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

Altered receptor binding, antibody evasion and retention of T cell recognition by the SARS-CoV-2 XBB.1.5 spike protein

29 Feb 2024

Abstract excerpt

Abstract The XBB.1.5 variant of SARS-CoV-2 has rapidly achieved global dominance and exhibits a high growth advantage over previous variants. Preliminary reports suggest that the success of XBB.1.5 stems from mutations within its spike glycoprotein, causing immune evasion and enhanced receptor binding. We present receptor binding studies that demonstrate retention of binding contacts with the human ACE2 receptor...

Read the complete abstract on PubMed

Topics

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

Share to COVID-19 Clinical Research Studies
Share to SARS-CoV-2 and COVID-19 Research
Share to vaccines and immunoinformatics approaches

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 38424106
DOI: 10.1038/s41467-024-46104-2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Altered receptor binding, antibody evasion and retention of T cell recognition by the SARS-CoV-2 XBB.1.5 spike proteinPMID 38424106Read ↗

SARS-CoV-2 Spike Protein XBB.1.5 Mutations Altered Four Conserved Antigenic Determinants.Semantic proximity Read ↗

Immunological imprinting shapes the specificity of human antibody responses against SARS-CoV-2 variantsSemantic proximity Read ↗

Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spikeSemantic proximity Read ↗

Neutralization, effector function and immune imprinting of Omicron variants.Semantic proximity Read ↗

Antigenicity and receptor affinity of SARS-CoV-2 BA.2.86 spike.Semantic proximity Read ↗

Unraveling the impact of SARS-CoV-2 mutations on immunity: insights from innate immune recognition to antibody and T cell responses.Semantic proximity Read ↗

Structural analysis of receptor binding domain mutations in SARS-CoV-2 variants of concern that modulate ACE2 and antibody binding.Semantic proximity Read ↗

The SARS-CoV-2 neutralizing antibody response to SD1 and its evasion by BA.2.86Semantic proximity Read ↗

Molecular basis of immune evasion by the delta and kappa SARS-CoV-2 variantsSemantic proximity Read ↗

Spike structures, receptor binding, and immune escape of recently circulating SARS-CoV-2 Omicron BA.2.86, JN.1, EG.5, EG.5.1, and HV.1 sub-variants.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 ↗

Therapeutic and vaccine-induced cross-reactive antibodies with effector function against emerging Omicron variantsSemantic proximity Read ↗

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