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Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
The glycosylation in SARS-CoV-2 and its receptor ACE2
Yanqiu Gong1, Suideng Qin2, Lunzhi Dai3
1National Clinical Research Center for Geriatrics and Department of General Practice, State Key Laboratory of Biotherapy, West China Hospital, Sichuan University, and Collaborative Innovation Center of Biotherapy, 610041, Chengdu, China.
Abstract:
Coronavirus disease 2019 (COVID-19), a highly infectious disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has infected more than 235 million individuals and led to more than 4.8 million deaths worldwide as of October 5 2021. Cryo-electron microscopy and topology show that the SARS-CoV-2 genome encodes lots of highly glycosylated proteins, such as spike (S), envelope (E), membrane (M), and ORF3a proteins, which are responsible for host recognition, penetration, binding, recycling and pathogenesis. Here we reviewed the detections, substrates, biological functions of the glycosylation in SARS-CoV-2 proteins as well as the human receptor ACE2, and also summarized the approved and undergoing SARS-CoV-2 therapeutics associated with glycosylation. This review may not only broad the understanding of viral glycobiology, but also provide key clues for the development of new preventive and therapeutic methodologies against SARS-CoV-2 and its variants.
Insights
Glycosylation of SARS-CoV-2 proteins and ACE2 is crucial for viral pathogenesis. Understanding this viral glycobiology offers new therapeutic strategies against COVID-19 and its variants.
Area of Science:
- Virology
- Glycobiology
- Structural Biology
Background:
- Coronavirus disease 2019 (COVID-19), caused by SARS-CoV-2, has led to a global health crisis.
- SARS-CoV-2 possesses highly glycosylated proteins (spike, envelope, membrane, ORF3a) essential for viral functions.
- Glycosylation plays a significant role in viral entry, pathogenesis, and immune evasion.
Purpose of the Study:
- To review the detection, substrates, and biological functions of glycosylation in SARS-CoV-2 proteins and human ACE2.
- To summarize current and emerging therapeutics targeting glycosylation in SARS-CoV-2.
- To provide insights into viral glycobiology for developing novel anti-SARS-CoV-2 strategies.
Main Methods:
- Literature review of studies on SARS-CoV-2 glycosylation.
- Analysis of structural data (cryo-electron microscopy) and topological information.
- Compilation of information on therapeutic interventions related to glycosylation.
Main Results:
- Glycosylation affects critical viral processes including host cell recognition and entry.
- ACE2, the human receptor for SARS-CoV-2, is also glycosylated, influencing viral binding.
- Various therapeutic approaches targeting viral glycosylation are under investigation.
Conclusions:
- A comprehensive understanding of SARS-CoV-2 glycosylation is vital for combating the pandemic.
- Targeting viral and host glycosylation presents a promising avenue for developing effective COVID-19 treatments.
- Further research into viral glycobiology can accelerate the development of antivirals and vaccines against SARS-CoV-2 and its future variants.
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