Article

Compared with SARS-CoV2 wild type’s spike protein, the SARS-CoV2 omicron’s receptor binding motif has adopted a more SARS-CoV1 and/or bat/civet-like structure

2021-12-15

Abstract excerpt

Our study focuses on free energy calculations of SARS-CoV2 spike protein receptor binding motives (RBMs) from wild type and variants-of-concern with particular emphasis on currently emerging SARS- CoV2 omicron variants of concern (VOC). Our computational free energy analysis underlines the occurrence of positive selection processes that specify omicron host adaption and bring changes on the molecular level into co...

Topics

Open a Topic to create a Post that cites this publication.

Identifiers and source

Literature Corpus work: 5227ad49-39e8-51f3-836f-1e556d1579e5
DOI: 10.1101/2021.12.14.472585

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Compared with SARS-CoV2 wild type’s spike protein, the SARS-CoV2 omicron’s receptor binding motif has adopted a more SARS-CoV1 and/or bat/civet-like structureDOI 10.1101/2021.12.14.472585Read

Improved binding affinity of the Omicron’s spike protein with hACE2 receptor is the key factor behind its increased virulenceSemantic proximity Read

In silico analysis of SARS-CoV-2 spike protein N501Y and N501T mutation effects on human ACE2 binding.Semantic proximity Read

Mutations in Spike Protein of SARS-CoV-2 Modulate Receptor Binding, Membrane Fusion and Immunogenicity: An Insight into Viral Tropism and Pathogenesis of COVID-19Semantic proximity Read

Evolutionary trajectory of receptor binding specificity and promiscuity of the spike protein of SARS-CoV-2Semantic proximity Read

Molecular dynamics simulations of the delta and omicron SARS-CoV-2 spike – ACE2 complexes reveal distinct changes between both variantsSemantic proximity Read

Different aspects in explaining how mutations could affect the binding mechanism of receptor binding domain of SARS-CoV-2 spike protein in interaction with ACE2.Semantic proximity Read

Assessment of Mutations on RBD in the Spike Protein of SARS-CoV-2 Alpha, Delta and Omicron VariantsSemantic proximity Read

SARS-CoV-2 spike protein predicted to form complexes with host receptor protein orthologues from a broad range of mammals.Semantic proximity Read

SARS-CoV-2 spike protein predicted to form complexes with host receptor protein orthologues from a broad range of mammalsSemantic proximity Read

SARS-CoV-2 Spike mutations modify the interaction between virus Spike and human ACE2 receptors.Semantic proximity Read

Effect of Delta and Omicron Mutations on the RBD-SD1 Domain of the Spike Protein in SARS-CoV-2 and the Omicron Mutations on RBD-ACE2 Interface Complex.Semantic proximity Read

SARS-COV-2 Omicron variant predicted to exhibit higher affinity to ACE-2 receptor and lower affinity to a large range of neutralizing antibodies, using a rapid computational platformSemantic proximity Read