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Structural model at atomic resolution of bacteriophage T4 [1] The structure of a typical myovirus bacteriophage Anatomy and infection cycle of bacteriophage T4. A bacteriophage (/ b æ k ˈ t ɪər i oʊ f eɪ dʒ /), also known informally as a phage (/ ˈ f eɪ dʒ /), is a virus that infects and replicates within bacteria and archaea.
These receptors vary with the phage; teichoic acid, cell wall proteins and lipopolysaccharides, flagella, and pili all can serve as receptors for the phage to bind to. In order for the T-even phage to infect its host and begin its life cycle it must enter the first process of infection , adsorption of the phage to the bacterial cell.
Upon encountering a host cell, the tail section of the virion binds to receptors on the cell surface and delivers the DNA into the cell by use of an injectisome-like mechanism (an injectisome is a nanomachine that evolved for the delivery of proteins by type III secretion).
The virion is similar in structure to the T4 phage but simpler. [1] It has an icosahedral head [2] containing the genome attached at one vertex to the tail. The tail has a tube surrounded by a contractile sheath. It ends in a base plate with six tail fibres. The tail fibres are involved in attaching to the host and providing specificity. [3]
The bacterial cell wall differs from that of all other organisms by the presence of peptidoglycan (poly-N-acetylglucosamine and N-acetylmuramic acid), which is located immediately outside of the cytoplasmic membrane. Peptidoglycan is responsible for the rigidity of the bacterial cell wall and for the determination of cell shape. It is ...
The tailspike protein (P22TSP) of Enterobacteria phage P22 mediates the recognition and adhesion between the bacteriophage and the surface of Salmonella enterica cells. It is anchored within the viral coat and recognizes the O-antigen portion of the lipopolysaccharide (LPS) on the outer-membrane of Gram-negative bacteria .
Bacterial lysis and release of newly formed virions occurs when sufficient lysis protein has accumulated. Lysis (L) protein forms pores in the cytoplasmic membrane, which leads to loss of membrane potential and breakdown of the cell wall. [1] The lysis protein is known to bind to DnaJ via an important P330 residue. [8]
structure summary In molecular biology , a phage major coat protein is an alpha-helical protein that forms a viral envelope of filamentous bacteriophages . These bacteriophages are flexible rods, about one to two micrometres long and six nm in diameter, with a helical shell of protein subunits surrounding a DNA core.