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The viral envelope is made up of a lipid bilayer embedded with viral proteins, including viral glycoproteins. [1] These viral glycoproteins bind to specific receptors and coreceptors on the membrane of host cells, and they allow viruses to attach onto their target host cells. [1] Some of these glycoproteins include:
In virology, a spike protein or peplomer protein is a protein that forms a large structure known as a spike or peplomer projecting from the surface of an enveloped virus. [2] [3]: 29–33 The proteins are usually glycoproteins that form dimers or trimers. [3]: 29–33 [4]
By understanding glycoproteins and their synthesis, they can be made to treat cancer, Crohn's Disease, high cholesterol, and more. [ 3 ] The process of glycosylation (binding a carbohydrate to a protein) is a post-translational modification , meaning it happens after the production of the protein. [ 3 ]
Gray block: lipid membrane of the virus. The spike protein is very large, often 1200 to 1400 amino acid residues long; [8] it is 1273 residues in SARS-CoV-2. [5] It is a single-pass transmembrane protein with a short C-terminal tail on the interior of the virus, a transmembrane helix, and a large N-terminal ectodomain exposed on the virus ...
Since CD4 receptor binding is the most obvious step in HIV infection, gp120 was among the first targets of HIV vaccine research. Efforts to develop HIV vaccines targeting gp120, however, have been hampered by the chemical and structural properties of gp120, which make it difficult for antibodies to bind to it. gp120 can also easily be shed from the surface of the virus and captured by T cells ...
These glycoproteins mediate the interaction between virion and host cell, typically initiating the fusion between the viral envelope and the host's cellular membrane. [9] In some cases, the virus with an envelope will form an endosome within the host cell. [10]
Viral neuraminidase is a type of neuraminidase found on the surface of influenza viruses that enables the virus to be released from the host cell. Neuraminidases are enzymes that cleave sialic acid (also called neuraminic acid ) groups from glycoproteins .
In addition, glycosylation is often used by viruses to shield the underlying viral protein from immune recognition. A significant example is the dense glycan shield of the envelope spike of the human immunodeficiency virus. [8] Overall, glycosylation needs to be understood by the likely evolutionary selection pressures that have shaped it.