Abstract
Recent applications of phage therapy in localized wound and drug-resistant bacterial infection have brought bacteriophage back to the spotlight. While these works demonstrated the safety and effectiveness of engineered bacteriophages in human patients, the exact molecular machinery behind the bacteria killing remains largely uncharacterized. This is particularly noticable outside Escherichia coli phages, as most studies are based on bacteriophages of this Gram-negative model bacterium. In the attempt to extent our understanding to the bacteriophage of Gram-positive bacteria, we chose the host hijacking module of Bacillus subtilis phage SPO1 for systemic functional and structural studies. Gp49, an acidic protein located within operon 4 of this module, is believed to have a role during the host takeover event. Here we describe the complete resonance assignment of Gp49, which shares no sequence homology with any known protein, as the basis for the structure determination and further mechanism study.
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Acknowledgements
We thank Professor Steve Matthews of Imperial College London for useful discssions. We also thank Dr Zhijun Liu and Mr. Wei Zhan of Zhangjiang Laboratory, Chinese Academy of Sciences for recording spectra on 900 MHz spectrometer.
Funding
This research is supported by Young Talent project of Xi’an Jiaotong University for Professor Bing Liu and special equipment fund from Xi’an Jiaotong University 1st affiliated Hospital.
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Wang, Z., Liang, Y., Liu, H. et al. Resonance assignments of bacteriophage SPO1 Gp49 protein. Biomol NMR Assign 14, 111–114 (2020). https://doi.org/10.1007/s12104-020-09929-8
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DOI: https://doi.org/10.1007/s12104-020-09929-8