Initial interaction of the P22 phage with the Salmonella typhimurium surface.
OBJECTIVE
The goals of these studies were to characterize the interaction of the P22 phage particle with the Salmonella cell surface and to determine the phage elements involved in this interaction by mutational analysis.


BACKGROUND
The phage P22 has been characterized extensively. The gene and protein for the phage P22 tailspike, which is the phage adsorption organelle, have been intensively studied. The kinetics of the interaction of the tailspike protein with the cell surface has been studied in detail, surprisingly no mutational analysis has ever been reported that has defined these components and their interaction between themselves and the cell surface. The main and perhaps only component needed for this cell surface interaction is the tailspike protein.


METHODS
Adsorption to the cell surface has been measured in the wild type phage and in mutant derivatives, isolated in this study. Phage mutants have been isolated after hydroxylamine mutagenesis.


RESULTS
The adsorption of P22 to the cell surface is a temperature-independent event. Forty putative phage adsorption mutants have been isolated. A sample of them have been further analyzed. These divide the adsorption process into at least two stages. One stage contains mutants that absorb with essential wild type phage kinetics to the cell surface while the other stage with delayed adsorption kinetics.


CONCLUSIONS
The interaction of the phage P22 with the Salmonella cell surface has been shown to be a complicated one which is temperature-independent and multi-stage. Mutants isolated in this study may help dissect this process even further.
Venza Colon
Celia Johanna
CJ
Universidad Central del Caribe School of Medicine, Department of Microbiology, Bayamón, Puerto Rico.
Vasquez Leon
Andrea Y
AY
Villafañe
Robert J
RJ
D000327:Adsorption; D017100:Bacteriophage P22 / Q000378:metabolism* / Q000648:ultrastructure; D006801:Humans; D008070:Lipopolysaccharides / Q000378:metabolism; D012486:Salmonella typhimurium / Q000378:metabolism / Q000648:ultrastructure / Q000821:virology*; D013696:Temperature; D017376:Viral Tail Proteins / Q000378:metabolism
D008070:Lipopolysaccharides; D017376:Viral Tail Proteins