Extended Data Fig. 3: S protein localization, susceptibility to divers antibiotics and co-deletions.
From: Pneumococcal S protein coordinates cell wall modification and repair to resist host antimicrobials
(A) Deconvolved epifluorescence microscopy of live S. pneumoniae cells containing truncation fragments of S protein tagged with msfGFP (GFP). Numbers represent amino acids. Transmembrane (TM) domain is necessary for S protein septal localization. Scale bar = 2 μm. (B-H) Growth curve at 37°C. Data are represented as the mean of n ≥ 3 replicates and shading represents SEM. (B) Growth curve of pneumococcal cells deleted with either ΔlytA or ΔessSp, or both. (C) Growth curves of WT or ΔessSp cells to DNA targeting antibiotic ciprofloxacin (CIP). ΔessSp mutant has the same susceptibility to DNA targeting antibiotic compared to the WT. (D) Growth curves of WT or ΔessSp cells subject to diverse cell-wall targeting antibiotics; penicillin (PEN), piperacillin (PIP) or ceftriaxone (CTR). ΔessSp mutant is more susceptible to cell wall targeting antibiotics (PEN, PIP, CTR) than the WT. (E) Confirmation of CRISPRi-seq synthetic lethal screen. Growth curve of pneumococcal cells deleted with ΔessSp, and/or ΔdivIB (left), as well as ΔessSp, and/or mreD−/+ (right). (F) Growth curves of pneumococcal cells subject to cefotaxime (CTX) show that the ΔpgdA mutants is not more susceptible compared to the WT. (G) Growth curves of S. salivarius HSISS4 cells subject to penicillin (PEN) at 37°C show that the Δess mutants is more susceptible compared to the wild type. (H) Growth curve of pneumococcal cells deleted with either Δpbp2a or ΔessSp, or both.
