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RSV Fusion (F) Protein
Fusion glycoprotein F0 of the human respiratory syncytial virus (RSV) is a critical fusion glycoprotein that facilitates entry of the virus into host cells by mediating the fusion of the viral and cellular membranes. This class I fusion protein is synthesized as an inactive precursor (F0), which undergoes cleavage to form two disulfide linked subunits, F1 and F2, that are essential for its fusion activity. The RSV F protein exists in two conformations: a metastable prefusion form and a stable postfusion form, with the prefusion form being a major target for neutralizing antibodies due to its role in viral entry. The structural transitions of the F protein during the fusion process are crucial for its function, making it a significant focus in the development of vaccines and antiviral therapies against RSV infections. See also * Nirsevimab Nirsevimab, sold under the brand name Beyfortus, is a human recombinant monoclonal antibody with activity against respiratory syncytial vir ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Respiratory Syncytial Virus
Respiratory syncytial virus (RSV), also called human respiratory syncytial virus (hRSV) and human orthopneumovirus, is a virus that causes infections of the respiratory tract. It is a negative-sense, single-stranded RNA virus. Its name is derived from the large cells known as ''syncytia'' that form when infected cells fuse. RSV is a common cause of respiratory hospitalization in infants, and reinfection remains common in later life, though often with less severity. It is a notable pathogen in all age groups. Infection rates are typically higher during the cold winter months, causing bronchiolitis in infants, common colds in adults, and more serious respiratory illnesses, such as pneumonia, in the elderly and Immunodeficiency, immunocompromised. RSV can cause outbreaks both in the community and in hospital settings. Following initial infection via the eyes or nose, the virus infects the Epithelium, epithelial cells of the upper and lower airway, causing inflammation, cell damage, ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Viral Protein
The term viral protein refers to both the products of the genome of a virus and any host proteins incorporated into the viral particle. Viral proteins are grouped according to their functions, and groups of viral proteins include structural proteins, nonstructural proteins, regulatory proteins, and accessory proteins. Viruses are non-living and do not have the means to reproduce on their own, instead depending on their host cell's machinery to do this. Thus, viruses do not code for most of the proteins required for their replication and the translation of their mRNA into viral proteins, but use proteins encoded by the host cell for this purpose. Viral structural proteins Most viral structural proteins are components for the capsid and the envelope of the virus. Capsid The genetic material of a virus is stored within a viral protein structure called the capsid. The capsid is a "shield" that protects the viral nucleic acids from getting degraded by host enzymes or other types ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Glycoprotein
Glycoproteins are proteins which contain oligosaccharide (sugar) chains covalently attached to amino acid side-chains. The carbohydrate is attached to the protein in a cotranslational or posttranslational modification. This process is known as glycosylation. Secreted extracellular proteins are often glycosylated. In proteins that have segments extending extracellularly, the extracellular segments are also often glycosylated. Glycoproteins are also often important integral membrane proteins, where they play a role in cell–cell interactions. It is important to distinguish endoplasmic reticulum-based glycosylation of the secretory system from reversible cytosolic-nuclear glycosylation. Glycoproteins of the cytosol and nucleus can be modified through the reversible addition of a single GlcNAc residue that is considered reciprocal to phosphorylation and the functions of these are likely to be an additional regulatory mechanism that controls phosphorylation-based signalling. In ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Disulfide
In chemistry, a disulfide (or disulphide in British English) is a compound containing a functional group or the anion. The linkage is also called an SS-bond or sometimes a disulfide bridge and usually derived from two thiol groups. In inorganic chemistry, the anion appears in a few rare minerals, but the functional group has tremendous importance in biochemistry. Disulfide bridges formed between thiol groups in two cysteine residues are an important component of the tertiary and quaternary structure of proteins. Compounds of the form are usually called ''persulfides'' instead. Organic disulfides Structure Disulfides have a C–S–S–C dihedral angle approaching 90°. The S–S bond length is 2.03 Å in diphenyl disulfide, similar to that in elemental sulfur. Disulfides are usually symmetric but they can also be unsymmetric. Symmetrical disulfides are compounds of the formula . Most disulfides encountered in organosulfur chemistry are symmetrical disulfides. Unsymme ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Neutralizing Antibodies
A neutralizing antibody (NAb) is an antibody that defends a cell from a pathogen or infectious particle by neutralizing any effect it has biologically. Neutralization renders the particle no longer infectious or pathogenic. Neutralizing antibodies are part of the humoral response of the adaptive immune system against viruses, bacteria and microbial toxin. By binding specifically to surface structures (antigen) on an infectious particle, neutralizing antibodies prevent the particle from interacting with its host cells it might infect and destroy. Mechanism In order to enter cells, pathogens, such as circulating viral particles or extracellular bacteria, use molecules on their surfaces to interact with the cell surface receptors of their target cell which allows them to enter the cell and start their replication cycle. Neutralizing antibodies can inhibit infectivity by binding to the pathogen and blocking the molecules needed for cell entry. This can be due to the antibodies ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Nirsevimab
Nirsevimab, sold under the brand name Beyfortus, is a human recombinant monoclonal antibody with activity against respiratory syncytial virus (RSV). It is a respiratory syncytial virus (RSV) F protein‑directed fusion inhibitor that is designed to bind to the fusion protein on the surface of the RSV virus. The most common side effects are rash, fever and injection site reactions (such as redness, swelling and pain where the injection is given). It was developed by AstraZeneca and Sanofi. Nirsevimab was approved for medical use in both the European Union and the United Kingdom in November 2022, in Canada in April 2023, and in the United States in July 2023. Medical uses In the European Union, nirsevimab is indicated for the prevention of respiratory syncytial virus RSV lower respiratory tract disease in neonates and infants during their first RSV season. In the United States, nirsevimab is indicated for the prevention of RSV lower respiratory tract disease in neonates and i ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
Viral Structural Proteins
A viral structural protein is a viral protein that is a structural component of the mature virus. Examples include the SARS coronavirus 3a and 7a accessory proteins. Bacteriophage T4 structural proteins During assembly of the bacteriophage (phage) T4 virion, the structural proteins encoded by the phage genes interact with each other in a characteristic sequence. Maintaining an appropriate balance in the amounts of each of these structural proteins produced during viral infection appears to be critical for normal phage T4 morphogenesis. Phage T4 encoded proteins that determine virion structure include major structural components, minor structural components and non-structural proteins that catalyze specific steps in the morphogenesis sequence. Phage T4 morphogenesis is divided into three independent pathways: the head, the tail and the long tail fibres as detailed by Yap and Rossman.Yap ML, Rossmann MG. Structure and function of bacteriophage T4. Future Microbiol. 2014;9(12):131 ... [...More Info...] [...Related Items...] OR: [Wikipedia] [Google] [Baidu] |
