New Publication! Salipro® Enables New Insights into Antibiotic Resistance

Bacteria developing resistance to antibiotics is a major global health challenge. Understanding the mechanisms they use, like modifying their protective membranes, is crucial. A key player in this process for pathogens like Pseudomonas aeruginosa is the membrane protein MprF. But how does it work?

In this new study with the Salipro® platform published in Science Advances, Dr. Maike Bublitz-Meier and her team shed light on the structure and function of the Pseudomonas aeruginosa membrane protein MprF, a key player in antimicrobial resistance.

Key Highligths:

• Salipro® enabled the first cryo-EM structure of MprF from P. aeruginosa (PaMprF).   

• The structure, combined with functional assays, revealed MprF acts as a versatile    lipid scramblase, transporting lipids without external energy.

• The findings provide a detailed blueprint for understanding a critical component of the bacterial defense system

This work suggests a novel mechanism for lipid transport involving membrane deformation and provides crucial insights into a potential target for combating antibiotic resistance.   

Congratulations to the authors: Maike Bublitz, Matthew T. K. Hankins, Matyas Parrag, Alisa A. Garaeva, Jennifer C. Earp, Markus A.Seeger, and Phillip J. Stansfeld on this fantastic research!

Dive deeper into this study: M. T. K. Hankins, et al., MprF from Pseudomonas aeruginosa is a promiscuous lipid scramblase with broad substrate specificity. Sci. Adv.11,eads9135(2025).