A new study co-authored by Fábio Fernandes (DBE, iBB, i4HB) with the group of Mariana G. Pinho at ITQB NOVA reports a FLIM-FRET method to visualize protein–protein interactions in living Staphylococcus aureus, published in Nature Communications. Fluorescence-lifetime imaging microscopy (FLIM) combined with Förster resonance energy transfer (FRET) offers a spatially resolved way to track the septal peptidoglycan-synthesizing complex in vivo. Applied to the glycosyltransferase FtsW, the assay confirmed interactions with PBP1 and DivIB, and showed that FtsW also self-interacts — meaning septal peptidoglycan synthesis likely proceeds via multimeric complexes that can produce more than one glycan strand at a time. Imipenem treatment weakened the FtsW–PBP1 interaction, which points to conformational coupling rather than activity alone. See more.