Spike protein mutations and structural insights of pangolin lineage B.1.1.25 with implications for viral pathogenicity and ACE2 binding affinity

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Location: Deutsche Nationalbibliothek Frankfurt am Main

Extent: 1 Online-Ressource.

Language: Englisch

Bibliographic citation: Spike protein mutations and structural insights of pangolin lineage B.1.1.25 with implications for viral pathogenicity and ACE2 binding affinity ; volume:13 ; number:1 ; day:12 ; month:8 ; year:2023 ; pages:1-19 ; date:12.2023
Scientific reports ; 13, Heft 1 (12.8.2023), 1-19, 12.2023

Creator: Akter, Shahina
Oliveira, Jonas Ivan Nobre
Barton, Carl
Sarkar, Murshed Hasan
Shahab, Muhammad
Banu, Tanjina Akhtar
Goswami, Barna
Osman, Eshrar
Uzzaman, Mohammad Samir
Nafisa, Tasnim
Molla, Maruf Ahmed
Yeasmin, Mahmuda
Farzana, Maisha
Habib, Ahashan
Shaikh, Aftab Ali
Khan, Salim

Contributor: SpringerLink (Online service)

DOI: 10.1038/s41598-023-40005-y

URN: urn:nbn:de:101:1-2024020113421893944328

Rights: Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.

Last update: 15.08.2025, 7:35 AM CEST

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Associated

Akter, Shahina
Oliveira, Jonas Ivan Nobre
Barton, Carl
Sarkar, Murshed Hasan
Shahab, Muhammad
Banu, Tanjina Akhtar
Goswami, Barna
Osman, Eshrar
Uzzaman, Mohammad Samir
Nafisa, Tasnim
Molla, Maruf Ahmed
Yeasmin, Mahmuda
Farzana, Maisha
Habib, Ahashan
Shaikh, Aftab Ali
Khan, Salim
SpringerLink (Online service)

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Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Interfacial subregions of SARS-CoV-2 spike RBD to hACE2 affect intermolecular affinity by their distinct roles played in association and dissociation kinetics

Omicron sub-lineage BA.5 infection results in attenuated pathology in hACE2 transgenic mice

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Antibody Fc-binding profiles and ACE2 affinity to SARS-CoV-2 RBD variants

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Substitution of T403R allows efficient utilization of human ACE2 by Spike proteins of bat coronaviruses

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Mutations in the SARS-CoV-2 spike protein modulate the virus affinity to the human ACE2 receptor, an in silico analysis

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Interfacial subregions of SARS-CoV-2 spike RBD to hACE2 affect intermolecular affinity by their distinct roles played in association and dissociation kinetics

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Antibody Fc-binding profiles and ACE2 affinity to SARS-CoV-2 RBD variants

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Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level

Substitution of T403R allows efficient utilization of human ACE2 by Spike proteins of bat coronaviruses

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Spike protein mutations and structural insights of pangolin lineage B.1.1.25 with implications for viral pathogenicity and ACE2 binding affinity

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Other Objects (12)

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Mutations in the SARS-CoV-2 spike protein modulate the virus affinity to the human ACE2 receptor, an in silico analysis

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Interfacial subregions of SARS-CoV-2 spike RBD to hACE2 affect intermolecular affinity by their distinct roles played in association and dissociation kinetics

Omicron sub-lineage BA.5 infection results in attenuated pathology in hACE2 transgenic mice

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

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Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level

Substitution of T403R allows efficient utilization of human ACE2 by Spike proteins of bat coronaviruses

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Mutations in the SARS-CoV-2 spike protein modulate the virus affinity to the human ACE2 receptor, an in silico analysis

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Interfacial subregions of SARS-CoV-2 spike RBD to hACE2 affect intermolecular affinity by their distinct roles played in association and dissociation kinetics

Omicron sub-lineage BA.5 infection results in attenuated pathology in hACE2 transgenic mice

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Antibody Fc-binding profiles and ACE2 affinity to SARS-CoV-2 RBD variants

Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level

Substitution of T403R allows efficient utilization of human ACE2 by Spike proteins of bat coronaviruses

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Spike residue 403 affects binding of coronavirus spikes to human ACE2

Mutations in the SARS-CoV-2 spike protein modulate the virus affinity to the human ACE2 receptor, an in silico analysis

Compensatory epistasis maintains ACE2 affinity in SARS-CoV-2 Omicron BA.1

Interfacial subregions of SARS-CoV-2 spike RBD to hACE2 affect intermolecular affinity by their distinct roles played in association and dissociation kinetics

Omicron sub-lineage BA.5 infection results in attenuated pathology in hACE2 transgenic mice

Structural bioinformatics analysis of SARS-CoV-2 variants reveals higher hACE2 receptor binding affinity for Omicron B.1.1.529 spike RBD compared to wild type reference

Antibody Fc-binding profiles and ACE2 affinity to SARS-CoV-2 RBD variants

Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

Force-tuned avidity of spike variant-ACE2 interactions viewed on the single-molecule level

Substitution of T403R allows efficient utilization of human ACE2 by Spike proteins of bat coronaviruses

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