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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.

Structure (London, England : 1993) - 8 Aug 2024

Li Linjie, Shi Kaiyuan, Gu Yuhang, Xu Zepeng, Shu Chang, Li Dedong, Sun Junqing, Cong Mengqing, Li Xiaomei, Zhao Xin, Yu Guanghui, Hu Songnian, Tan Hui, Qi Jianxun, Ma Xiaopeng, Liu Kefang, Gao George F

Abstract excerpt

The recently emerged BA.2.86, JN.1, EG.5, EG.5.1, and HV.1 variants have a growth advantage. In this study, we explore the structural bases of receptor binding and immune evasion for the Omicron BA.2.86, JN.1, EG.5, EG.5.1, and HV.1 sub-variants. Our findings reveal that BA.2.86 exhibits strong receptor binding, whereas its JN.1 sub-lineage displays a decreased binding affinity to human ACE2 (hACE2). Through...

Topics

Humans
SARS-CoV-2
Spike Glycoprotein, Coronavirus
Immune Evasion
Protein Binding
Antibodies, Monoclonal
Angiotensin-Converting Enzyme 2
COVID-19
Binding Sites

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Models, Molecular

Antibodies, Neutralizing

Antibodies, Viral

Mutation

Source

Identifiers

PMID: 39013463
DOI: 10.1016/j.str.2024.06.012

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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