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Article
Biochemistry & Molecular Biology
Pengcheng Han et al.
Summary: The study found that the omicron variant, unlike other variants, has a similar affinity to the human receptor ACE2 as the prototype variant. Multiple mutations in the omicron variant may compensate for both immune escape and transmissibility. The complex structures of the omicron and delta variants binding to ACE2 provide insights into how specific mutations affect the binding.
Article
Multidisciplinary Sciences
Elisabetta Cameroni et al.
Summary: The Omicron variant of SARS-CoV-2 has raised concerns due to its 37 amino acid substitutions in the spike protein, particularly in the receptor-binding domain (RBD), leading to increased binding affinity with human ACE2. Neutralizing activity against Omicron was greatly reduced in convalescent and vaccinated individuals compared to the ancestral virus, but this decrease was less significant after a third vaccine dose. Broadly neutralizing monoclonal antibodies recognizing conserved RBD epitopes may be crucial in combating the Omicron variant and future zoonotic transmissions.
Article
Multidisciplinary Sciences
Dhiraj Mannar et al.
Summary: The newly reported Omicron variant shows new salt bridges and hydrogen bonds formed by mutated residues in the receptor binding domain, compensating for reduced ACE2 binding affinity. It also exhibits increased antibody evasion, which likely contributes to its rapid spread.
Article
Multidisciplinary Sciences
James W. Saville et al.
Summary: The Delta and Kappa variants of SARS-CoV-2, emerged in India in late 2020, demonstrate antibody escape and enhanced ACE2 binding, which contribute to their global dominance.
NATURE COMMUNICATIONS
(2022)
Article
Multidisciplinary Sciences
Yifan Wang et al.
Summary: The authors use cryo-EM to study the conformational dynamics of the SARS-CoV-2 Delta spike and its interaction with the ACE2 receptor and the Mab 8D3 neutralizing antibody. The study provides insights into the mechanisms of receptor recognition and antibody neutralization for the Delta variant.
NATURE COMMUNICATIONS
(2022)
Review
Immunology
Haolin Liu et al.
Summary: The mutations in the receptor binding domain (RBD) of SARS-CoV-2 variants affect the binding affinity to ACE2 and allow the virus to escape neutralization by antibodies, impacting immunity and treatment efficacy.
FRONTIERS IN IMMUNOLOGY
(2022)
Article
Multidisciplinary Sciences
Mary Hongying Cheng et al.
Summary: In this study, the interactions between SARS-CoV-2 variants (Alpha, Beta, Gamma, and Delta) and host cells, as well as the impact on neutralizing antibodies, were investigated using computational methods and experimental assays. It was found that certain antibodies were ineffective against Beta and Delta variants, while others remained sensitive. Specific substitutions in the Delta variant enhanced binding to host cells and recognition by proteases, facilitating viral entry.
Article
Pharmacology & Pharmacy
Deepa Raghu et al.
Summary: Severe acute respiratory syndrome-associated coronavirus 2 (SARS-CoV-2) is a global health issue and the emergence of spike protein mutations may affect its binding to host cells and the effectiveness of neutralizing antibodies. This study investigated the binding activities of spike protein variants and their interactions with the ACE2 receptor, monoclonal antibodies, and the original spike protein receptor binding domain (RBD) sequence. The findings showed that certain mutants had increased binding affinity to ACE2, while others had reduced affinity. The neutralizing capability of monoclonal antibodies was also assessed, with one antibody showing partial blocking for a specific mutant.
JOURNAL OF PHARMACEUTICAL ANALYSIS
(2022)
Article
Chemistry, Physical
Danyang Xiong et al.
Summary: This study elucidates the binding mechanism of SARS-CoV-2 Delta variant, which has increased infectivity, through molecular dynamics simulations and energy analysis. The study also provides a preliminary evaluation of the changes in the binding ability of Delta variant with neutralizing monoclonal antibodies. The findings offer important theoretical insights for the development of novel targeted RBD drugs and antibodies.
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
(2022)
Article
Chemistry, Physical
Xiaoyu Zhao et al.
Summary: This study used molecular dynamics simulations to investigate the binding mode differences between the Omicron variant and ACE2. It found that the multi-point mutations in the Omicron variant led to conformational changes and tighter binding. The stronger electrostatic interactions were the main reason for the enhanced binding affinity. The study also revealed that these mutations may affect the virus's sensitivity to antibodies.
PHYSICAL CHEMISTRY CHEMICAL PHYSICS
(2022)
Article
Immunology
Karen Colwill et al.
Summary: This study describes a scalable solution to detect and quantify SARS-CoV-2 antibodies, discriminate between natural infection and vaccination-induced responses, and assess the inhibitory effect of antibodies on ACE2-spike interaction. They developed methods and reagents for antibody detection using ELISA and snELISA, enabling large-scale analysis. In addition, they provided detailed protocols for the experiments.
CLINICAL & TRANSLATIONAL IMMUNOLOGY
(2022)
Correction
Chemistry, Physical
Seonghan Kim et al.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION
(2022)
Article
Biotechnology & Applied Microbiology
Matthew Stuible et al.
Summary: Recombinant forms of the spike protein of SARS-CoV-2 and related viruses have proven difficult to produce with good yields in mammalian cells. However, through exploring new transient gene expression methods and a high-cell-density protocol using specific cells, researchers have successfully produced highly homogenous preparations of full-length spike protein with good yields. The efficient two-step affinity purification method developed in this study also contributed to the high productivity of the production process.
JOURNAL OF BIOTECHNOLOGY
(2021)
Article
Chemistry, Physical
Seonghan Kim et al.
Summary: This study investigated the binding interactions between ACE2 and RBD of different SARS-CoV-2 variants, finding that the Alpha variant requires the highest force to detach, while the Epsilon variant is relatively easily detached. The results shed light on the mechanisms of transmission for each variant.
JOURNAL OF CHEMICAL THEORY AND COMPUTATION
(2021)
Article
Biophysics
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)
Article
Biochemistry & Molecular Biology
Piyada Supasa et al.
Summary: Research on the UK-dominant variant B.1.1.7 shows that it is harder to neutralize than the parental virus, but widespread escape from antibodies or monoclonal antibodies has not been observed yet.
Article
Biochemistry & Molecular Biology
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)
Article
Multidisciplinary Sciences
Dhiman Ray et al.
Summary: Researchers are focusing on the correlation between the RBD region of the SARS-CoV-2 virus and residues distant from it to understand molecular recognition events and predict key mutations for therapeutics. Their model can identify multiple residues with long-distance coupling with the RBD opening and successfully predict some key mutations.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2021)
Article
Multidisciplinary Sciences
Chen Chen et al.
Summary: This study presents a two-step framework using molecular dynamics trajectories and neural networks to predict the effects of amino acid changes on the binding affinity between RBD and hACE2. The computational model achieved a validation accuracy of 82.8% for classifying single-amino acid substitution variants and a correlation coefficient of 0.73 between predicted and experimentally calculated binding affinities changes.
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
(2021)
Article
Multidisciplinary Sciences
Matthew McCallum et al.
Summary: The transmission of SARS-CoV-2 leads to the emergence of variants, such as the B.1.617.2 (Delta) variant, which dampens the in vitro potency of vaccine-elicited serum neutralizing antibodies. Mutations in the B.1.617.1 (Kappa) and Delta spike glycoproteins alter key antigenic sites, affecting the recognition by monoclonal antibodies. The angiotensin-converting enzyme 2 binding affinities of Kappa and Delta are comparable to the Wuhan-Hu-1 isolate, while Delta+ exhibits significantly reduced affinity.
Article
Multidisciplinary Sciences
Seiya Ozono et al.
Summary: The naturally occurring mutations of SARS-CoV-2 spike protein can affect cell entry, with the D614G mutation resulting in increased cell entry and maintaining susceptibility to neutralization by antisera against prototypic viruses. Further global surveillance is needed to understand the transmissibility of SARS-CoV-2 among humans.
NATURE COMMUNICATIONS
(2021)
Article
Multidisciplinary Sciences
Amit Singh et al.
Summary: Studies on the structural mechanism of the novel coronavirus SARS-CoV-2 have identified the importance of amino acid residue S477 in the binding process with the hACE2 receptor, with its mutations S477G and S477N enhancing the binding of the spike protein to the receptor.
SCIENTIFIC REPORTS
(2021)
Article
Multidisciplinary Sciences
Pengcheng Han et al.
Summary: Multiple SARS-CoV-2 variants, including Alpha, Beta, and Gamma, were studied in terms of their interactions with the human ACE2 receptor. The study identified key residues in the receptor-binding domain that affect binding affinity and demonstrated the potential of soluble ACE2 protein in preventing viral entry. The findings could contribute to the development of novel therapeutic and prophylactic agents targeting these emerging mutants.
NATURE COMMUNICATIONS
(2021)
Letter
Cell Biology
Haolin Liu et al.
Article
Biochemistry & Molecular Biology
Hin Hark Gan et al.
Summary: The study reveals that new variants of the SARS-CoV-2 Spike protein show enhanced binding affinity to the human ACE2 receptor, potentially increasing transmissibility. Structural analysis predicts variant combinations with both enhanced affinity and antibody resistance, highlighting the complexity of viral evolution and potential impact on intervention strategies.
JOURNAL OF MOLECULAR BIOLOGY
(2021)
Article
Multidisciplinary Sciences
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)
Article
Virology
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.
Article
Virology
Ieva Bagdonaite et al.
Summary: Enveloped viruses hijack host glycosylation machinery and cover viral surface proteins with host-like structures. A study mapped O-glycosylation sites on SARS-CoV-2 surface protein S, identifying 25 sites primarily located near N-glycosites. O-glycosylation was found on unoccupied peptide regions and had negligible effects on subunit vaccine design.
Article
Biochemistry & Molecular Biology
Kefang Liu et al.
Summary: Research has shown that the SARS-CoV-2 virus may originate from bats, with genetic sequences closely related to RaTG13. Experiments revealed that residue 501 plays a key role in determining the potential host range of RaTG13. Additionally, it was found that SARS-CoV-2 can induce strong cross-reactive antibodies and a monoclonal antibody capable of cross-neutralizing RaTG13.
Review
Biochemistry & Molecular Biology
Catherine Forest-Nault et al.
Summary: Surface plasmon resonance (SPR)-based optical biosensors play a crucial role in studying the quality attributes of monoclonal antibodies (mAbs), particularly the influence of N-glycosylation on IgG-Fc gamma R interactions. Discrepancies in research conclusions are partly attributed to experimental design and data analysis methods in SPR assays. Recent advancements in SPR analysis methods and glycoprofile control strategies are promising for a better understanding of IgG-Fc gamma R interactions.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Microbiology
Veronika Tchesnokova et al.
Summary: A recent global expansion of various independent SARS-CoV-2 variants with mutation L452R in the spike protein's receptor-binding domain has been reported. The emergence of these variants, including epsilon, delta, kappa, iota, and lambda, has been associated with increased viral transmissibility, infectivity, and pathogenicity due to the L452R mutation near the ACE2 interaction interface.
JOURNAL OF CLINICAL MICROBIOLOGY
(2021)
Article
Biochemistry & Molecular Biology
Charlie Laffeber et al.
Summary: Different mutations in new variants of SARS-CoV-2 have varying effects on receptor binding affinity, viral transmission, and immune evasion, highlighting the importance of global viral genome surveillance and functional characterization.
JOURNAL OF MOLECULAR BIOLOGY
(2021)
Review
Microbiology
William T. Harvey et al.
Summary: The evolution of SARS-CoV-2 has been characterized by the emergence of mutations and variants that impact virus characteristics. Manufacturers are preparing for possible updates to vaccines in response to changes in the virus population, and it is crucial to monitor genetic and antigenic changes alongside experiments to understand the impacts of mutations.
NATURE REVIEWS MICROBIOLOGY
(2021)
Article
Multidisciplinary Sciences
Zengyuan Zhang et al.
Summary: The study found that the spike protein receptor binding domain (RBD) of SARS-CoV-2 can bind to the receptor of dog angiotensin-converting enzyme 2 (dACE2), allowing both pseudotyped and authentic SARS-CoV-2 to infect cells expressing dACE2. Additionally, important mutations in the RBD binding interface are identified to play a pivotal role in the binding affinity of RBD to both dACE2 and hACE2, providing insights into potential animal spread and cross-species transmission of SARS-CoV-2.
NATURE COMMUNICATIONS
(2021)
Article
Biology
Michael Barton et al.
Summary: The study analyzed the effects of mutations in the Spike protein of SARS-CoV-2 on its interaction with ACE2, finding that most mutations increased affinity with ACE2. Two ACE2 mutations were also found to enhance binding with the Spike protein.
Article
Biology
Fang Tian et al.
Summary: Research indicates that the N501Y mutation in SARS-CoV-2 variants strengthens its interaction with ACE2, leading to an increased transmission rate, highlighting the need for close monitoring of future mutations in the virus' RBD.
Article
Immunology
Ashlesha Deshpande et al.
Summary: This study investigated the impact of RBD mutations in SARS-CoV-2 on ACE2 and NAb binding, revealing that mutations such as K417T, E484K, and N501Y disrupted the binding of 65% of evaluated NAbs, indicating concern for the P.1 Japan/Brazil strain. Additionally, the L452R mutation enhanced ACE2 binding affinity while disrupting C1 and C2 NAb classes.
FRONTIERS IN IMMUNOLOGY
(2021)
Article
Microbiology
Sarah Cherian et al.
Summary: Genomic epidemiology and whole genome sequencing were used to investigate the transmission and evolution of the SARS-CoV-2 virus during the global pandemic. The study identified new variants B.1.617.1 and B.1.617.2 in India, responsible for the second wave of COVID-19 in Maharashtra, with B.1.617.2 designated as a VOC delta and B.1.617.1 as a variant of interest kappa. Monitoring of these and emerging variants in India is crucial for public health.
Review
Biochemistry & Molecular Biology
Angel Yun-Kuan Thye et al.
Summary: The battle against the SARS-CoV-2 virus continues globally, with various clinically significant variants emerging, including Alpha, Beta, Delta, and Gamma. These variants possess key mutations on the spike protein, which contribute to increased transmissibility and evasion of the host immune response, leading to detrimental effects on public health.
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Multidisciplinary Sciences
Daniel Wrapp et al.
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Biochemistry & Molecular Biology
Qihui Wang et al.
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Multidisciplinary Sciences
Jian Shang et al.
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Medicine, Research & Experimental
Florian Cambay et al.
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Multidisciplinary Sciences
Robert N. Kirchdoerfer et al.
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(2018)
Article
Engineering, Biomedical
Frederic Murschel et al.
ACTA BIOMATERIALIA
(2013)
Article
Cell & Tissue Engineering
Gregory De Crescenzo et al.
CELLULAR AND MOLECULAR BIOENGINEERING
(2008)
Article
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CH Shi et al.
Article
Biochemistry & Molecular Biology
G De Crescenzo et al.
Article
Biochemical Research Methods
JR Litowski et al.
JOURNAL OF PEPTIDE RESEARCH
(2001)
Article
Biochemical Research Methods
M Ben Khalifa et al.
ANALYTICAL BIOCHEMISTRY
(2001)
Review
Biochemical Research Methods
RL Rich et al.
CURRENT OPINION IN BIOTECHNOLOGY
(2000)
