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

Author

Mathew Scott Greenberg

Date of Award

5-1995

Degree Type

Thesis

Degree Name

Master of Science

Major

Microbiology

Major Professor

Robert Villafane

Committee Members

Peterson, Savage

Abstract

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.

Recommended Citation

Greenberg, Mathew Scott, "The identification and partial purification of the tailspike protein of the Salmonella newington bacteriophage, E34. " Master's Thesis, University of Tennessee, 1995.
https://trace.tennessee.edu/utk_gradthes/11122