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Mukherjee, S.

Publications and source records attributed to Mukherjee, S..

At least 73 records · Page 4Linked to original sources

Regulatory Plasticity and Metabolic Trade-offs Drive Adaptive Evolution of Alternative Flagellar Configurations in Pseudomonas aeruginosa

Evolutionary constraints governing flagellar number in bacterial pathogens remain poorly understood. While related Pseudomonas species are hyperflagellated, P. aeruginosa maintains strict monoflagellation through the FleQ-FleN regulatory circuit. Here, we demonstrate that FleN dosage is essential for maintaining monoflagellation and bacterial fitness. Wild-type P. aeruginosa consistently displayed unipolar monoflagellation, while {Delta}fleN mutants developed over two-to-five flagella per cell in uni- or bipolar arrangements. Hyperflagellated {Delta}fleN cells exhibited severe fitness defects including reduced growth rates, attenuated virulence in nematode infection models, and competitive disadvantages in co-culture experiments. Remarkably, {Delta}fleN cells rapidly evolved suppressor mutations in fleQ that partially restored growth and motility without always restoring monoflagellation. Five independent suppressor alleles mapped to critical FleQ functional domains (four in the AAA+ ATPase domain, one in the DNA-binding domain), suggesting reduced protein activity that rebalances the disrupted regulatory circuit. Single-cell motility analysis revealed that suppressor strains exhibit heterogeneous swimming dynamics, with subpopulations achieving wild-type speeds despite carrying multiple flagella. Proteomic analysis demonstrated that hyperflagellation triggers extensive cellular reprogramming beyond flagellar components, affecting metabolic pathways, stress responses, and signaling networks. While hyperflagellated cells suffered complete loss of pathogenicity in animal infection models, environmental selection under viscous conditions could drive wild-type cells to evolve enhanced motility through specific fleN mutations. These findings suggest that bacterial flagellar regulatory circuits function as evolutionary capacitors, normally constraining phenotypic variation but enabling rapid adaptation to alternative motility configurations when environmental pressures exceed the performance limits of standard monotrichous flagellation. SIGNIFICANCE STATEMENTBacterial flagella are extracellular appendages that rotate to propel the cell and enable swimming motility. While some bacteria have multiple flagella, many pathogenic species like Pseudomonas aeruginosa have just one. Surprisingly, mutants of P. aeruginosa with multiple flagella performed worse, i.e., they grew more slowly, were less infectious in laboratory animals, and were outcompeted by wild-type bacteria. Even when some mutant bacteria evolved compensatory changes, they still struggled compared to single-flagellum bacteria. This reveals an important evolutionary trade-off: while multiple flagella might seem advantageous for movement, having just one flagellum allows bacteria to grow faster and cause more severe infections. This plasticity likely explains why P. aeruginosa is so successful both in the environment and as a human pathogen.

microbiology↗

Canonical and phosphoribosyl ubiquitination coordinate to stabilize a proteinaceous structure surrounding the Legionella-containing vacuole

Legionella pneumophila (L.p.), an intracellular bacterial pathogen, hijacks the ubiquitin signaling network of its eukaryotic host cells to establish infection. Two families of L.p. secreted ubiquitin ligases are instrumental in the maturation of the Legionella-containing vacuole (LCV): the SidC/SdcA family, which catalyzes canonical ubiquitination, and the SidE family, which bypasses the E1-E2-E3 enzymatic cascade and directly conjugates ubiquitin to a target through a phosphoribosyl (PR) linkage. Here, we demonstrate that the coordinated activities of these two effector families generate a hyperstable, ubiquitin-rich structure surrounding the LCV. We propose a model in which an initial wave of SidC/SdcA-mediated canonical ubiquitination around the LCV is further modified by SidE family-driven PR-ubiquitination, resulting in a detergent-resistant "cloud". The "cloud" is transient, breaking down as infection progresses, suggesting that L.p. reshapes the properties of the proteinaceous shell surrounding the vacuole to meet changing needs throughout its intracellular lifecycle. This unusual structure likely stabilizes and protects the LCV, shielding it from host defense mechanisms during early infection. Our findings reveal cellular consequences of effector interplay during infection and provide a foundation for future studies into the structure and function of the proteinaceous "cloud" surrounding the LCV.

cell biology↗

Interventionally-guided representation learning for robust and interpretable AI models in cancer medicine

Machine learning models hold promise in cancer medicine but often lack robustness and interpretability. We introduce a new class of model for high-dimensional molecular data that incorporate interventional auxiliary information to learn latent representations that are informative and interpretable by design. By using causal signals from genetic loss-of-function screens, our approach generates representations that generalize well across data distributions and biological contexts. In cancer cell line datasets, we show that causal guidance enables "zero-shot" transfer to cancer types unseen during training. Moreover, models trained solely on cell line data translate effectively to clinical cohorts, demonstrating strong "bench-to-bedside" generalization without fine-tuning. This strategy highlights a scalable way to leverage tractable laboratory assays for clinical modeling. More broadly, our results establish how integrating causal biological information within generative frame-works enhances data efficiency, interpretability, and robustness, opening avenues for a new generation of scientifically informed AI models in molecular medicine.

bioinformatics↗

SND3 is the membrane insertase within a fungal multipass translocon

During the biogenesis of most eukaryotic integral membrane proteins (IMPs), transmembrane domains are inserted into the endoplasmic reticulum membrane by a dedicated insertase or the SEC61 translocon. The SRP-independent (SND) pathway is the least understood route into the membrane, despite catering for a broad range of IMP types. Here, we show that Chaetomium thermophilum SND3 is a membrane insertase of novel fold. We further present a cryo-electron microscopy structure of a ribosome-associated SND3 translocon complex involved in co-translational IMP insertion. The structure reveals that the SND3 translocon additionally comprises the complete SEC61 translocon, CCDC47 and TRAP[a]. Here, the SEC61{beta} N-terminus works together with CCDC47 to prevent substrate access to the translocon. Instead, molecular dynamics simulations show that SND3 disrupts the lipid bilayer to promote IMP insertion via its membrane-embedded hydrophilic groove. Structural and sequence comparisons indicate that the SND3 translocon is a distinct multipass translocon for the insertion of multipass IMPs in fungi, euglenozoan parasites and other eukaryotic taxa.

biophysics↗

Beyond Static Screens: A High-Throughput Pooled Imaging CRISPR Platform for Dynamic Phenotype Discovery

Genetic screens are powerful tools for linking gene perturbations to cellular phenotypes, yet most pooled imaging approaches rely on static endpoint measurements. Here, we extend optical pooled screening to dynamic signaling phenotypes by combining time-lapse Forster resonance energy transfer-fluorescence lifetime imaging microscopy (FRET-FLIM) with optical enrichment and downstream genotyping. To enable high-throughput live-cell screening of dynamic phenotypes, we optimized and benchmarked all major steps in the pipeline. We developed FAST-HIPPOS, a Fiji-based automated analysis pipeline that rapidly segments hundreds of thousands of cells, extracts single-cell lifetime time traces, and identifies phenotypic hits in minutes for targeted photoactivation. We further established a robust phototagging strategy using the photoactivatable dye PA-JaneliaFluor646, providing bright, cloning-free labeling across diverse cell types. Benchmarking further demonstrated high sorting fidelity with low false-positive rates and efficient recovery of guide RNAs from as few as 200 sorted cells with minimal PCR bias. Applying this platform to cAMP signaling in HeLa cells using a custom CRISPR library recovered the expected primary regulators of {beta}-adrenergic signaling--ADRB2, GNAS, and ADCY6--with no gene-level false positives. Together, these optimizations establish a robust general framework for screening dynamic phenotypes that is easily adaptable to other live-cell readouts beyond FRET-FLIM and cAMP.

cell biology↗

Functional insights into a peculiar tetra-modular LPMO from the human pathogen Enterobacter cloacae

Enterobacter cloacae is a Gram-negative nosocomial human pathogen that inhabits diverse ecological niches. Its genome encodes a conserved set of putative chitin-active enzymes, including a peculiar lytic polysaccharide monooxygenase (LPMO), termed EcLPMO, which we functionally characterized in this study. EcLPMO is a tetra-modular protein consisting of an auxiliary activity family 10 (AA10) catalytic domain, two central domains of unknown function (DUF-A and DUF-B), and a C-terminal carbohydrate-binding module (CBM73). Functional assays using full-length EcLPMO and its truncated variants demonstrated that the AA10 domain oxidatively cleaves chitin at the C1 position. The CBM73 module enhances chitin binding and promotes synergy with endogenous chitinases. Notably, EcLPMO displayed a particularly strong synergistic effect with the unimodular chitinase EcChiA, leading to up to 14-fold and 60-fold increases in GlcNAc release from - and {beta}-chitin, respectively. Deletion of both DUFs reduced EcLPMO activity. While DUF-A alone and the association of DUF-A and DUF-B showed limited chitin binding, DUF-B alone exhibited no binding, suggesting a distinct role. Unexpectedly, using state-of-the-art structural modelling (AlphaFold3), we observed that the DUF-B domain contains two highly conserved histidines that coordinate the AA10-bound copper, forming a previously unreported inter-domain tetra-histidine copper coordination center. These findings highlight the structural and functional complexity of EcLPMO and suggest that its accessory domains, particularly DUF-B, may contribute to enzyme stability and substrate interaction. We speculate that DUF-B may protect the LPMO active site from oxidative damage, a feature that could prove crucial in its ecological and pathogenic contexts.

biochemistry↗

12-Hydroxystearic acid induces epidermal keratinocytes to secrete antimicrobial peptides that are potent inhibitors of viral infection.

Epidermal keratinocytes produce antimicrobial peptides (AMPs) that serve as a crucial component of the skins innate immune barrier. These peptides effectively target a broad spectrum of pathogenic microorganisms while preserving commensal microbiota essential for skin barrier homeostasis and overall skin health. Regulating the release of these AMPs presents a promising approach to enhancing the skin barriers defense mechanisms with minimal side effects. We have identified 12-hydroxystearic acid (12-HSA) as a potent stimulator of AMP secretion from primary epidermal keratinocytes. Mechanistic investigations revealed that, akin to bacterial stimulation, 12-HSA induces AMP release through the downregulation of caspase-8, which subsequently activates the inflammasome. Notably, we discovered that 12-HSA mediates caspase-8 downregulation via the acute activation of DNA methyltransferase 3A (DNMT3A), leading to transcriptional silencing of the caspase-8 locus. Importantly, 12-HSA is widely utilized in the cosmetic industry for its several skin beneficial properties including hydration and emolliency. Our findings suggest that this compound can be leveraged to enhance innate immune defenses in the skin, effectively mobilizing stored AMPs from keratinocytes to counteract microbial threats. This discovery highlights the potential for 12-HSA as a novel agent in dermatological applications aimed at fortifying skin barrier immunity.

cell biology↗

Pan-cancer prediction of tumor immune activation and response to immune checkpoint blockade from tumor transcriptomics and histopathology

Accurately predicting which patients will respond to immune checkpoint blockade (ICB) remains a major challenge. Here, we present TIME_ACT, an unsupervised 66-gene transcriptomic signature of tumor immune activation derived from TCGA (The Cancer Genome Atlas) melanoma data. First, we demonstrate that TIME_ACT scores accurately identify tumors with activated immune microenvironments across different cancer types. Further, analysis of spatial features reveals that tumor microenvironment regions with dense lymphocyte infiltration near tumor cells have high TIME_ACT scores, successfully marking localized immune activation. Second, across 25 transcriptomic ICB cohorts encompassing nine cancer types, TIME_ACT achieves a mean AUC of 0.76 and a mean odds ratio of 5.77, significantly outperforming 30 established transcriptomic signatures and prediction methods for ICB response, including a recently developed foundation model for immunotherapy response prediction. Third, we show that TIME_ACT scores can be accurately inferred from routine tumor histopathology slides and that slide-inferred TIME_ACT scores predict ICB response across nine new independent patient cohorts spanning eight cancer types, achieving a mean AUC of 0.72 and a mean odds ratio of 4.99. These findings establish TIME_ACT as a robust, pan-cancer biomarker that enables accurate, low-cost, and clinically scalable prediction of ICB response from routine histopathology.

cancer biology↗

Sensitizing Immune-Refractory Ovarian Tumors via p53 Mutation-Tailored Immunotherapy

High-grade serous ovarian cancer demonstrates limited responsiveness to immune checkpoint inhibitors, owing in part to immunosuppressive environments shaped by nearly universal p53 aberrations. Utilizing an immunocompetent mouse model and individual p53 mutations, we identified a dependence of the p53-R270H mutation (equivalent of human R273H) on regulatory T cells (Tregs) and the PD-1/PD-L1 axis. Analysis of patient datasets associated R273H with elevated levels of two p53 targets, PD-L1 and amphiregulin (AREG), a Tregs growth factor. In contrast to p53-R172H tumors, where there was limited activity, dual antibody therapy targeting AREG and PD-L1 selectively and effectively inhibited R270H tumors. This involved polarization toward M1 macrophages, infiltration of CD8+ T cells, diminished Ly6G+ neutrophils and downregulation of interleukin-4. In patient-derived R273C organoids, the combination treatment reduced the CD4/CD8 ratio. This study is the first to establish a mutation-tailored therapeutic approach that leverages the capacity of p53 to modulate immunosuppressive mechanisms.

cancer biology↗

CFIm25-Dependent Alternative Polyadenylation in AKT2 mRNA Programs Macrophage Polarization

Macrophage polarization is essential for immune responses, tissue homeostasis, and progression of many diseases. It is a tightly regulated process involving an intricate network of signaling pathways and control mechanisms at the level of transcription, alternative mRNA splicing, translation and mRNA stability. However, regulation through alternative mRNA polyadenylation (APA), remains poorly understood. This study explores the function of CFIm25, a key APA regulator, in macrophage polarization. Our findings show that CFIm25 overexpression drives M1 polarization, as evident from increased nitric oxide synthase activity, CD80 expression, and pro-inflammatory cytokine secretion, but dampens the M2 phenotype. Conversely, CFIm25 knockdown suppresses M1 traits and promotes M2 characteristics. Functionally, CFIm25 enhances phagocytosis, migration, and cancer cell inhibition. Mechanistically, CFIm25 favors proximal polyadenylation site usage of AKT2 mRNA, increasing Akt2 protein levels to support M1 polarization. Blocking this site with an antisense oligonucleotide reduces Akt2 expression and M1 traits. These findings establish CFIm25 as a crucial regulator of macrophage identity, offering insights into RNA-based immune regulation and potential therapeutic targets. In briefCFIm25 drives macrophage polarization toward the M1 phenotype through specific regulatory pathways. The presence of CFIm25 profoundly shifts surface marker expression, enhancing M1 markers while suppressing M2 signatures. This extends to biochemical properties, where CFIm25 boosts nitric oxide and pro-inflammatory cytokine production while reducing anti-inflammatory mediators. Functionally, CFIm25 enhances phagocytosis, inflammatory migration, and cancer cell killing. Mechanistically, this orchestration of the M1 polarization program involves CFIm25s regulation of AKT2 mRNA alternative polyadenylation which increases Akt2 protein expression and amplifies NF-{kappa}B pathway activation, a central driver of M1 polarization. HighlightsO_LICFIm25 overexpression enhances M1 surface markers and biochemical properties including nitric oxide production and pro-inflammatory cytokine secretion. C_LIO_LICFIm25 promotes M1 functional activities including phagocytosis, migration, and cancer-cytotoxic effects. C_LIO_LIBlocking the AKT2 proximal polyadenylation site usage causes a decrease in Akt2 protein, suppressing M1 polarization phenotypes including NOS activity and cytokine profiles. C_LIO_LIThe CFIm25-Akt2-NF-{kappa}B axis represents a novel target for macrophage polarization reprogramming. C_LI O_FIG O_LINKSMALLFIG WIDTH=196 HEIGHT=200 SRC="FIGDIR/small/660629v1_ufig1.gif" ALT="Figure 1"> View larger version (36K): org.highwire.dtl.DTLVardef@15e28f6org.highwire.dtl.DTLVardef@d35314org.highwire.dtl.DTLVardef@1f382feorg.highwire.dtl.DTLVardef@1d083d_HPS_FORMAT_FIGEXP M_FIG C_FIG

immunology↗

Alternative Polyadenylation Releases PCBP1-Mediated Suppression of CFIm25 During Macrophage Differentiation

CFIm25, a key component of the CFIm complex needed for mRNA 3 end processing, shows increased protein expression during monocyte-to-macrophage differentiation despite stable mRNA levels. We demonstrate that PCBP1 suppresses CFIm25 translation in monocytes by binding to its long 3UTR. During differentiation, alternative polyadenylation generates a shorter CFIm25 3UTR lacking PCBP1 binding sites. RNA immunoprecipitation confirms PCBP1 binding to the long 3UTR, while ribosome association analysis shows enhanced translation without this interaction. PCBP1 knockdown increases CFIm25 protein specifically in undifferentiated cells and induces macrophage differentiation markers without stimulation. These findings reveal how alternative polyadenylation controls CFIm25 expression during immune cell differentiation by modulating RNA-binding protein interactions and provide insight into post-transcriptional regulation of RNA processing factors.

molecular biology↗

The Luminal Ring Protein C2CD3 Acts as a Radial In-to-Out Organizer of the Distal Centriole and Appendages

Centrioles are polarized microtubule-based structures with appendages at their distal end that are essential for cilia formation and function. The protein C2CD3 is critical for distal appendage assembly, with mutations linked to orofaciodigital syndrome and other ciliopathies. However, its precise molecular role in appendage recruitment remains unclear. Using Ultrastructure Expansion Microscopy (U-ExM), iterative U-ExM, and in situ cryo-electron tomography (cryo-ET), we reveal that C2CD3 adopts a radially symmetric 9-fold organization within the centrioles distal lumen. We show that the C-terminal region of C2CD3 localizes close to a [~]100 nm luminal ring structure consisting of [~]27 nodes, while its N-terminal region localizes close to a hook-like structure that attaches to the A-microtubule as it extends from the centriole interior to exterior. This hook structure is adjacent to the DISCO complex (MNR/CEP90/OFD1), which marks future appendage sites. C2CD3 depletion disrupts not only the recruitment of the DISCO complex via direct interaction with MNR but also destabilizes the luminal ring network composed of C2CD3/SFI1/centrin-2/CEP135/NA14, as well as the distal microtubule tip protein CEP162. This reveals an intricate "in-to-out" molecular hub connecting the centriolar lumen, distal microtubule cap, and appendages. Although C2CD3 loss results in shorter centrioles and appendage defects, key structural elements remain intact, permitting continued centriole duplication. We propose that C2CD3 forms the luminal ring structure and extends radially to the space between triplet microtubules, functioning as an architectural hub that scaffolds the distal end of the centriole, orchestrating its assembly and directing appendage formation.

cell biology↗

Post-translational modifications distinguish amyloid-β isoform patterns extracted from vascular deposits and parenchymal plaques

Deposition of amyloid-{beta} (A{beta}) aggregates is a core pathological hallmark of both cerebral amyloid angiopathy (CAA) and extracellular parenchymal plaques in Alzheimers disease (AD). While both disease processes share progressive, decades-long deposition of fibrillar A{beta} peptide, they differ in isoform composition. We hypothesized that post-translational modifications (PTMs) on A{beta} would also differ between CAA and parenchymal plaques. Using Lys-N enzymatic digestion followed by quantitative mass spectrometry, we profiled A{beta} isoforms and N-terminus PTMs (aspartic acid isomerization and pyroglutamate formation) across CAA severity and compared them to parenchymal plaque A{beta} in AD. Moderate to severe CAA primarily featured intact N-terminus (A{beta}1-x) ([~]95%) with minimal N-truncated species (A{beta}2-x, A{beta}3pGlu-x, A{beta}4-x), whereas parenchymal plaques displayed diverse N-terminus truncations and PTMs. Increasing CAA severity correlated with a shift from longer, hydrophobic C-terminal isoforms (A{beta}41, A{beta}42, A{beta}43) to shorter, less hydrophobic C-terminal isoforms (A{beta}37, A{beta}38, A{beta}39, A{beta}40). Importantly, moderate and severe CAA displayed minimal isomerization of Asp-1 and Asp-7 residues, which correlated significantly (r > 0.9) with shorter C-terminal isoforms (A{beta}37, A{beta}38, A{beta}39, A{beta}40). These patterns suggest distinct A{beta} aggregation mechanisms in CAA versus parenchymal plaques. We propose that the intact N-terminus found in CAA with limited Asp isomerization is due to its inclusion within the protofibril structure (less disordered and inaccessible to PTMs), unlike the parenchymal plaques, where the N-terminus is more disordered and accessible to PTMs. These biochemical differences may reflect distinct protofibril architectures with potential implications for biomarker development for early CAA detection and therapeutic targeting of vascular and parenchymal A{beta}.

neuroscience↗

Swarm-seq Reveals Functional Divergence in CsrA Homologs Across Bacteria.

Bacteria employ sophisticated post-transcriptional regulatory mechanisms to adapt to environmental changes. Carbon storage regulator A (CsrA), a highly conserved small RNA-binding protein, serves as a critical post-transcriptional regulator by recognizing GGA motifs in target transcripts and typically repressing translation. Despite extensive research, how this conserved regulator has evolved diverse species-specific regulatory networks remains unclear. Here, using Bacillus subtilis as an experimental chassis, we have developed Swarm-seq -- a high-throughput functional genomics platform capable of assessing CsrA homologs across the Bacterial domain for their ability to regulate flagella-dependent swarming motility. Systematically testing over five-hundred codon-optimized csrA homologs for flagellin (Hag) repression revealed striking functional divergence, i.e., broadly two classes of CsrAs. Class I, exemplified by CsrAHp from Helicobacter pylori and RsmN from Pseudomonas aeruginosa strongly inhibited swarming, while Class II, exemplified by CsrAEc from Escherichia coli and RsmA from P. aeruginosa failed despite high sequence conservation. This differential activity occurred despite all proteins targeting identical GGA motifs in the hag transcripts 5UTR, indicating evolutionary plasticity in RNA-binding specificity beyond motif recognition. We propose that this plasticity enables a conserved global regulator to develop species-specific regulons through subtle structural adaptations, facilitating diverse physiological responses across bacterial taxa. Our findings establish B. subtilis as a powerful platform for characterizing CsrA homologs from genetically intractable bacteria, providing insights into post-transcriptional regulatory network evolution.

microbiology↗

Isomerized Aβ in the brain can distinguish the status of amyloidosis in the Alzheimer's Disease spectrum

Extracellular amyloid plaques, the pathognomonic hallmark of Alzheimers Disease (AD), are also observed in cognitively unimpaired subjects in the preclinical stages. Progressive accumulation of fibrillar amyloid-{beta} (A{beta}) as plaques and perivascular deposits occur two decades prior to clinical onset, making A{beta} a long-lived peptide. To characterize the amyloid plaques biochemically, both the A{beta}-load as well the post-translational modifications (PTMs) could serve as markers for distinguishing the pre-clinical stage compared to later prodromal and clinical stages of AD. Recently, we described the presence of extensive isomerization of the A{beta} N-terminus in AD post-mortem brains that are significantly increased compared to the age-matched non-AD control brains with A{beta} aggregates in the frontal cortex. In this report, we used targeted mass spectrometry to conduct a quantitative analysis of the most common PTMs associated with A{beta}; pyroglutamation, citrullination, N-terminal truncation (A{beta}4-x), C-terminal truncation (A{beta}42 and A{beta}40), and isomerization of aspartic acid residues (Asp-1 and Asp-7) in postmortem human brain tissue from pathologically negative (no A{beta} plaques) controls, controls with A{beta} plaques, Parkinsons disease (PD) with and without A{beta} accumulation/plaques and symptomatic AD. The AD cases contained statistically significant amounts of Asp-1and Asp-7 isomerized A{beta}1-15 ([~] 90 %) compared to controls (preclinical AD) and PD brains with fibrillar A{beta} aggregates/deposits. We find that ratio of isomerized N-terminus A{beta} (A{beta}1-15) species in the brain detergent soluble pool differentiates older fibrillar A{beta} deposits in symptomatic AD brain compared to A{beta} deposits detected in preclinical AD and PD. Citrullinated A{beta}3pglu-15 was increased only in symptomatic AD, highlighting this A{beta} PTM is a unique feature of parenchymal plaques in advanced AD. Our results have implications for early therapeutic targeting of these modified species as well potential for better biofluid biomarker development for drug efficacy monitoring.

neuroscience↗

Influence of simplifications on FE modelling of mandible and TMJ implants

End-stage temporomandibular joint (TMJ) disorders often necessitate joint replacement to restore bilateral mastication. Patient-specific TMJ implants typically rely on detailed in silico modelling derived from subject-specific computed tomography (CT) scans of the mandible. However, generating highly detailed finite element (FE) models is computationally expensive. Although structural simplifications of the mandible are known to influence mechanical behaviour, their quantitative impact on TMJ implant evaluation has not been systematically investigated. This study examines the influence of three modelling simplifications on stress-strain predictions in intact and implanted mandibles: (i) a detailed segmented mandible with tissue-specific material properties (Model 1), (ii) a simplified mandible comprising cortical bone only (Model 2), and (iii) a further simplified mandible excluding dental crowns (Model 3). Both narrow and standard TMJ implants were analysed under osseointegrated and non-osseointegrated conditions, resulting in fifteen FE models. Physiological clenching activities were simulated. Compared with the detailed model, simplified models showed reductions of up to 50% in maximum principal strain in bone and up to 44% in von Mises stress in TMJ implants, while preserving spatial stress-strain trends. These findings indicate that simplified models may be suitable for preliminary implant design, whereas detailed FE modelling remains essential for final pre-clinical evaluation.

bioengineering↗

A light-induced microprotein triggers regulated intramembrane proteolysis to promote photo sensing in a pathogenic bacterium.

Light, a ubiquitous environmental stimulus, shapes behavior and physiology across all domains of life. While photoreceptors are widespread in bacterial genomes, their functional roles and signal transduction mechanisms in non-photosynthetic bacteria remain understudied. Light represses biofilms and virulence factors through a bacteriophytochrome photoreceptor BphP and response regulator AlgB in the human pathogen Pseudomonas aeruginosa. Here, we used transposon mutagenesis screening to identify a conserved hypothetical microprotein, DimA, as the master activator of the photo-sensing cascade. Transcriptomics, luciferase reporter assays and physiological assays revealed that deletion of dimA abolishes light-dependent suppression of virulence factors and biofilms. Mechanistically, we demonstrated that DimA activates the site-I protease AlgW, triggering regulated intramembrane proteolysis of the anti-sigma factor MucA, liberating sigma factor AlgU ({sigma}22), which promotes algB expression. We discovered a positive feedback loop where light-activated AlgB upregulates dimA expression, thereby amplifying the photosensory response. This work establishes DimA as a crucial activator of photo sensing and expands our understanding of bacterial adaptation to changing light environments.

microbiology↗

Interactions between the picornavirus 3C(D) main protease and RNA induce liquid-liquid phase separation

The picornavirus 3CD protein is a precursor to the 3C main protease and the 3D RNA-dependent RNA polymerase. In addition to its functions in proteolytic processing of the virus polyprotein and cleavage of key host factors, the 3C domain interacts with cis-acting replication elements (CREs) within the viral genome to regulate replication and translation events. We investigated the molecular determinants of RNA binding to 3C using a wide range of biophysical and computational methods. These studies showed that 3C binds to a broad spectrum of RNA oligonucleotides, displaying minimal dependence on RNA sequence and structure. However, they also uncovered a novel aspect of these interactions, that is, 3C-RNA binding can induce liquid-liquid phase separation (LLPS), with 3CD-RNA interactions likewise leading to LLPS. This may be a general phenomenon for other 3C and 3C-like proteases, and polyprotein incorporating 3C domains. These findings have potential implications in understanding virally induced apoptosis and controlling stress granules, which involve LLPS and include other proteins with known interactions with 3C/3CD. O_FIG O_LINKSMALLFIG WIDTH=200 HEIGHT=72 SRC="FIGDIR/small/648818v1_ufig1.gif" ALT="Figure 1"> View larger version (28K): org.highwire.dtl.DTLVardef@16bbd2corg.highwire.dtl.DTLVardef@50a2cborg.highwire.dtl.DTLVardef@1efc3beorg.highwire.dtl.DTLVardef@1beff0_HPS_FORMAT_FIGEXP M_FIG C_FIG

biophysics↗