Facilitating and restraining virus infection using cell-attachable soluble viral receptors DOI Creative Commons
Heng Zhang, Zhengli Wang,

Huong T. T. Nguyen

et al.

Proceedings of the National Academy of Sciences, Journal Year: 2024, Volume and Issue: 121(45)

Published: Oct. 31, 2024

SARS-CoV-2 uses the receptor binding domain (RBD) of its spike protein to recognize and infect host cells by cell surface angiotensin converting enzyme 2 (ACE2). The ACE2 is composed peptidase (PD), collectrin-like domain, transmembrane short cytoplasmic may exist as a dimer on surface. RBD site located atop PD, but involvement other domains in virus infection uncertain. We found that PD alone, whether anchored membrane via glycosylphosphatidylinositol anchor or attached another protein, fully functional for spike-mediated fusion infection. However, function viral receptor, must be positioned close proximity membrane. Elevating height using long rigid spacers reduces eliminates Moreover, we RBD-targeting neutralizing antibodies, nanobodies, de novo designed miniprotein binders, when present surface, also act receptors, facilitating Our data demonstrate are essential properties effectively mediate Importantly, show soluble RBD-binders can engineered make either susceptible resistant infection, which has significant implications antiviral therapy various virus-mediated applications.

Language: Английский

Design of customized coronavirus receptors DOI
Peng Liu, Meiling Huang, Hua Guo

et al.

Nature, Journal Year: 2024, Volume and Issue: 635(8040), P. 978 - 986

Published: Oct. 30, 2024

Language: Английский

Citations

7
SARS-CoV-2 spike protein: structure, viral entry and variants DOI
Bing Chen, Michael Farzan, Hyeryun Choe

et al.

Nature Reviews Microbiology, Journal Year: 2025, Volume and Issue: unknown

Published: May 6, 2025

Language: Английский

Citations

0
The role of IL-22 in cancer DOI

Zachary E. Hunzeker,

Lei Zhao,

Austin M. Kim

et al.

Medical Oncology, Journal Year: 2024, Volume and Issue: 41(10)

Published: Sept. 4, 2024

Language: Английский

Citations

2
Antibody‐mediated SARS‐CoV‐2 entry in cultured cells DOI Open Access
Md. Golam Kibria, Christy L. Lavine, Weichun Tang

et al.

EMBO Reports, Journal Year: 2023, Volume and Issue: 24(12)

Published: Nov. 2, 2023

Language: Английский

Citations

6
RBD mutations at the residues K417, E484, N501 reduced immunoreactivity with antisera from vaccinated and COVID-19 recovered patients DOI Creative Commons
Dablu Lal Gupta, Jhasaketan Meher, Anjan Kumar Giri

et al.

Drug Target Insights, Journal Year: 2024, Volume and Issue: 18(1), P. 20 - 26

Published: May 31, 2024

Introduction: It is unclear whether induced spike protein-specific antibodies due to infections with SARS-CoV-2 or the prototypic Wuhan isolate-based vaccination can immune-react emerging variants of SARS-CoV-2. Aim/objectives: The main objective study was measure immunoreactivity postvaccination Covishield™ (ChAdOx1 nCoV-19 coronavirus vaccines) by using selected peptides protein wild type and Methodology: Thirty patients who had recovered from 30 individuals vaccinated both doses were recruited for study. Venous blood samples (5 mL) collected at a single time point within 3-4 weeks recovery receiving vaccines. serum levels total immunoglobulin measured in groups. A 12 10 24 amino acids length spanning receptor-binding domain (RBD) their synthesized. immune-reactive these peptides. Results: found be significantly (p<0.001) higher as compared COVID-19 patients. Our reported that mutations RBD residues K417, E484, N501 have been associated reduced anti-sera people Conclusion: acid substitutions potential escape humoral immune response.

Language: Английский

Citations

1
Facilitating and restraining virus infection using cell-attachable soluble viral receptors DOI Creative Commons
Heng Zhang, Zhengli Wang,

Huong T. T. Nguyen

et al.

Proceedings of the National Academy of Sciences, Journal Year: 2024, Volume and Issue: 121(45)

Published: Oct. 31, 2024

SARS-CoV-2 uses the receptor binding domain (RBD) of its spike protein to recognize and infect host cells by cell surface angiotensin converting enzyme 2 (ACE2). The ACE2 is composed peptidase (PD), collectrin-like domain, transmembrane short cytoplasmic may exist as a dimer on surface. RBD site located atop PD, but involvement other domains in virus infection uncertain. We found that PD alone, whether anchored membrane via glycosylphosphatidylinositol anchor or attached another protein, fully functional for spike-mediated fusion infection. However, function viral receptor, must be positioned close proximity membrane. Elevating height using long rigid spacers reduces eliminates Moreover, we RBD-targeting neutralizing antibodies, nanobodies, de novo designed miniprotein binders, when present surface, also act receptors, facilitating Our data demonstrate are essential properties effectively mediate Importantly, show soluble RBD-binders can engineered make either susceptible resistant infection, which has significant implications antiviral therapy various virus-mediated applications.

Language: Английский

Citations

1