Pal, also known as peptidoglycan-associated lipoprotein, from Escherichia coli (E. coli) has been implicated in the clinical condition of sepsis. Pal’s clinical role in sepsis requires its release from E. coli, although the mechanism of its release is largely unknown. We propose that Pal’s release from E. coli is influenced by its tight non-covalent interaction with peptidoglycan. To test our hypothesis, we prepared recombinant site-directed mutants of Pal, which we predicted would have altered Pal-peptidoglycan binding affinities. These Pal mutants were analyzed using an ultracentrifugation protocol and standard protein detection methods. Our preliminary data suggest that a few key residues are responsible for the Pal-peptidoglycan interaction. Future work will determine how changes to these residues affect Pal’s release from E. coli.

Modulating the binding affinity of Pal to peptidoglycan

256th National Meeting (2018)

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