P. L. Howell

Autoaggregation in Streptococcus intermedius is driven by the Pel polysaccharide

This study identifies the Pel polysaccharide as a driver of autoaggregation in S. intermedius, linking it to biofilm formation and increased pathogenicity.

CD56-mediated activation of human natural killer cells is triggered by Aspergillus fumigatus galactosaminogalactan

This study identifies galactosaminogalactan as the fungal ligand for CD56 on human NK cells, triggering antifungal responses and immune cell activation.

The Metabolic Usage and Glycan Destinations of GlcNAz in E. coli

This paper investigates the metabolic incorporation of GlcNAz into glycans in E. coli, finding it primarily in peptidoglycan with lower levels in PNAG and none in LPS or ECA.

Pseudomonas aeruginosa AlgF is a protein-protein interaction mediator required for acetylation of the alginate exopolysaccharide

This study identifies AlgF as a protein-protein interaction mediator in Pseudomonas aeruginosa that facilitates the formation of an acetylation and export complex for alginate modification.

PNAG exopolysaccharide eradication gives neutrophils access to Staphylococcus aureus biofilm infections

This study shows that disrupting the PNAG biofilm matrix with PgaB allows neutrophils to access and clear S. aureus biofilms in vivo.

Distinct types of multicellular aggregates in Pseudomonas aeruginosa liquid cultures

This study identifies two distinct types of multicellular aggregates in Pseudomonas aeruginosa cultures, mediated by different factors in exponential vs stationary phase.

Bps polysaccharide of Bordetella pertussis resists antimicrobial peptides by functioning as a dual surface shield and decoy and converts Escherichia coli into a respiratory pathogen.

Truncation of poly-N-acetylglucosamine (PNAG) polymerization with N-acetylglucosamine analogues

The paper identifies UDP-GlcNAc analogues that inhibit PNAG polymerization and biofilm formation in E. coli by terminating PNAG chains.

PelX is a UDP-N-acetylglucosamine C4-epimerase involved in Pel polysaccharide-dependent biofilm formation

The paper identifies PelX as a UDP-GlcNAc C4-epimerase essential for Pel polysaccharide synthesis and biofilm formation in Pseudomonas protegens.

Pseudomonas aeruginosa uses c-di-GMP phosphodiesterases RmcA and MorA to regulate biofilm maintenance

This study identifies RmcA and MorA as c-di-GMP phosphodiesterases essential for Pseudomonas aeruginosa to maintain mature biofilms under nutrient limitation.

CryoEM map of Pseudomonas aeruginosa PilQ enables structural characterization of TsaP

The paper determines the structure of PilQ from Pseudomonas aeruginosa and identifies TsaP as the spoke-forming component, revealing its role in surface-sensing signal transduction.

Discovery and characterization of a Gram-positive Pel polysaccharide biosynthetic gene cluster

The paper identifies and characterizes a Pel polysaccharide biosynthetic gene cluster in Gram-positive bacteria, showing its role in biofilm formation and regulation by c-di-GMP.

Multiple conformations facilitate PilT function in the type IV pilus

The paper determines four X-ray structures of PilT in different conformations and validates their physiological importance through co-evolution analysis and functional studies.

cAMP-Independent Control Of Twitching Motility In Pseudomonas aeruginosa

This study shows FimV regulates twitching motility in Pseudomonas aeruginosa independently of cAMP, through polar localization of regulatory proteins and structural components.

Microbial glycoside hydrolases as antibiofilm agents with cross-kingdom activity

This study identifies microbial glycoside hydrolases that disrupt biofilms and enhance antifungal efficacy against Aspergillus fumigatus and Pseudomonas aeruginosa.

The type IVa pilus machinery is pre-installed during cell division

This study shows that the T4aP machinery is pre-installed at future cell division sites in P. aeruginosa without requiring dedicated peptidoglycan hydrolases.

The molecular mechanism of the type IVa pilus motors

This study determines the structure of PilB ATPase domains bound to nucleotides, revealing rotational mechanisms for pilus assembly and disassembly.