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Biology subjects

Reynolds, E. C.

Publications and source records attributed to Reynolds, E. C..

4 recordsLinked to original sources

The Spatial Architecture of Human Subgingival Biofilms

Human microbiome studies have transformed understanding of disease-associated microbial communities, yet most approaches collapse polymicrobial biofilms into compositional profiles and lose the spatial relationships through which microorganisms interact in vivo. Periodontitis provides a clinically important model to investigate microbial spatial organisation because the disease is associated with deep, anaerobic periodontal pockets colonized by dense polymicrobial biofilms. Here, using multiplex fluorescence in situ hybridization with spectral and confocal microscopy of subgingival plaque across 174 sites from 36 individuals with periodontitis, we define taxon-resolved spatial architectures of the human subgingival plaque microbiome. We show that subgingival plaque is organized into recurrent multicellular assemblages of microbial consortia rather than unstructured layers of biomass, including assemblages defined as test-tube-brushes, corncobs and additional polymicrobial architectures with distinct taxonomic patterning. Test-tube brushes were enriched in severe periodontal niches, and their detection and burden increased with pocket depth, with distinct patterns observed in smoking-associated disease sites. In a longitudinal treatment subset, sites containing test-tube brushes before therapy lacked detectable test-tube brushes after treatment and instead showed corncobs concomitant with reduced pocket depth and resolution of disease. In addition to canonical oral biofilm structures, we identify previously undescribed polymicrobial assemblages whose occurrence is patterned by pocket depth and anatomical tooth site. These findings show that disease-associated human biofilms are organized into reproducible spatial states and suggest that microbial architecture provides an additional axis for interpreting microbiome-associated disease.

microbiology↗

Structural basis for curvature generation and functional specialization in spirochete flagella

Spirochetes are a distinctive phylum of spiral-shaped bacteria, defined by their curved periplasmic flagella, which drive motility by deforming the cell body and enabling efficient corkscrew-like propulsion through viscous environments. Despite their clinical importance, the molecular mechanisms underlying flagellar assembly, curvature and thus motility, remain poorly understood. Here we used cryo-electron microscopy combined with visual proteomic analysis to determine near-atomic resolution structures of two distinct flagellar filaments natively isolated from T. denticola, a major oral pathogen. Our structures reveal that filament curvature is generated by the asymmetric decoration of a conserved FlaB core by multiple sheath proteins, including FlaA1/2/3 and two previously uncharacterized proteins, termed FlaL1 and FlaL2. We show that the sheath imposes differential axial compaction on the FlaB core: FlaA1 expands the lattice at the outer curvature, FlaA2/3 compress the lattice at the inner curvature, and FlaL proteins stabilize these asymmetric interactions. Incorporation of distinct FlaB homologs contributes to assembled filament identity, with FlaB3 forming thin filaments and FlaB1/2 interacting with the sheath to form thick filaments. Comparative analysis reveals that FlaL proteins are conserved amongst some Treponema species and several other spirochetes, indicating that asymmetric assembly represents a modular solution to the mechanical demands of periplasmic flagella. These findings provide a structural framework for understanding functional specialization in bacterial filaments.

microbiology↗

Novel action of proline-rich antimicrobial peptides Api88, Api137, Onc72 and Onc112 against Pseudomonas aeruginosa and Escherichia coli in ion-rich environments.

The rise in antibiotic resistance has meant that there is a need for new strategies and one avenue is the use of proline-rich antimicrobial peptides (PrAMPs). Here we investigate how different metal ion environments (Na+, Mg2+, Ca2+) affect antimicrobial activity of PrAMPs derived from apidaecin 1b (Api88, Api137) and Oncopeltus antibacterial peptide 4 (Onc72, Onc112) against Pseudomonas aeruginosa and Escherichia coli. Initial antimicrobial testing in an ion-rich media (ion levels similar to mammalian body fluids) found that the PrAMPs were effective against E. coli but not P. aeruginosa. Both Api88 and Api137 were bactericidal, while Onc72 and Onc112 were bacteriostatic against E. coli. In a lower ion-media the activity of the PrAMPs significantly improved against both bacteria and Onc72 and Onc112 altered the mode of action to bactericidal. In low Na+, Ca2+ and Mg2+ ion conditions all of the peptides were able to penetrate the outer membrane of P. aeruginosa, however at higher ion concentrations none of the peptides were able to penetrate the outer membrane. PrAMPs were found to cause E. coli cells to swell and have a hyperpolarised membrane indicating a new mechanism of action for PrAMPs. Our data indicates that bacteria reduce susceptibility to AMPs by stabilising their LPS layer with metal ions and that the PrAMPs have secondary modes of action affecting the functionality of the bacterial membrane. Combining an ion chelator with PrAMPs may be a novel solution to combat weak antimicrobial activity in ion-rich environments such as host tissues.

microbiology↗

In situ structure and organisation of the type IX secretion system

The Bacteroidetes type IX secretion system (T9SS) consists of at least 19 components that translocate proteins with a type A or type B C-terminal domain (CTD) signal across the outer membrane. The overall organisation and architecture of this system including how the secretion pore (Sov) interacts with the other components is unknown. We used cryo-electron tomography to obtain the first images of the T9SS including PorK/N rings inside intact Porphyromonas gingivalis cells. Using proteomics, we identified a novel complex between Sov, PorV and PorA and showed that Sov interacts with the PorK/N rings via PorW and a new component PGN_1783. A separate complex comprising the outer membrane {beta}-barrel protein PorP, PorE, and the type B CTD protein PG1035 was also identified. Similarly, the Flavobacterium johnsoniae PorP-like protein, SprF was found bound to the major gliding motility adhesin, SprB. Based on these data, we propose cell surface anchorage for type B CTD proteins to PorP-like proteins and a unique model where the PorK/N rings function as an outer membrane barrier to maintain the close proximity of the translocon to the shuttle and attachment complexes inside the rings, ensuring the harmonized secretion and cell surface attachment of the T9SS substrates.

microbiology↗