A putative GtrB-like glycosyltransferase modulates cation-dependent BCP8-2 phage infection and cell surface structure in Bacillus cereus.

In Bacillus cereus ATCC 14579, a BC_RS27090 (BC_5432) GtrB-like bactoprenol glycosyltransferase mutation in strain BC2012 is linked to significantly reduced BCP8-2 phage binding and infectivity, especially under cation-rich conditions.

• Why it matters: Molecular determinants of B. cereus susceptibility to phage BCP8-2 are poorly understood, limiting rational phage-based control of this persistent, antimicrobial-resistant pathogen.
• What they did: A mini-Tn 10 transposon mutant library of B. cereus ATCC 14579 was screened for altered phage susceptibility; BC2012 carried an insertion in BC_RS27090, and complementation restored phage sensitivity, with adsorption assays and adsorption kinetics plus one-step growth curves assessing early infection.
• The result: The gtrB mutation reduced initial adsorption and altered cell surface morphology, producing thinner, smoother cell walls, supporting that gtrB affects surface properties essential for cation-dependent phage adsorption and infection.