Publication details

Structure of protein from neck of bacteriophage infecting Staphylococcus aureus

Authors

BŘENKOVÁ Barbora ŠIBOROVÁ Marta BÁRDY Pavol PANTŮČEK Roman PLEVKA Pavel

Year of publication 2018
Type Appeared in Conference without Proceedings
MU Faculty or unit

Central European Institute of Technology

Citation
Description Bacteriophage phi812 is a lytic phage from the family Myoviridae. Phi812 infects most staphylococcal strains including those resistant to antibiotics. The structure of this bacteriophage was previously determined by cryo electron microscopy but functions of individual proteins remain unclear. Here we present our work towards resolving the structure of protein gp99 that forms the neck region of phi812. The protein may play a role in a regulation of the genome release from the virion during infection. Gp99 was cloned and expressed in E. coli and purified by affinity and size exclusion chromatography. A suitable crystallization condition was found and X-ray diffraction data with a resolution of 2.3 A were collected. To solve the phase problem, a variety of methods had been tried, including molecular replacement, heavy atom soaking and co-crystallization, and seleno-methionine incorporation. The structure of gp99 will help explain the mechanism of bacterial infection by bacteriophage. As there is a rising number of antibiotic resistant bacterial strains causing severe illnesses, phage therapy has a high potential. For this purpose, detailed knowledge of bacteria-phage interactions is vital.

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