Entropic contribution of ACE2 glycans to RBD binding

Article Chemistry, Multidisciplinary

The Role of Host Cell Glycans on Virus Infectivity: The SARS-CoV-2 Case

Silvia Acosta-Gutierrez et al.

Summary: Glycans play a critical role in modulating the interaction between viruses and cells. By balancing the interactions between specific host receptors and glycan chains on viral proteins, viral tropism can be predicted.

ADVANCED SCIENCE (2023)

Add to Collection

Article Biochemistry & Molecular Biology

Structural remodeling of SARS-CoV-2 spike protein glycans reveals the regulatory roles in receptor-binding affinity

Yen-Pang Hsu et al.

Summary: The glycans of SARS-CoV-2 spike protein play functional roles in the infection process and are highly conserved. Glycosylation of the receptor-binding domain (RBD) of the spike protein can be controlled and simplified through glycoengineering, affecting its behavior and interaction with host receptors. The antibody S309 can neutralize the impact of different RBD glycoforms on receptor binding affinity.

GLYCOBIOLOGY (2023)

Add to Collection

Article Biophysics

SARS-CoV-2 spike binding to ACE2 is stronger and longer ranged due to glycan interaction

Yihan Huang et al.

Summary: Highly detailed steered molecular dynamics simulations were conducted on differently glycosylated receptor binding domains of the SARS-CoV-2 spike protein. Glycosylation increased the binding strength and range, and a catch-slip behavior was observed during protein pulling, where new interactions replaced broken interactions. Hydrogen bonds were the dominant interaction mode, while Lennard-Jones and electrostatic interactions were also relevant.

BIOPHYSICAL JOURNAL (2022)

Add to Collection

Article Biochemistry & Molecular Biology

Sialic acid-containing glycolipids mediate binding and viral entry of SARS-CoV-2

Linh Nguyen et al.

Summary: Evidence suggests that host glycans, specifically glycolipids containing sialic acid, play a role in facilitating the entry of SARS-CoV-2 virus into host cells by binding to the receptor-binding domain (RBD) of the spike protein. Depletion of cell surface sialic acid levels through various methods decreases RBD binding and infection of the virus, indicating the importance of sialylated glycans in viral entry.

NATURE CHEMICAL BIOLOGY (2022)

Add to Collection

Article Biology

ACE2 N-glycosylation modulates interactions with SARS-CoV-2 spike protein in a site-specific manner

Ayana Isobe et al.

Summary: This study investigates the importance of ACE2 glycosylation in the interaction between SARS-CoV-2 virus and ACE2 receptor. The findings demonstrate that the deletion of glycosylation sites results in significant changes in the interaction with spike protein and is consistent across viral variants.

COMMUNICATIONS BIOLOGY (2022)

Add to Collection

Article Engineering, Multidisciplinary

Mass Spectrometry Analysis of Newly Emerging Coronavirus HCoV-19 Spike Protein and Human ACE2 Reveals Camouflaging Glycans and Unique Post-Translational Modifications

Zeyu Sun et al.

Summary: This study uncovered the glycan and post-translational modification profiles of the HCoV-19 virus spike protein and hACE2, providing important structural details for understanding the virus's biological traits and developing therapeutics and vaccines.

ENGINEERING (2021)

Add to Collection

Article Biophysics

Biomechanical characterization of SARS-CoV-2 spike RBD and human ACE2 protein-protein interaction

Wenpeng Cao et al.

Summary: This study utilizes single-molecule force spectroscopy and molecular dynamics simulations to quantify the interactions between SARS-CoV-2 or SARS-CoV-1 RBD and ACE2, revealing that the N-linked glycan interaction plays a crucial role in the binding difference between the two viruses. The study uncovers the mechanism behind ACE2 binding disparity and provides insights for developing new strategies to inhibit SARS-CoV-2 entry.

BIOPHYSICAL JOURNAL (2021)

Add to Collection

Article Biochemistry & Molecular Biology

Subtle Influence of ACE2 Glycan Processing on SARS-CoV-2 Recognition

Joel D. Allen et al.

Summary: The severity of SARS-CoV-2 infection varies greatly, but the molecular basis for this variability remains unclear. Differences in glycosylation of target human cells may be a contributing factor. Research shows that the glycosylation state of ACE2 has a subtle impact on interaction with SARS-CoV-2, but overall, it does not significantly influence viral spike binding.

JOURNAL OF MOLECULAR BIOLOGY (2021)

Add to Collection

Article Biology

Structure-guided glyco-engineering of ACE2 for improved potency as soluble SARS-CoV-2 decoy receptor

Tuemay Capraz et al.

Summary: The interaction between the Spike protein of SARS-CoV-2 and ACE2 on host cells is crucial for viral entry, with glycosylation playing a critical role. Engineering ACE2 glycosylation can enhance virus neutralization without affecting protein stability or activity. Removing all N-glycans from recombinant soluble human ACE2 can create a superior decoy receptor for effective COVID-19 treatment.

ELIFE (2021)

Add to Collection

Article Biophysics

The flexibility of ACE2 in the context of SARS-CoV-2 infection

Emilia P. Barros et al.

Summary: The COVID-19 pandemic has caused significant loss of life worldwide, and there are still unanswered questions regarding the viral association to ACE2 receptor. Molecular dynamics simulations reveal the flexibility of the ACE2 receptor and its dynamics on the cell surface, which could provide insights for the development of therapeutics against SARS-CoV-2.

BIOPHYSICAL JOURNAL (2021)

Add to Collection

Article Multidisciplinary Sciences

Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike

Ahmad Reza Mehdipour et al.

Summary: Glycosylation of the human ACE2 receptor plays a substantial role in the binding of the SARS-CoV-2 virus. Glycans at the N90 and N322 sites have opposite effects on spike protein binding, with the N90 glycan interfering with binding and the N322 glycan strengthening the complex. Additionally, the N322 glycan binds to a conserved region of the spike protein that has been identified as a cryptic epitope for a neutralizing antibody, showing potential for the development of targeted neutralizing antibodies and fusion inhibitors against SARS-CoV-2.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2021)

Add to Collection

Article Virology

Exploring the Role of Glycans in the Interaction of SARS-CoV-2 RBD and Human Receptor ACE2

Kien Nguyen et al.

Summary: COVID-19, caused by the novel coronavirus SARS-CoV-2, has become a global pandemic with challenges for vaccine development due to frequent mutations. Understanding the interaction between the Spike RBD and human host cell receptor ACE2 is crucial for therapeutic strategies.

VIRUSES-BASEL (2021)

Add to Collection

Article Biology

Human ACE2 receptor polymorphisms and altered susceptibility to SARS-CoV-2

Kushal Suryamohan et al.

Summary: This study analyzed genetic data and identified ACE2 variants that can potentially alter host susceptibility to SARS-CoV-2. Specific ACE2 variants were predicted to either increase susceptibility or provide protection against the virus by altering the interaction between the virus and host cells. Further biochemical assays confirmed the effects of these ACE2 variants on the affinity for the viral spike protein, suggesting that these genetic variations can modulate susceptibility to COVID-19.

COMMUNICATIONS BIOLOGY (2021)

Add to Collection

Article Chemistry, Multidisciplinary

A glycan gate controls opening of the SARS-CoV-2 spike protein

Terra Sztain et al.

Summary: Through simulations, the study reveals the mechanism of spike protein receptor binding domain (RBD) opening in SARS-CoV-2 infection, highlighting the crucial role of N-glycan in facilitating RBD opening. This research represents a milestone in ensemble pathway simulations and provides a foundation for understanding the fundamental mechanisms of viral entry and infection.

NATURE CHEMISTRY (2021)

Add to Collection

Article Microbiology

Analysis of the Role of N-Linked Glycosylation in Cell Surface Expression, Function, and Binding Properties of SARS-CoV-2 Receptor ACE2

Raymond Rowland et al.

Summary: The study highlights the importance of N-glycosylation for proper cell surface expression of ACE2, with no effect on its carboxiprotease activity. The binding of SARS-CoV and SARS-CoV-2 to ACE2 was not affected by deglycosylation. N-glycosylation was found to reduce cell-to-cell fusion mediated by SARS-CoV but not SARS-CoV-2.

MICROBIOLOGY SPECTRUM (2021)

Add to Collection

Article Biochemistry & Molecular Biology

Comprehensive characterization of N- and O-glycosylation of SARS-CoV-2 human receptor angiotensin converting enzyme 2

Asif Shajahan et al.

Summary: The emergence of the COVID-19 pandemic caused by SARS-CoV-2 has led to the development of new therapeutic strategies, with a focus on understanding the viral attachment, entry, and replication mechanisms. Analysis of glycomic and glycoproteomic profiles of human angiotensin converting enzyme 2 (hACE2) provides insight into viral binding and entry, aiding in the development of novel therapeutics. Studying the site-specific glycosylation of hACE2 and its role in virus-receptor interactions is crucial for understanding the complications of COVID-19 patients with different demographics and pre-existing conditions.

GLYCOBIOLOGY (2021)

Add to Collection

Article Chemistry, Multidisciplinary

ACE2 glycans preferentially interact with SARS-CoV-2 over SARS-CoV

Atanu Acharya et al.

Summary: The study reveals a distinct difference in the interactions of the glycans of the host-cell receptor ACE2 with the SARS-CoV-2 and SARS-CoV S-protein receptor-binding domains. It suggests that specific glycans on ACE2 may enhance or block interactions with the receptor-binding domains of the coronaviruses, potentially impacting infection outcomes. The absence of a glycosylation site in the SARS-CoV-2 RBD may contribute to its enhanced binding with ACE2.

CHEMICAL COMMUNICATIONS (2021)

Add to Collection

Article Multidisciplinary Sciences

A pneumonia outbreak associated with a new coronavirus of probable bat origin

Peng Zhou et al.

NATURE (2020)

Add to Collection

Article Biochemical Research Methods

SciPy 1.0: fundamental algorithms for scientific computing in Python

Pauli Virtanen et al.

NATURE METHODS (2020)

Add to Collection

Article Multidisciplinary Sciences

Cryo-EM structure of the 2019-nCoV spike in the prefusion conformation

Daniel Wrapp et al.

SCIENCE (2020)

Add to Collection

Article Biochemistry & Molecular Biology

Structural and Functional Basis of SARS-CoV-2 Entry by Using Human ACE2

Qihui Wang et al.

CELL (2020)

Add to Collection

Article Biochemistry & Molecular Biology

Structure, Function, and Antigenicity of the SARS-CoV-2 Spike Glycoprotein

Alexandra C. Walls et al.

CELL (2020)

Add to Collection

Article Biochemistry & Molecular Biology

SARS-CoV-2 Cell Entry Depends on ACE2 and TMPRSS2 and Is Blocked by a Clinically Proven Protease Inhibitor

Markus Hoffmann et al.

CELL (2020)

Add to Collection

Article Multidisciplinary Sciences

Site-specific glycan analysis of the SARS-CoV-2 spike

Yasunori Watanabe et al.

SCIENCE (2020)

Add to Collection

Article Biochemistry & Molecular Biology

SARS-CoV-2 Infection Depends on Cellular Heparan Sulfate and ACE2

Thomas Mandel Clausen et al.

CELL (2020)

Add to Collection

Article Microbiology

Virus-Receptor Interactions of Glycosylated SARS-CoV-2 Spike and Human ACE2 Receptor

Peng Zhao et al.

CELL HOST & MICROBE (2020)

Add to Collection

Article Multidisciplinary Sciences

Development and simulation of fully glycosylated molecular models of ACE2-Fc fusion proteins and their interaction with the SARS-CoV-2 spike protein binding domain

Austen Bernardi et al.

PLOS ONE (2020)

Add to Collection

Article Multidisciplinary Sciences

Engineering human ACE2 to optimize binding to the spike protein of SARS coronavirus 2

Kui K. Chan et al.

SCIENCE (2020)

Add to Collection

Article Multidisciplinary Sciences

Analysis of the SARS-CoV-2 spike protein glycan shield reveals implications for immune recognition

Oliver C. Grant et al.

SCIENTIFIC REPORTS (2020)

Add to Collection

Article Chemistry, Multidisciplinary

Beyond Shielding: The Roles of Glycans in the SARS-CoV-2 Spike Protein

Lorenzo Casalino et al.

ACS CENTRAL SCIENCE (2020)

Add to Collection

Article Biochemistry & Molecular Biology

Deducing the N- and O-glycosylation profile of the spike protein of novel coronavirus SARS-CoV-2

Asif Shajahan et al.

GLYCOBIOLOGY (2020)

Add to Collection

Article Biology

Inhibition of SARS-CoV-2 viral entry upon blocking N- and O-glycan elaboration

Qi Yang et al.

ELIFE (2020)

Add to Collection

Article Virology

Virus recognition of glycan receptors

Andrew J. Thompson et al.

CURRENT OPINION IN VIROLOGY (2019)

Add to Collection

Article Chemistry, Multidisciplinary

Minimizing the Entropy Penalty for Ligand Binding: Lessons from the Molecular Recognition of the Histo Blood-Group Antigens by Human Galectin-3

Ana Gimeno et al.

ANGEWANDTE CHEMIE-INTERNATIONAL EDITION (2019)

Add to Collection

Article Biochemistry & Molecular Biology

Crystal Structure of a Homogeneous IgG-Fc Glycoform with the N-Glycan Designed to Maximize the Antibody Dependent Cellular Cytotoxicity

Chia-Lin Chen et al.

ACS CHEMICAL BIOLOGY (2017)

Add to Collection

Article Virology

Targeting host-derived glycans on enveloped viruses for antibody-based vaccine design

Max Crispin et al.

CURRENT OPINION IN VIROLOGY (2015)

Add to Collection

Review Biochemistry & Molecular Biology

The intrinsic and extrinsic effects of N-linked glycans on glycoproteostasis

Daniel N. Hebert et al.

NATURE CHEMICAL BIOLOGY (2014)

Add to Collection

Review Chemistry, Multidisciplinary

Role of Water in Protein Aggregation and Amyloid Polymorphism

D. Thirumalai et al.

ACCOUNTS OF CHEMICAL RESEARCH (2012)

Add to Collection

Article Chemistry, Physical

CHARMM Additive All-Atom Force Field for Glycosidic Linkages in Carbohydrates Involving Furanoses

E. Prabhu Raman et al.

JOURNAL OF PHYSICAL CHEMISTRY B (2010)

Add to Collection

Article Physics, Multidisciplinary

Factors Governing Fibrillogenesis of Polypeptide Chains Revealed by Lattice Models

Mai Suan Li et al.

PHYSICAL REVIEW LETTERS (2010)

Add to Collection

Article Biochemistry & Molecular Biology

Principles of protein folding - A perspective from simple exact models

Ken A. Dill et al.

PROTEIN SCIENCE (2010)

Add to Collection

Review Biochemistry & Molecular Biology

Folding of glycoproteins: toward understanding the biophysics of the glycosylation code

Dalit Shental-Bechor et al.

CURRENT OPINION IN STRUCTURAL BIOLOGY (2009)

Add to Collection

Review Chemistry, Medicinal

Effects of Glycosylation on the Stability of Protein Pharmaceuticals

Ricardo J. Sola et al.

JOURNAL OF PHARMACEUTICAL SCIENCES (2009)

Add to Collection

Article Multidisciplinary Sciences

Effect of glycosylation on protein folding: A close look at thermodynamic stabilization

Dalit Shental-Bechor et al.

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA (2008)

Add to Collection

Article Biotechnology & Applied Microbiology

Engineering of protein thermodynamic, kinetic, and colloidal stability:: Chemical glycosylation with monofunctionally activated glycan

Ricardo J. Sola et al.

BIOTECHNOLOGY AND BIOENGINEERING (2006)

Add to Collection

Entropic contribution of ACE2 glycans to RBD binding

Related references

Export Citation

Share Paper