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Article

SARS-CoV-2 D614G spike mutation increases entry efficiency with enhanced ACE2-binding affinity.

Nature communications - 8 Feb 2021

Ozono Seiya, Zhang Yanzhao, Ode Hirotaka, Sano Kaori, Tan Toong Seng, Imai Kazuo, Miyoshi Kazuyasu, Kishigami Satoshi, Ueno Takamasa, Iwatani Yasumasa, Suzuki Tadaki, Tokunaga Kenzo

Abstract excerpt

The causative agent of the COVID-19 pandemic, SARS-CoV-2, is steadily mutating during continuous transmission among humans. Such mutations can occur in the spike (S) protein that binds to the ACE2 receptor and is cleaved by TMPRSS2. However, whether S mutations affect SARS-CoV-2 cell entry remains unknown. Here, we show that naturally occurring S mutations can reduce or enhance cell entry via ACE2 and TMPRSS2. A...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 33558493
DOI: 10.1038/s41467-021-21118-2
PMCID: PMC7870668

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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