Jean‐Marc Ghigo

This study tracks lineage evolution in biofilms using DNA barcoding and spatial sampling, revealing phases of segregation, migration, and adaptation that influence antibiotic resistance.

The paper shows how oxygen gradients in the gut reshape cross-feeding between Bacteroides thetaiotaomicron and Escherichia coli through spatial organization and metabolic feedback.

CIPHR-FISH improves microbiome imaging by enabling strain-level taxonomic resolution through machine learning and probe design, revealing spatial community structures in zebrafish.

This paper develops conjugative plasmids that block antibiotic resistance plasmid spread by combining metabolic enhancement and plasmid spread mechanisms in microbial communities.

The paper analyzes trimeric autotransporters across bacteria to identify secretion adaptations, finding phylogenetic differences in periplasmic domains and ESPRs.

This study identifies CSAP-1, a MACPF domain protein from Chryseobacterium massiliae, as a broad-spectrum antimicrobial that inhibits Flavobacteriales species and contributes to zebrafish larval protection against Flavobacterium covae.

This study shows IL-26 from innate lymphoid cells regulates gut epithelial homeostasis by shaping microbiota composition in zebrafish larvae.

This study investigates the incomplete lytic cycle of hankyphage, a Bacteroides bacteriophage, revealing defective virion formation and incomplete DNA packaging.

This study investigates how phage-phage competition and biofilm formation affect the efficacy of a two-phage combination against Pseudomonas aeruginosa in vitro.

This study identifies adhesins in V. parvula and S. gordonii that mediate co-aggregation and shows its role in biofilm structure without affecting cell-cell communication.

This paper identifies a bile-induced RND efflux pump in Bacteroides thetaiotaomicron that facilitates magnesium efflux, reducing eDNA concentration and promoting biofilm formation.

This study investigates GPL trafficking in Veillonella parvula, revealing a minimal Mla system that directly connects membranes without chaperones or outer membrane lipoproteins, suggesting an ancestral core of the Mla system.