Experimental study demonstrates that expressing foreign murE disrupts cell morphology and alters peptidoglycan structure in Escherichia coli, suggesting partial cross-species wall integration.
In the biosynthesis of peptidoglycan (PG), murE protein (MurE) adds a diamino acid at position 3 of the peptide chain of peptidoglycan. The diamino acid that is added by MurE and makes cross-linkage with adjacent peptide chain differs depending on the bacterial species: Gram-negative bacteria add meso-diaminopimelic acid (DAP), while most Gram-positive bacteria add L-lysine (Lys). In this study, the murE gene of Levilactobacillus brevis that transfers Lys in PG synthesis was cloned into Escherichia coli that has DAP-type PG. The transformant cells harboring L. brevis murE showed reduction of colony forming units during cultivation, and were elongated or burst when murE was expressed. Amino acid analysis of solubilized PG revealed that the Lys/DAP ratio increased in the PG of the transformants. Interestingly, aspartic acid that is responsible for the formation of cross-linkages between Lys and other peptide chain in the PG of L. brevis also increased, suggesting that Lys-type PG with Asp cross-linkage was partially formed by the cloning of murE gene.
No takes yet. Share an insight, caveat, or question.
Onoue et al. (2025) studied this question.
Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context: