Identification of the tailspike protein from the Salmonella newington phage epsilon 34 and partial characterization of its phage-associated properties.
The lipopolysaccharide (LPS) of the Salmonella cell surface serves as the receptor for a very large number of bacterial viruses. The tailspike protein from these viruses recognizes the LPS as its initial receptor. It is proposed that the study of the P22 and epsilon 34 tailspike proteins could serve as a model for the study of the interaction of proteins with LPS. Toward this end, the tailspike protein of the epsilon 34 phage has been identified. The data suggest similarities between the epsilon 34 tailspike protein and the P22 tailspike protein. Some properties related to the interaction of the phage tailspike with its receptor are reported.
Greenberg
M
M
Department of Microbiology, University of Tennessee, Knoxville 37996, USA.
Dunlap
J
J
Villafane
R
R
D000327:Adsorption; D017100:Bacteriophage P22 / Q000737:chemistry / Q000648:ultrastructure; D008070:Lipopolysaccharides / Q000378:metabolism; D011991:Receptors, Virus / Q000378:metabolism; D012475:Salmonella / Q000145:classification / Q000378:metabolism / Q000821:virology; D012483:Salmonella Phages / Q000737:chemistry* / Q000648:ultrastructure; D017376:Viral Tail Proteins / Q000737:chemistry* / Q000378:metabolism / Q000648:ultrastructure; D014771:Virion / Q000737:chemistry / Q000648:ultrastructure
D008070:Lipopolysaccharides; D011991:Receptors, Virus; D017376:Viral Tail Proteins