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

Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants.

Science (New York, N.Y.) - 13 Aug 2021

Yuan Meng, Huang Deli, Lee Chang-Chun D, Wu Nicholas C, Jackson Abigail M, Zhu Xueyong, Liu Hejun, Peng Linghang, van Gils Marit J, Sanders Rogier W, Burton Dennis R, Reincke S Momsen, Prüss Harald, Kreye Jakob, Nemazee David, Ward Andrew B, Wilson Ian A

Abstract excerpt

Neutralizing antibodies (nAbs) elicited against the receptor binding site (RBS) of the spike protein of wild-type severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) are generally less effective against recent variants of concern. RBS residues Glu484, Lys417, and Asn501 are mutated in variants first described in South Africa (B.1.351) and Brazil (P.1). We analyzed their effects on angiotensin-converting...

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 Antibodies, Viral

Share to Antigenic Variation

Share to Antigens, Viral

Share to Binding Sites, Antibody

Share to Immune Evasion

Share to Spike Glycoprotein, Coronavirus

Source

Open in PubMed Open full text

Identifiers

PMID: 34016740
DOI: 10.1126/science.abh1139
PMCID: PMC8284396

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variants.PMID 34016740Read ↗

Structural and functional ramifications of antigenic drift in recent SARS-CoV-2 variantsSemantic proximity Read ↗

Structure-based analyses of neutralization antibodies interacting with naturally occurring SARS-CoV-2 RBD variantsSemantic proximity Read ↗

Analysis of SARS-CoV-2 variant mutations reveals neutralization escape mechanisms and the ability to use ACE2 receptors from additional species.Semantic proximity Read ↗

Structural basis for enhanced infectivity and immune evasion of SARS-CoV-2 variantsSemantic 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 ↗

Broadly neutralizing antibodies targeting a conserved silent face of spike RBD resist extreme SARS-CoV-2 antigenic driftSemantic proximity Read ↗

Cross-neutralizing antibodies bind a SARS-CoV-2 cryptic site and resist circulating variantsSemantic proximity Read ↗

Mapping the antigenic diversification of SARS-CoV-2Semantic proximity Read ↗

Structural basis for accommodation of emerging B.1.351 and B.1.1.7 variants by two potent SARS-CoV-2 neutralizing antibodies.Semantic proximity Read ↗

Insights on SARS-CoV-2’s Mutations for Evading Human Antibodies: Sacrifice and SurvivalSemantic proximity Read ↗

Antigenic drift: Understanding COVID-19.Semantic proximity Read ↗

Structural and functional dissection of neutralisation differences among SARS-CoV-2 variants using antigenicity prediction and CR3022 binding analysis.Semantic proximity Read ↗

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