Smooth specific phage adsorption: endorhamnosidase activity of tail parts of P22.

  title={Smooth specific phage adsorption: endorhamnosidase activity of tail parts of P22.},
  author={Shintaro Iwashita and Shiro Kanegasaki},
  journal={Biochemical and biophysical research communications},
  volume={55 2},
Adsorption of phage P22 to Salmonella typhimurium.
Adsorption of phage P22 to its receptor in the lipopolysaccharide (LPS) of the envelope of Salmonella typhimurium is accompanied by a hydrolytic cleavage of the O poly Saccharide chain, which appears to be influenced by the cation concentration.
A model for the adsorption of phage P22 to Salmonella typhimurium.
  • V. Israel
  • Biology
    The Journal of general virology
  • 1978
A new model for the adsorption of bacteriophage P22 to its host Salmonella typhimurium is proposed, which explains why there is a difference in the specific endoglycosidase activity of the tail protein of mature virions as opposed to unattached tail protein.
Baseplate protein of bacteriophage T4 with both structural and lytic functions
It is speculated that the physiological role of normal gp5 functions in the initiation of infection by catalyzing local cell wall digestion to facilitate penetration of the tail tube through the cell envelope and may also be responsible for the well-known phenomenon of lysis from without observed with T4.
Role of the bacteriophage P22 tail in the early stages of infection
The initial binding of phage P22 to its host, Salmonella typhimurium, is dependent in a linear fashion on the number of tail parts per phage head, but there is also a later step which depends on tail parts.
Isolation of Enterobacteriaceae bacteriophage particles catalysing cell wall lipopolysaccharide degradation.
Using pairs of smooth and rough forms of Enterobacteriaceae, six smooth-specific bacteriophages were isolated from sewage and another was obtained from Dr Hedda Milch, Budapest, Hungary, and all phages were seen to exhibit Bradley group B or C morphology and to carry tail spikes.
Phage P22 tail protein: gene and amino acid sequence.
Comparison of the gene and protein sequences indicates that mature tail protein arises by cleavage of the initiator N-formyl-methionine from the nascent chain.
Structure and Functions of the Bacteriophage P22 Tail Protein
It is proposed that the glycosidic activity of the P22 tail protein is not essential for phage assembly or adsorption of the phage to its host but is required for subsequent steps in the process of infection.


Binding of Bacteriophage P22 Tail Parts to Cells
Purified base-plate parts of bacteriophage P22 can bind to the host cell, Salmonella typhimurium, and the site-destroying activity reacts with P22 heads to make active phage and with antiserum made against purified phage.
Structure of Cell Wall Lipopolysaccharide from Salmonella typhimurium IV. Anomeric Configuration of l-Rhamnose Residues and Its Taxonomic Implications
The results indicate that lipopolysaccharides of Salmonella groups A, B, and D 1 share an identical main chain polysaccharide and differ essentially only in the configuration of 3,6-dideoxyhexose branches; they thus suggest close evolutionary relationship between these three serogroups ofSalmonella.