1H, 13C and 15N NMR assignments of Bacillus subtilis bacteriophage SPO1 protein Gp46.

Abstract

Bacterial antibiotic resistance is a serious threat to public health and bacteriophage therapy is an alternative for antibiotics in the era of multidrug resistance. While phage draws attention in fighting bacterial infection and is used in protein display to study macromolecular interactions, the molecular machinery of the host invasion mechanism remains largely unclear for many bacteriophages. Despite recent studies on T4 and T7 phages of Gram-negative model organism Escherichia coli revealing many interesting features of their invasive strategies, the studies on Gram-positive bacterial phages still lag far behind their counterparts. SPO1 is a lytic phage of model organism Bacillus subtilis and one of the best studied Gram-positive bacterial phages. SPO1 features a unique Host Takeover Module coding for 24 proteins which show little similarity to any previously known proteins. Gp46, located in this module, is an acidic protein that is produced by SPO1 presumably during the host takeover event. Here we describe the complete resonance assignment of Gp46 as the basis for the first structure determination of SPO1 phage protein and further mechanism study.