Articles tagged with Capsids
The study reveals differences in protein arrangement between immature Zika and other flaviviruses, shedding light on the virus's role in infection and disease. Understanding the structure of the immature form could help develop effective antiviral treatments and vaccines for diseases like microcephaly.
Scientists created a coarse-grained model of the Cowpea Chlorotic Mottle Virus (CCMV) capsid and applied forces to it. This allowed them to see how the capsid broke apart, providing clues about its assembly process. The study reveals that weaker protein-protein contacts assemble first, followed by stronger ones.
Scientists have discovered a key component of the HIV virus that it uses to infect cells while avoiding detection by the immune system. They identified iris-like pores in the capsid shell that suck in nucleotides needed for replication, explaining why HIV is successful at evading the immune system.
University of Chicago scientists developed a computer model of HIV that gives real insight into how the virus matures and becomes infective. The model reveals critical proteins inside the bud are cut into bits by the enzyme HIV protease, which can be targeted by anti-viral drugs.
Researchers propose that DNA shape changes can produce strong forces, a new target for antiviral drugs. The 'scrunched' DNA mechanism could help block viral replication by invading viral shells.
Researchers have gained a clearer understanding of how HIV defeats a cellular defender by interacting with cyclophilin A. The study reveals that the virus uses cyclophilin A as a disguise to trick the cellular protein, allowing it to enter the nucleus and commandeer the cell.
Researchers at UMMS have identified a new life cycle stage in HIV infection, dubbed intra-nuclear migration, which relies on human protein CPSF6 to guide the virus through the host cell's nucleus. This phase was previously unappreciated and sheds light on early events of HIV infection.
A Stanford team re-engineered a virus to create a smart particle that can deliver therapeutic payloads to specific cells. By adding molecular tags, the particles can target diseased areas while leaving healthy tissue alone.
Researchers at the University of Missouri captured detailed images of the capsid protein in its natural state, revealing ordered water molecules that help stabilize the complex scaffold. This discovery aims to inform the development of new and more effective antiviral drugs.
Uruguayan researchers have observed the three-dimensional structure of the capsid of Bovine Leukemia Virus (BLV) with high resolution, revealing its flexibility and key regions. This breakthrough can lead to new antiviral medicines for diseases caused by retroviruses.
Researchers found that even minimal mutations in viral RNA can make it too bulky for the capsid, preventing replication. The study used computer simulations and verified previous research on optimized RNA packing.
Researchers have identified how PF74 and CPSF6 molecules bind to HIV-1's capsid, preventing its disassembly. This process can be targeted for therapeutic purposes in HIV-1 infections, potentially blocking viral replication.
Researchers discovered flu virus exploits aggresome, a cellular waste bundle, to release genetic material. The process takes 20-30 minutes and is gradual, with the virus tricking the waste pickup and disposal system.
Berkeley lab researchers have discovered that the viral packaging motor rotates DNA in response to changing conditions, a crucial process for viral replication. This finding could lead to new strategies for combating viral infections and designing more effective drugs.
Researchers identified weak points in capsids and inferred spontaneous assembly processes, discovering each shell is made of protein 'tiles' that spontaneously join up like Lego pieces.
Researchers have developed a bioengineered decoy that fools the immune system and prevents it from neutralizing the benefits delivered by a corrective gene. The approach could potentially increase the number of patients who can be treated with gene therapy, offering new hope for genetic diseases like hemophilia.
Researchers at Brandeis University have developed a sophisticated computational model that helps scientists understand how viruses spread by analyzing genomic data, virus structure, and capsid formation. The team's tool predicts key structural features of the virus genome and controls capsid assembly.
Researchers used computer simulations to study how HIV-1 virus creates its capsid, a protective armor around the viral genome. The simulations provide new insights into the process, which could lead to better understanding and prevention of infection.
A team led by Peijun Zhang has described the 4-million-atom structure of HIV's capsid protein shell, revealing critical molecular interactions that could lead to new treatments. The findings may enable the development of drugs that disrupt the shell's assembly or disassembly, potentially stopping the virus from replicating.
Scientists have determined the precise chemical structure of the HIV capsid using a combination of laboratory techniques and computational simulations. The resulting structure revealed 216 protein hexagons and 12 protein pentagons, which work together to form the cone-shaped capsid.
Researchers have developed antiviral drugs for other enteroviruses that cause the common cold. The new work obtained a near-atomic-scale resolution three-dimensional structure of enterovirus 71 binding with an inhibitor called WIN 51711. This study provides a structural basis for development of antienterovirus 71 capsid-binding drugs.
A new model reveals that viruses construct intermediate structures before final capsid production, outperforming direct assembly in efficiency. This method allows the viral genome to be protected and propagated successfully, even without host cells.
A team of researchers has made significant strides in understanding the life cycle of flaviviruses, including the dengue fever virus, which causes viral hemorrhagic fever and affects millions worldwide. The study provides new insights into the molecular details of viral replication and interactions with host cells.
Researchers at Scripps Research and UVa determine the structure of HIV's protein package, also known as the capsid. The detailed description provides a roadmap for developing drugs that can disrupt its formation and prevent infection. The study uses X-ray crystallography to reveal the flexibility and mobility of the capsid's components.
Researchers at the University of Pittsburgh School of Medicine have identified a functional importance seam in the HIV coat that could lead to new treatments for blocking HIV infection. The findings may allow scientists to rationally design therapeutic compounds that interfere with assembly and function of the protein.
The study reveals the atomic structure of the hepatitis E protein shell, which could lead to new ways to stop the virus. Researchers have identified potential sites on the model for designing drugs that can interrupt the binding process and prevent the virus from attaching to cell receptors.
Scientists have revealed the structure of the HIV protein shell, providing a close-up look at its unique honeycomb arrangement. The discovery may help identify new ways to block HIV infection and develop novel therapeutic strategies.
Researchers from Purdue University have determined key structural features of the mimivirus, a possible 'missing link' between viruses and living cells. The findings revealed a starfish-shaped structure that covers a special vertex where genetic material leaves the virus to infect its host.
Researchers have determined key structural features of the mimivirus, a giant virus large enough to be seen with a light microscope. The findings reveal a starfish-shaped structure that covers a special vertex where the genetic material leaves the virus to infect its host.
Researchers at Rice University have created a precise image of a virus' protective coat, containing 5 million atoms. The image provides the clearest picture yet of the viruses' genome-encasing shell called a 'capsid', which could lead to new approaches for antiviral therapies and gene delivery.
A recent study found a nanoscale motor in the T4 virus, which drives DNA packaging into its capsid. This discovery could inspire engineers designing sophisticated nanomachines and may also help pharmaceutical companies develop methods to sabotage virus machinery.
Researchers used laser tweezers to measure the forces exerted by a virus's motor as it pushes DNA into its capsid. The study found that positively charged ions play a critical role in overcoming electrostatic repulsion, allowing the virus to inject genetic material into bacterial cells.
Biologists have determined the structure of an enzyme that powers 'molecular motors' in viruses, allowing for better understanding of DNA packaging. The motor, essential for inserting DNA into viral capsids, has been likened to a house-building process.
A team of researchers investigated the mechanism of phage DNA packaging, directly testing the connector rotation hypothesis. They found that it is unlikely to be the correct mechanism, and instead suggest a nonrotating model where ATPases compress and extend alternately, drawing in the DNA.
Stanford engineer James Swartz has made significant advances in cell-free protein synthesis, including the production of nanoscale viral spheres that can act as delivery trucks for new vaccines. These engineered capsids have the potential to provide safer and more effective vaccinations by targeting specific immune-system cells.
The study revealed the outer lipid envelope interacts with the capsid shell of hepatitis B virus, which is enormous and nearly 10 times larger than a hemoglobin molecule. The findings may offer new clues on how the virus replicates in vivo.
Researchers at Purdue University found that the flexible structure of WIN compounds allows them to shimmy into the proteins forming the virus' outer shell and alter them. This could potentially stop the infection process. The team believes WIN compounds may be effective in stabilizing proteins, preventing the viral trap door from opening.
Researchers at Purdue University found that viruses T4 and HK97 share similar protein folds in their outer shells, suggesting a common ancestor. The findings, published in the Proceedings of the National Academy of Sciences, provide further evidence for the evolutionary conservation of viral capsid structures.
A powerful molecular motor enables the virus to pack its DNA under high pressure, compacting it nearly 6,000 times its normal volume. The motor generates an enormous force of 57-60 picoNewtons, enough to lift six aircraft carriers.