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A capsid is the protein shell of a virus, enclosing its genetic material. It consists of several oligomeric (repeating) structural subunits made of protein called protomers . The observable 3-dimensional morphological subunits, which may or may not correspond to individual proteins, are called capsomeres .
The encapsulin systems were first identified through the use of bioinformatics that linked capsid-like proteins to specific operons in bacterial and archaeal genomes. [4] When protein nanocompartments were discovered in 1994, and later renamed encapsulins, they were found in the supernatant fluid of the Brevibacterium linens culture. [3]
Both in-vivo assembly (i.e., assembly inside E. coli bacteria via recombinant co-expression of multiple proteins) and in-vitro assembly (i.e., protein self-assembly in a reaction vessel using stoichiometric quantities of previously purified proteins) have been successfully shown to form virus-like particles.
The bacterial capsule is a large structure common to many bacteria. [1] It is a polysaccharide layer that lies outside the cell envelope, and is thus deemed part of the outer envelope of a bacterial cell. It is a well-organized layer, not easily washed off, and it can be the cause of various diseases.
The capsid proteins are often differentiated into major and minor capsid proteins (MCP and mCP). In exceptional cases, there are also viruses without a capsid (i.e., true virions), such as the RNA viruses of the Narnaviridae and the viroids of the Pospiviroidae (with the Citrus Exocortis Viroid and the Citrus Bark Crack Viroid ).
The role of these proteins in rotavirus replication is not entirely understood; their functions are thought to be related to RNA synthesis and packaging in the virion, mRNA transport to the site of genome replication, and mRNA translation and regulation of gene expression.
The integration itself is a sequential exchange (see genetic recombination) via a Holliday junction and requires both the phage protein Int and the bacterial protein IHF (integration host factor). Both Int and IHF bind to attP and form an intasome, a DNA-protein-complex designed for site-specific recombination of the phage and host DNA. The ...
The BMC shell appears icosahedral [26] or quasi-icosahedral, and is formed by (pseudo)hexameric and pentameric protein subunits. [27] Structures of intact shells have been determined for three functionally distinct: BMC types, carboxysomes, [28] the GRM2 organelles involved in choline catabolism [29] and a metabolosome of unknown function.