Matthew Thomas Doyle

A diverse family of protein antibiotics inhibits the BAM complex by β-signal mimicry

This study identifies how diverse Llps inhibit the BAM complex by β-signal mimicry, revealing structural and functional mechanisms across Pseudomonas species.

Mechanism of phospholipid transport to the bacterial outer membrane by TAM.

This study identifies TAM as a bacterial phospholipid transport system, revealing its structure and mechanism for lipid delivery to the outer membrane.

First inhibitor of a bacterial two-partner secretion system.

This paper identifies a peptide inhibitor of FhaC, a TpsB protein involved in bacterial virulence, showing it inhibits exoprotein secretion and reduces virulence correlates.

A Protein Antibiotic Inhibits the BAM Complex to Kill Without Cell Entry

This study shows that L-type pyocins inhibit the BAM complex at the cell surface to kill Pseudomonas aeruginosa without entering the cell.

Near-atomic structure of the PorKN rings, disulfide bonded to PorG and bound to Attachment Complexes, provide mechanistic insights into the type IX secretion system

The paper presents a cryo-EM structure of the PorKN rings and shows their interaction with PorG and Attachment Complexes, proposing a mechanism for protein secretion in the Type IX Secretion System.

Extracellular loops of the β-barrel domain catalyze rapid folding for function of self-associating autotransporters

This study shows that extracellular loops of the β-barrel domain in Ag43 are essential for passenger domain folding and bacterial aggregation.

Sequestration of dead-end undecaprenyl phosphate-linked oligosaccharide intermediate

The paper shows that incomplete O-antigen repeat units are sequestered on Und-P, leading to cell death, and that membrane disruption allows their processing.