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. 2015 Mar 3;6(2):e02507-14. doi: 10.1128/mBio.02507-14

FIG 2 .

FIG 2 

Heterologous expression of GlmU and GlmM in PUL5 and siaC mutant bacteria restores growth and normal cell shape. (A) Peptidoglycan biosynthetic pathway showing C. canimorsus 5 orthologs of the E. coli enzymes. (B) Schematic representation of the E. coli GlmU bifunctional protein. The protein domains are boxed. The recombinant monofunctional proteins are indicated by the arrows. (C) Growth in coculture with HEK293 cells of PUL5 (ΔPUL5) mutant bacteria producing different combinations of GlmS, GlmM, GlmU, and monofunctional GlmU (MOI, 0.05; 23 h of growth). The averages from three independent experiments are shown. Error bars represent 1 standard deviation from the mean. *, P < 0.05. (D) Bright-field microscopy pictures of bacteria grown for 23 h with HEK293 cells (MOI, 0.05). (E) Growth on HEK293 cells of of wt (C. canimorsus 5) and siaC (ΔsiaC) bacteria expressing GlmM and monofunctional GlmU (MOI, 0.05; 23 h of growth). The averages from three independent experiments are shown. Error bars represent 1 standard deviation from the mean. **, P < 0.01. (F) Bright-field microscopy pictures of bacteria grown for 23 h on HEK293 cells (MOI, 0.05).