Article

Omicron Spike protein has a positive electrostatic surface that promotes ACE2 recognition and antibody escape

2022-02-14

Abstract excerpt

High transmissibility is a hallmark of the Omicron variant of SARS-CoV-2. Understanding the molecular determinants of Omicron’s transmissibility will impact development of intervention strategies. Here we map the electrostatic potential surface of the Spike protein to show that major SARS-CoV-2 variants have accumulated positive charges in solvent-exposed regions of the Spike protein, especially its ACE2-binding i...

Topics

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

Identifiers and source

Literature Corpus work: d369b613-1097-5c95-ac1f-ee9c3d675643
DOI: 10.1101/2022.02.13.480261

Open publication

Related research

Semantic proximity does not establish scientific evidence.

Click a neighbor to travelStep 1 · 12 closest

Omicron Spike protein has a positive electrostatic surface that promotes ACE2 recognition and antibody escapeDOI 10.1101/2022.02.13.480261Read

Omicron Spike Protein Has a Positive Electrostatic Surface That Promotes ACE2 Recognition and Antibody EscapeSemantic proximity Read

SARS-CoV-2 Omicron Variant: ACE2 Binding, Cryo-EM Structure of Spike Protein-ACE2 Complex and Antibody EvasionSemantic proximity Read

SARS-CoV-2 Omicron variant: Antibody evasion and cryo-EM structure of spike protein-ACE2 complex.Semantic proximity Read

Antibody escape and cryptic cross-domain stabilization in the SARS-CoV-2 Omicron spike proteinSemantic proximity Read

Structural modeling of Omicron spike protein and its complex with human ACE-2 receptor: Molecular basis for high transmissibility of the virus.Semantic proximity Read

Structures of the Omicron spike trimer with ACE2 and an anti-Omicron antibody: mechanisms for the high infectivity, immune evasion and antibody drug discoverySemantic proximity Read

Omicron SARS-CoV-2 mutations stabilize spike up-RBD conformation and lead to a non-RBM-binding monoclonal antibody escape.Semantic proximity Read

Antibody escape and cryptic cross-domain stabilization in the SARS-CoV-2 Omicron spike protein.Semantic proximity Read

In Silico Analysis of the Effects of Omicron Spike Amino Acid Changes on the Interactions with Human Proteins.Semantic proximity Read

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 The Effects Of Omicron Spike Amino Acid Changes On The Interactions With Human ACE2 Receptor And Structurally Characterized Complexes With Human AntibodiesSemantic proximity Read

Distinct Conformations of SARS-CoV-2 Omicron Spike Protein and Its Interaction with ACE2 and Antibody.Semantic proximity Read