Binding affinity between coronavirus spike protein and human ACE2 receptor

Shum, Marcus Ho-Hin; Lee, Yang; Tam, Leighton; Xia, Hui; Chung, Oscar Lung-Wa; Guo, Zhihong; Lam, Tommy Tsan-Yuk

doi:10.1016/j.csbj.2024.01.009

Cited by 2 publications

(3 citation statements)

References 159 publications

(253 reference statements)

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“…Omicron and prototype RBDs share a highly similar binding property to hACE2, but a group of Omicron RBD residues (S496, R498, and Y501) contributes to significant interactions between RBD and hACE2 [11]. Although various in silico and biochemical studies have been reported for the affinity between the Omicron RBD/S protein and ACE2 [8,9,11,12], our FCCS results support the high affinity of Omicron RBD for hACE2.…”

Section: Increased Affinity Between Rbd Of the Omicron Variant And Hace2supporting

confidence: 70%

“…As the affinity between cell receptors and the virus through its S protein could promote the infection and transmission process, it is important to confirm the variant-specific affinity with ACE2. Although various biochemical and in silico studies have been reported on how these amino acid substitutions affect the affinity of Omicron variants for ACE2 [8,9,11,12], it is not completely conclusive. Fluorescence correlation spectroscopy (FCS) and its advanced method using two-color fluorescence, fluorescence cross-correlation spectroscopy (FCCS), have been used for biomolecular interactions with single-molecule sensitivity [13][14][15].…”

Section: Introductionmentioning

confidence: 99%

“…The S1 subunit contains the receptor-binding domain (RBD) [6,7]. The S protein and the RBD domain itself of SARS-CoV-2 interact with hACE2 with a dissociation constant ( K d ) of several tens of nanomolars, and their structural insight has been reported [8,9]. Variant-specific missense mutations are scattered in viral proteins but relatively abundant in the S protein [10].…”

Section: Introductionmentioning

confidence: 99%

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Spike protein of the SARS-CoV-2 omicron variant interacts with actin

Fujimoto,

Kawai,

Kawamura

et al. 2024

Preprint

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The omicron variant of SARS-CoV-2 is responsible for the COVID-19 pandemic, serving as a significant origin for the variants still being detected today. It affects the spike protein that most vaccines used to target when the Omicron strain was discovered. Here, we demonstrate that the receptor binding domain (RBD) of the Omicron variant of SARS-CoV-2 exhibits an increased affinity for human angiotensin-converting enzyme type 2 (hACE2) as a viral cell receptor compared to the prototype RBD. We also identified that β- and γ-actin are Omicron-specific binding partners of RBD. Protein complex predictions suggested that many of the Omicron-specific amino acid substitutions might be involved in the affinity of RBD and actin. Accordingly, we highlight the intriguing observation that proteins expected to localize to different cellular compartments exhibit strong binding.

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Section: Increased Affinity Between Rbd Of the Omicron Variant And Hace2supporting

confidence: 70%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Spike protein of the SARS-CoV-2 omicron variant interacts with actin

Fujimoto,

Kawai,

Kawamura

et al. 2024

Preprint

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Interaction of Receptor-Binding Domain of the SARS-CoV-2 Omicron Variant with hACE2 and Actin

Fujimoto,

Kawai,

Kawamura

et al. 2024

Cells

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The omicron variant of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) was identified in 2021 as a variant with heavy amino acid mutations in the spike protein, which is targeted by most vaccines, compared to previous variants. Amino acid substitutions in the spike proteins may alter their affinity for host viral receptors and the host interactome. Here, we found that the receptor-binding domain (RBD) of the omicron variant of SARS-CoV-2 exhibited an increased affinity for human angiotensin-converting enzyme 2, a viral cell receptor, compared to the prototype RBD. Moreover, we identified β- and γ-actin as omicron-specific binding partners of RBD. Protein complex predictions revealed that many omicron-specific amino acid substitutions affected the affinity between RBD of the omicron variant and actin. Our findings indicate that proteins localized to different cellular compartments exhibit strong binding to the omicron RBD.

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Binding affinity between coronavirus spike protein and human ACE2 receptor

Cited by 2 publications

References 159 publications

Spike protein of the SARS-CoV-2 omicron variant interacts with actin

Spike protein of the SARS-CoV-2 omicron variant interacts with actin

Interaction of Receptor-Binding Domain of the SARS-CoV-2 Omicron Variant with hACE2 and Actin

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