Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Investigating the role of glycans in Omicron sub-lineages XBB.1.5 and XBB.1.16 binding to host receptor using molecular dynamics and binding free energy calculations.

Journal of computer-aided molecular design - 1 Nov 2023

Singh Jaikee Kumar, Singh Jai, Srivastava Sandeep Kumar

Abstract excerpt

Omicron derived lineages viz. BA.2, BA.3, BA.4 BA.5, BF.7 and XBBs show prominence with improved immune escape, transmissibility, infectivity, and pathogenicity in general. Sub-variants, XBB.1.5 and XBB.1.16 have shown rapid spread, with mutations embedded throughout the viral genome, including the spike protein. Changing atomic landscapes in spike contributes significantly to modulate host pathogen interactions...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Molecular Dynamics Simulation
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Polysaccharides

Share to Protein Binding

Share to Software

Share to Spike Glycoprotein, Coronavirus

Source

Identifiers

PMID: 37542610
DOI: 10.1007/s10822-023-00526-0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 4 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Investigating the role of glycans in Omicron sub-lineages XBB.1.5 and XBB.1.16 binding to host receptor using molecular dynamics and binding free energy calculations.PMID 37542610Read ↗

The XBB.1.5 slightly increase the binding affinity for host receptor ACE2 and exhibit strongest immune escaping features: molecular modeling and free energy calculationSemantic proximity Read ↗

Molecular insights into the binding interactions and energetics of the omicron spike variant with hACE2 and a neutralizing antibody.Semantic proximity Read ↗

Is BF.7 more infectious than other Omicron subtypes: Insights from structural and simulation studies of BF.7 spike RBD variant.Semantic proximity Read ↗

Structure adaptation in Omicron SARS-CoV-2/hACE2: Biophysical origins of evolutionary driving forces.Semantic proximity Read ↗

Key mechanistic features of the trade-off between antibody escape and host cell binding in the SARS-CoV-2 Omicron variant spike proteinsSemantic proximity Read ↗

Impact of mutations in SARS-CoV-2 recombinant sub-variant XBB.1.16 on the binding affinity with human ACE2 receptor.Semantic proximity Read ↗

Ensemble-Based Mutational Profiling and Network Analysis of the SARS-CoV-2 Spike Omicron XBB Lineages for Interactions with the ACE2 Receptor and Antibodies: Cooperation of Binding Hotspots in Mediating Epistatic Couplings Underlies Binding Mechanism and Immune Escape.Semantic proximity Read ↗

Electrostatic Interactions Are the Primary Determinant of the Binding Affinity of SARS-CoV-2 Spike RBD to ACE2: A Computational Case Study of Omicron Variants.Semantic proximity Read ↗

Structural basis of Omicron immune evasion: A comparative computational study of Spike protein-Antibody interactionSemantic proximity Read ↗

Structure adaptation in Omicron SARS-CoV-2/hACE2: Biophysical origins of evolutionary driving forcesSemantic proximity Read ↗

SARS-CoV-2 Omicron XBB.1.5 May Be a Variant That Spreads More Widely and Faster Than Other VariantsSemantic proximity Read ↗

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

⌁Select a neighboring publication to make it the new centre.