalization by human host cells relies on the molecular binding of its spike glycoprotein (SGP) to the angiotensin-converting-enzyme-2 (hACE2) receptor. It remains unknown whether atypical N-glycosylation of SGP modulates SARS-CoV-2 tropism for infections. Here, we address this question through an extensive bioinformatics analysis of publicly available structural and genetic data. We identified two atypical sequons (sequences of N-glycosylation: NGV 481-483 and NGV 501-503), strategically located on the receptor-binding motif (RBM) of SGP and facing the hACE2 receptor. Interestingly, the cryo-electron microscopy structure of trimeric SGP in complex with potent-neutralizing antibodies from convalescent patients revealed covalently-linked N-glycans in NGV 481-483 atypical sequons. Furthermore, NGV 501-503 atypical sequon involves the asparagine-501 residue, whose highly-transmissible mutation N501Y is present in circulating variants of major concerns and affects the SGP-hACE2 binding-interface through the well-known hotspot-353. These findings suggest that atypical SGP post-translational modifications modulate the SGP-hACE2 binding-affinity affecting consequently SARS-CoV-2 transmission and pathogenesis.

Published
2021

5. Post-Vaccination Streptococcus pneumoniae Carriage and Virulence Gene Distribution among Children Less Than Five Years of Age, Cape Coast, Ghana

Author

Mills, Richael O., primary, Abdullah, Mohammed R., additional, Akwetey, Samuel A., additional, Sappor, Dorcas C., additional, Cole, Isaac, additional, Baffuor-Asare, Michael, additional, Bolivar, Johan A., additional, Gámez, Gustavo, additional, van der Linden, Mark P. G., additional, and Hammerschmidt, Sven, additional

Published
2020
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7. Pneumococcal Metabolic Adaptation and Colonization Are Regulated by the Two-Component Regulatory System 08

Author

Gómez-Mejia, Alejandro, primary, Gámez, Gustavo, additional, Hirschmann, Stephanie, additional, Kluger, Viktor, additional, Rath, Hermann, additional, Böhm, Sebastian, additional, Voss, Franziska, additional, Kakar, Niamatullah, additional, Petruschka, Lothar, additional, Völker, Uwe, additional, Brückner, Reinhold, additional, Mäder, Ulrike, additional, and Hammerschmidt, Sven, additional

Published
2018
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9. Atypical N-glycosylation of SARS-CoV-2 impairs the efficient binding of Spike-RBM to the human host receptor hACE2.

Author

Adolfo Gámez, Gustavo, Antonio Hermoso, Juan, Andrés Carrasco-López, César, Gómez-Mejia, Alejandro, Enrique Muskus, Carlos, and Hammerschmidt, Sven

Subjects
SARS-CoV-2, POST-translational modification, COVID-19, PATHOGENESIS
Abstract

Introduction: SARS-CoV-2 internalization by human host cells relies on the molecular binding of its spike glycoprotein (SGP) to the angiotensin-converting-enzyme-2 (hACE2) receptor. Objective: To get insights into the potential role of atypical N-glycosylation sequons of SGP in modulating SARS-CoV-2 tropism for infections. Materials and methods: We made an extensive bioinformatics analysis of publicly available structural and genomic data. Results: We identified two atypical sequons (sequences of N-glycosylation: NGV 481- 483 and NGV 501-503) strategically located on the receptor-binding motif (RBM) of SGP and facing the hACE2 receptor. Interestingly, the cryo-electron microscopy structure of trimeric-SGP in complex with potent-neutralizing antibodies from convalescent patients revealed covalently-linked N-glycans in NGV 481-483 atypical sequons. Furthermore, NGV 501-503 atypical sequon involves the asparagine-501 residue whose highlytransmissible mutation N501Y is present in circulating variants of major concern and affects the SGP-hACE2 binding interface through the well-known hotspot-353. Conclusion: These findings suggest that atypical SGP post-translational modifications modulate the SGP-hACE2 binding-affinity affecting consequently SARS-CoV-2 transmission and pathogenesis. [ABSTRACT FROM AUTHOR]

Published
2021

10. Atypical N-glycosylation of SARS-CoV-2 impairs the efficient binding of Spike-RBM to the human-host receptor hACE2

Author

César Carrasco-López, Gustavo Gámez, Juan A. Hermoso, Sven Hammerschmidt, Alejandro Gómez-Mejia, Carlos Muskus, Interconexión Eléctrica, Ministerio de Ciencia, Innovación y Universidades (España), Agencia Estatal de Investigación (España), Gámez, Gustavo, Hermoso, Juan A., Carrasco-López, César, Gómez-Mejia, Alejandro, Muskus, Carlos E., Hammerschmidt, Sven, Gámez, Gustavo [0000-0002-5957-9163], Hermoso, Juan A. [0000-0002-1862-8950], Carrasco-López, César [0000-0002-3853-8776], Gómez-Mejia, Alejandro [0000-0002-7313-7169], Muskus, Carlos E. [0000-0003-4280-5627], and Hammerschmidt, Sven [0000-0002-6382-6681]

Subjects
2019-20 coronavirus outbreak, Coronavirus disease 2019 (COVID-19), N-linked glycosylation, Host (biology), Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), Christian ministry, Spike (database), Biology, Receptor, Virology
Abstract

SARS-CoV-2 internalization by human host cells relies on the molecular binding of its spike glycoprotein (SGP) to the angiotensin-converting-enzyme-2 (hACE2) receptor. It remains unknown whether atypical N-glycosylation of SGP modulates SARS-CoV-2 tropism for infections. Here, we address this question through an extensive bioinformatics analysis of publicly available structural and genetic data. We identified two atypical sequons (sequences of N-glycosylation: NGV 481-483 and NGV 501-503), strategically located on the receptor-binding motif (RBM) of SGP and facing the hACE2 receptor. Interestingly, the cryo-electron microscopy structure of trimeric SGP in complex with potent-neutralizing antibodies from convalescent patients revealed covalently-linked N-glycans in NGV 481-483 atypical sequons. Furthermore, NGV 501-503 atypical sequon involves the asparagine-501 residue, whose highly-transmissible mutation N501Y is present in circulating variants of major concerns and affects the SGP-hACE2 binding-interface through the well-known hotspot-353. These findings suggest that atypical SGP post-translational modifications modulate the SGP-hACE2 binding-affinity affecting consequently SARS-CoV-2 transmission and pathogenesis., This study was funded by CELSIA and ISA (Interconexión Eléctrica S.A.) in Colombia and supported by the BFU2017-90030-P grant to J.A.H. from the Spanish Ministry of Science and Innovation.

Published
2021

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