Articles tagged with Spike Glycoprotein
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Researchers have identified a hidden region on the SARS-CoV-2 Spike protein that is masked by metabolites, making it inaccessible to antibodies. This finding highlights the importance of targeting this region in developing new vaccines.
Researchers have found that SARS-CoV-2 variants from minks can evade inhibition by COVID-19 antibodies, reducing immune control. The study showed that the Y453F mutation in the spike protein reduces the effectiveness of both therapeutic and human-made antibodies.
Large-scale simulations reveal the dominant G form variant of SARS-CoV-2 is more infectious due to its ability to readily bind to its target host receptor. The variant's symmetry in interactions with receptors also makes it more vulnerable to antibody neutralization.
The novel P.1 SARS-CoV-2 lineage emerged in November 2020, exhibiting 17 mutations, including those in the spike protein, making it more transmissible and lethal than its predecessor. Enhanced global genomic surveillance is critical to address increased transmission and immune evasion
Researchers discovered the first full structure of the Nucleocapsid protein, finding that antibody binding sites remain consistent across many coronaviruses, including recent COVID-19 variants.
New research reveals how the immune system influences SARS-CoV-2 evolution, with potential implications for COVID-19 treatment and vaccines. Studies show that immune responses can lead to the emergence of new virus strains, highlighting the need for periodic updates to remain effective.
A new model of the SARS-CoV-2 spike protein reveals potential new vaccine targets, including spots with minimal glycan shielding. The researchers identified novel sites and confirmed their vulnerability through lab experiments.
Researchers found that SARS-CoV-2 variants B.1.351 and P.1 are less inhibited by antibodies from recovered or vaccinated individuals, undermining current vaccination strategy. The study suggests limiting viral spread to control emerging variants.
Research reveals glycans on SARS-CoV-2 spike protein play key role in structural changes during cell invasion. Glycans help stabilize Down-form structure and facilitate change to Up-form upon electrostatic repulsion.
The UK and South Africa coronavirus variants are more contagious and deadly than the original virus due to mutations in their spike protein. The Frontera supercomputer aided in building infection models of these variants.
The D614G mutation stabilizes the spike protein, making it more infectious. Redesigned vaccines incorporating this mutant spike protein may elicit protective neutralizing antibodies.
A new multiscale coarse-grained model of the complete SARS-CoV-2 virion has been developed using supercomputers, providing a holistic understanding of the virus's behavior. The model reveals cooperative motion among spike proteins on the surface of the virus, which is informative of how it explores and detects host cell receptors.
Research reveals how glycans on SARS-CoV-2's surface facilitate activation of the virus by altering spike protein structure. This finding holds potential for identifying treatments to block or prevent viral activation.
Researchers at Ohio State University have developed protein fragments called peptides that effectively bind to the SARS-CoV-2 Spike protein, blocking the virus's ability to access host cells. The team envisions delivering these peptides in nasal sprays or aerosol disinfectants to prevent viral entry.
Scientists have identified potential new therapeutic targets beyond the RBD on the SARS-CoV-2 Spike protein, which may help explain how emerging variants become more infectious. The research could lead to new treatments targeting the S1/S2 cleavage site.
Scientists have detailed a mechanism in the Covid-19 corona that could help find new treatments by identifying promising drug targets. The researchers used computational modeling techniques to simulate movements of nearly 300 protein structures, focusing on the spike protein, which forms the extended corona of the virus.
A study by New York University researchers reveals the D614G mutation in SARS-CoV-2's spike protein renders the virus up to eight times more infectious. The mutation makes the virus more resistant to being cleaved and increases its ability to infect human cells, contributing to rapid spread.
Researchers observed SARS-CoV-2 mutating in a patient with compromised immune system treated with convalescent plasma. The virus developed key mutations similar to the new UK variant, making it more infectious on cells.
The BioNTech-Pfizer COVID-19 vaccine retains its immune protection against the B.1.1.7 viral variant, suggesting it can prevent 'escape' from vaccine-mediated protection. The study's findings support the use of mRNA-based vaccine technology for adapting to new virus strains.
Researchers at the University of Bonn have developed four nanobodies that effectively target the spike protein of SARS-CoV-2, offering a promising therapeutic option. These nanobodies can be produced in large quantities and are less likely to cause unwanted complications, making them an attractive alternative to traditional antibodies.
Researchers have developed a nanoparticle vaccine that elicits a virus-neutralizing antibody response in mice after just one dose. The spike/ferritin nanoparticles may be a viable strategy for single-dose vaccination against COVID-19, suggesting potential improvements over current two-dose regimens.
Researchers at the NIH have isolated promising nanobodies against SARS-CoV-2 that may prevent infections and detect virus particles. The nanobodies were produced by a llama named Cormac and showed high affinity for blocking the spike protein's interaction with human cells.
Researchers have made detailed images of coronavirus spike proteins in their natural state using cryo-EM and computation. The study provides crucial insights into how the virus initiates infections and sheds light on sugar molecule attachments that play a critical role in its life cycle.
A study published in Nature Neuroscience found that SARS-CoV-2's spike protein can cross the blood-brain barrier, suggesting the virus can enter the brain. This could explain many COVID-19 complications, including cognitive effects like brain fog and fatigue.
Researchers found that humans, ferrets, and cats are the most susceptible animals to SARS-CoV-2 infection due to their high binding affinity and codon adaptation index. Ducks, rats, mice, pigs, and chickens had lower or no susceptibility to infection.
The 2020 Golden Goose Award winners made significant breakthroughs in COVID-19 vaccine development, leveraging existing knowledge of coronaviruses and the human immune system. Their research has led to several vaccine candidates currently in Phase 3 clinical trials for effectiveness in preventing COVID-19 infection.
Researchers designed a protein decoy that replicates the spike protein target interface in hACE2, allowing it to neutralize SARS-CoV-2 infection in human cells. The decoy protected Syrian hamsters from lethal doses of the virus with modest weight loss.
Researchers identified nanobodies that bind tightly to the SARS-CoV-2 spike protein, providing a unique prophylactic and therapeutic strategy. These therapeutics have the potential to be produced in bulk from microbes and delivered via aerosol, offering an affordable alternative to monoclonal antibodies.
Researchers from University of Tartu discovered how coronavirus activates before attacking cells and identified a potential target for COVID-19 treatment. The study found that a specific enzyme, furin, plays a crucial role in the virus's life cycle.
A new ultrapotent COVID-19 vaccine candidate, designed via computer, has been shown to produce virus-neutralizing antibodies in mice at levels ten times greater than those seen in people who have recovered from COVID-19 infections. The vaccine candidate also elicited a strong B-cell response after immunization.
SARS-CoV-2 spike proteins can cause inflammation on endothelial cells forming the blood-brain barrier, making it 'leaky' and disrupting neural networks. This could lead to neuroinvasion and neurological manifestations in COVID-19 patients, especially those with pre-existing health conditions.
A joint UC Berkeley-ITU team uses molecular dynamics simulations and single molecule experiments to identify the processes that happen when the virus binds to human cells. They discover intermediate states and specific amino acids that stabilize each state, which may lead to targeted treatments.
A computer model shows that SARS-CoV-2 spike protein's superantigenic features interact with human T cells, leading to a 'cytokine storm' and severe inflammation. Researchers found similarities between this region and bacterial proteins causing toxic shock syndrome.
Researchers identify glycans linked to the SARS-CoV-2 spike protein as key players in infection, stabilizing shape change that exposes receptor-binding domain. Mutations reducing glycanaction can reduce binding to ACE2.
A team of scientists has discovered a druggable pocket in the SARS-CoV-2 Spike protein that could be used to stop the virus from infecting human cells. The pocket, which binds to linoleic acid, plays a crucial role in viral infectivity and is involved in COVID-19 disease progression.
Scientists at Karolinska Institutet have identified a nanobody that can block SARS-CoV-2 from entering human cells, offering potential as an antiviral treatment for COVID-19. The nanobody, Ty1, neutralizes the virus by binding to its spike protein, preventing infection.
The study sheds light on the SARS-CoV-2 spike protein's flexibility and its impact on viral infection. The research reveals that the stalk is extremely flexible, allowing it to move and search for receptors on host cells.
Researchers at Northwestern University have uncovered a new vulnerability in the SARS-CoV-2 spike protein's binding site, which enables the virus to infect host cells. A negatively charged molecule can block this site, inhibiting viral transmission.
A carefully engineered spike protein stabilizer has aided in the development of a new COVID-19 vaccine. The stabilizer, known as S-2P protein, keeps infection from spreading and prompts a helpful immune response.
Researchers identified a promising soluble variant of the human receptor for SARS-CoV-2 that competes with monoclonal antibodies. The variant, dubbed sACE2.v2.4, neutralizes both SARS-CoV-2 and SARS-CoV-1 in cell-based assays.
Researchers at the University of Texas at Austin have successfully redesigned a key protein from the coronavirus, enabling faster and more stable vaccine production. The new design, called HexaPro, produces up to 10 times more protein than an earlier version, potentially reducing vaccine doses or speeding up production.
Researchers have engineered a more stable SARS-CoV-2 spike protein that generates higher yields in the lab, accelerating vaccine development. The new design, called HexaPro, enables industrial production of subunit vaccines and improves DNA or mRNA-based vaccines.
The study captures the spike protein's shape change, showing how it can fuse with host membranes without ACE2 receptor binding. The researchers propose two conformational changes: one dependent on ACE2 and another independent.
Researchers at UC Davis Health are testing a new antibody cocktail, REGN-COV2, to prevent and treat COVID-19. The clinical trial aims to evaluate the efficacy and safety of the REGN-COV2 antibodies in hospitalized adult patients with COVID-19.
Texas A&M University researchers are producing COVID-19 spike proteins to detect antibodies that can block the virus from binding to cells. The goal is to find effective treatments and vaccines against SARS-CoV-2.
Researchers characterised the SARS-CoV-2 spike protein in high resolution and compared it to a bat coronavirus. The study found significant differences at receptor-binding sites, making the SARS-CoV-2 spike more stable and bind to human cells around 1,000 times tighter.
Researchers linked two llama antibodies to create a new antibody that binds tightly to the SARS-CoV-2 spike protein, blocking viruses from infecting cells. The team aims to conduct preclinical studies and eventually test the treatment in humans to develop a potential COVID-19 therapy.
A breakthrough in coronavirus research has led to the creation of a 3D atomic scale map of the part of the virus that attaches to and infects human cells. This mapping is crucial for developing vaccines and antiviral drugs against the 2019 novel coronavirus.
Scientists analyze Wuhan CoV genetic relationship with other coronaviruses and model its spike protein to evaluate human transmission risk. The study suggests bats as the native host of Wuhan CoV, but intermediate hosts may be involved in transmission.
Researchers solved the structure of a key coronavirus protein, revealing its conformation and potential vulnerabilities. This finding could guide future treatments for viruses like SARS and MERS.
Researchers have captured a snapshot of how coronaviruses enter cells using high-resolution cryo-electron microscopy. The atomic model suggests specific vaccine strategies against SARS-CoV and MERS-CoV. A fusion peptide on the outer edge of the spike protein may be an ideal target for neutralizing coronaviruses.
Scientists discovered that a common protease enzyme furin activates MERS-CoV to fuse with cell membranes and enter host cells. Blocking this process could lead to treatment by preventing the virus from infecting cells. The study found two cleavage sites on the spike protein, allowing for more spread in animals or humans.
A team of researchers has captured a high-resolution image of the HIV surface spike protein, revealing its dynamics and structure. This breakthrough provides new information on how the virus infects cells and may lead to the development of more effective treatments.
A study published in Science reveals the structure of the SARS spike protein's interaction with its human receptor, ACE2. The findings provide insights into how small mutations can affect viral transmission and inform potential vaccines.