M. Banzhaf

The mycobacterial glycoside hydrolase LamH enables capsular arabinomannan release and stimulates growth

This study identifies LamH, a glycoside hydrolase that cleaves -1,6-mannoside linkages in LAM/LM, enabling their export to the capsule and promoting bacterial growth.

Genome-wide synthetic-lethality screen of Bam complex associated genes in Escherichia coli

The paper identifies synthetic-lethal interactions of Bam complex associated genes in E. coli, revealing dependencies on lipid composition and peptidoglycan synthesis.

Structure-function analyses of dual-BON domain protein DolP identifies phospholipid binding as a new mechanism for protein localisation

This study identifies phospholipid binding as a mechanism for DolP localization, revealing its structure and function in Gram-negative bacteria.

Structure-function characterization of the conserved regulatory mechanism of the Escherichia coli M48 metalloprotease BepA

The paper presents the crystal structure of E. coli BepA, an M48 metalloprotease, and shows that its active site plug regulates function and is conserved across the family.

Midcell localization of PBP4 of Escherichia coli is modulating the timing of divisome assembly

This paper shows that PBP4 localizes at midcell during septal PG synthesis in E. coli and is important for the timing of divisome assembly.

Structure-function analysis of the Escherichia coli β-barrel assembly enhancing protease BepA suggests a role for a self-inhibitory state

This study presents the crystal structure of BepA, a protease involved in LptD folding, and shows its auto-regulation and role in maintaining outer membrane lipid asymmetry.

Biofilm inhibitor taurolithocholic acid alters colony morphology, specialized metabolism, and virulence of Pseudomonas aeruginosa

This study shows that taurolithocholic acid inhibits Pseudomonas aeruginosa biofilm formation and alters its specialized metabolism and virulence.

The outer membrane lipoprotein NlpI nucleates hydrolases within peptidoglycan multi-enzyme complexes in Escherichia coli

This study identifies NlpI as a scaffold for PG hydrolases in E. coli, forming multi-enzyme complexes that coordinate PG synthesis and hydrolase activity.