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

SARS-CoV-2 Spike Protein XBB.1.5 Mutations Altered Four Conserved Antigenic Determinants.

International journal of molecular sciences - 18 Feb 2026

Akbulut Ekrem, Yildirim Meltem, Kahraman Huseyin

Abstract excerpt

The continuous evolution of SARS-CoV-2 affects its infectivity and ability to evade the immune system. The XBB.1.5 subvariant carries numerous mutations compared to previous Omicron variants and exhibits significant evasion of polyclonal neutralizing antibodies. In this study, the mechanistic effects of mutations in the XBB.1.5 spike protein on structural stability, antigenic markers, and antibody epitopes were...

Read the complete abstract on PubMed

Topics

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

Share to Angiotensin-Converting Enzyme 2
Share to Antibodies, Neutralizing

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to COVID-19

Share to Epitopes, B-Lymphocyte

Share to Molecular Dynamics Simulation

Share to Protein Stability

Share to SARS-CoV-2

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 41752076
DOI: 10.3390/ijms27041940
PMCID: PMC12941379

Genes

ACE2

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

SARS-CoV-2 Spike Protein XBB.1.5 Mutations Altered Four Conserved Antigenic Determinants.PMID 41752076Read ↗

Exploring B-cell epitope conservation and antigenicity shift in current COVID-19 variants: Analyzing spike-antibody interactions for therapeutic uses.Semantic proximity Read ↗

Molecular and structural insights into SARS-CoV-2 evolution: from BA.2 to XBB subvariants.Semantic proximity Read ↗

Structural basis for the evolution and antibody evasion of SARS-CoV-2 BA.2.86 and JN.1 subvariants.Semantic proximity Read ↗

Structural Analysis of the SARS-CoV-2 Spike N-Terminal Domain Across Wild-Type and Recent Variants: A Comparative Study.Semantic proximity Read ↗

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

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

SARS-CoV-2 omicron BA.2.87.1 exhibits higher susceptibility to serum neutralization than EG.5.1 and JN.1.Semantic proximity Read ↗

Virological characteristics of the SARS-CoV-2 XBB.1.5 variantSemantic proximity Read ↗

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

Is the BNT162b2 vaccine still effective against the latest variant: XBB.1.5?Semantic proximity Read ↗

Immune Evasion, Cell-Cell Fusion, and Spike Stability of the SARS-CoV-2 XEC Variant: Role of Glycosylation Mutations at the N-terminal DomainSemantic proximity Read ↗

SARS-CoV-2 Omicron XBB lineage spike structures, conformations, antigenicity, and receptor recognition.Semantic proximity Read ↗

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