The identification and partial purification of the tailspike protein of the Salmonella newington bacteriophage, E34

The Salmonella newington bacteriophage, ε³⁴, must interact with the lipopolysaccharide (LPS) molecule of the host in order to start the infection process and was used in the investigations presented. An LPS-binding protein was identified and partially purified in these studies through standard biochemical techniques including salt precipitation and column chromatography. The protein identified was the tailspike protein of the ε³⁴ virus. was characterized by determining its stability in SDS and its ability to interfere with the in vitro assembly of a related virus. This study strongly suggests a close structural relationship between the ε³⁴ tailspike protein and the tailspike of a related phage and that the protein identified will be suitable for future investigations into LPS-protein interactions. The purpose of this work was to identify and purify the tailspike protein (TSP) of ε³⁴ so it could be utilized in comparative studies with the P22 TSP.