MP
Cryo-EM structure and polar assembly of the PS2 S-layer of Corynebacterium glutamicum.
Sogues A, Sleutel M, Petit J, Megrian D, Bayan N, Wehenkel AM, Remaut H.
Proc Natl Acad Sci U S A. 2025 Aug 5;122(31):e2426928122.
doi: 10.1073/pnas.2426928122. Epub 2025 Jul 29.
PMID: 40729392.
Cryo-EM => repeating architecture of the PS2 S‑layer + how its building blocks form a robust, semi‑permeable coat: mechanism for “polar assembly”.
Molecular basis of ligand binding and receptor activation at the human A3 adenosine receptor.
Zhang L, Mobbs JI, Bennetts FM, Venugopal H, Nguyen ATN, Christopoulos A, van der Es D, Heitman LH, May LT, Glukhova A, Thal DM.
Nat Commun. 2025 Aug 18;16(1):7674.
doi: 10.1038/s41467-025-62872-x.
PMID: 40825947.
Structure and pharmaco => how diverse ligands engage the A3 adenosine receptor and stabilize distinct conformational states.
Mapping of binding features and identification of networks that couple the binding pocket to activation ”microswitches”.
Mutagenesis and biophysics => key residue–ligand contacts and state preferences.
Molecular basis of human taurine transporter uptake and inhibition.
Du B, Cheng L, Xie J, Chen L, Yan K.
Nat Commun. 2025 Aug 11;16(1):7394.
doi: 10.1038/s41467-025-62857-w.
PMID: 40789850.
Cryo‑EM structures of human TauT => substrate‑bound and inhibitor‑bound states across the transport cycle.
Identification of residues for substrate specificity within the GABA‑subfamily. Several small‑molecule inhibitors lock TauT in inward‑open or occluded states.
TMEM65 functions as the mitochondrial Na+/Ca2+ exchanger.
Zhang JL, Chang YC, Lai PH, Yeh HI, Tsai CW, Huang YL, Liu TY, Lee IC, Foulon N, Xu Y, Rao B, Shih HM, Tu YC, Reyes AV, Xu SL, Feng L, Tsai MF.
Nat Cell Biol. 2025 Aug;27(8):1301-1310.
doi: 10.1038/s41556-025-01721-x. Epub 2025 Jul 21.
PMID: 40691517.
∆TMEM65 => loss of mitochondrial Na⁺/Ca²⁺ exchange activity.
Bioch => dimeric assembly with candidate ion‑coordinating residues.
Functional reconstitution of TMEM65 in liposomes.
TMEM65 deletion elevates matrix Ca²⁺ and sensitizes mitochondria to permeability transition, linking the exchanger to cell fate control.
Application of Protein Structure Encodings and Sequence Embeddings for Transporter Substrate Prediction.
Denger A, Helms V.
Molecules. 2025 Aug 1;30(15):3226.
doi: 10.3390/molecules30153226.
PMID: 40807401.
Deep‑learning + AlphaFold/Foldseek 3Di => classification of transporter substrates.
Water molecules in the cannabinoid receptor 2 binding site crucially impact the discovery of novel ligands.
Scharf MM, Scott-Dennis M, Borrega-Roman L, Giese FNZ, Plevako D, Sykes DA, Veprintsev DB, Kolb P.
Eur J Med Chem. 2025 Aug 10;299:117846.
doi: 10.1016/j.ejmech.2025.117846. Online ahead of print.
PMID: 40812071.
Large‑scale in‑silico screening against CB2 => conserved water sites in the hydrophobic pocket improves docking outcomes.
Using multiple receptor conformations and water placements boosts hit rates versus single‑setup screens.
The CueR-regulated transporters CopA and CusFABC coordinate copper detoxification in Vibrio parahaemolyticus.
Zheng C, Zhai Y, Wang M, Xu Z, Zhang Y, Zhou X, Chen X, Jiao X.
Virulence. 2025 Dec;16(1):2545557.
doi: 10.1080/21505594.2025.2545557. Epub 2025 Aug 11.
PMID: 40773510.
Transcriptomics and reporter assays => CueR upregulates copA and cusFABC upon copper stress.
Genetic and physiological tests => CopA and CusFABC maintain Cu/Fe homeostasis and protect from copper’s bactericidal effects.
The copA/cusFABC double mutant is impaired in zebrafish intestinal colonization : detoxification for host association.
CueR directly activates both systems, integrating copper sensing with detox transport.
Structures and zinc ion transport pathways of the human SLC39A family of metal transporters.
Xilan Wang, Christian Lorenz, Christer Hogstrand, and Wolfgang Maret.
bioRxiv posted 10 August 2025.
doi:10.1101/2025.08.09.669477.
Comparative analysis over the ZIP family structures/models to delineate putative Zn²⁺ entry routes and gating elements shared across subfamilies.
=> conserved residues lining translocation pathways; proposed as determinants for ion selectivity.
Packing of apolar amino acids is not a strong stabilizing force in transmembrane helix dimerization.
Gilbert J. Loiseau and Alessandro Senes.
bioRxiv posted 17 August 2025.
doi:10.1101/2025.04.26.649789.
Van der Waals packing by bulky apolar side chains contributes modestly to TM helix‑helix stability: specific small‑residue motifs, interfacial H‑bonding, and electrostatics dominate dimer energetics.
The results challenge “knobs‑into‑holes” as a primary stabilizer.
Membranes
A constricted mitochondrial morphology formed during respiration.
Singh MK, Cavellini L, Morcillo-Parra MA, Kunz C, Lelek M, Bomme P, Barascu A, Alsayyah C, Teixeira MT, Belgareh-Touzé N, Mallet A, Dietrich L, Zimmer C, Cohen MM.
Nat Commun. 2025 Jul 1;16(1):5314.
doi: 10.1038/s41467-025-60658-9.
PMID: 40595511.
Live‑cell and ultrastructural analyses reveal a characteristic “constricted” mitochondrial state that emerges under respiratory activity.
=> Link between respiration dynamics and membrane ultrastructure and mitochondrial function.
This morphology reflects coordinated IM/OM remodeling and is reversible with metabolic shifts.
The state associates with altered cristae organization and impacts bioenergetic readouts.
How PGL finds a sweet spot in phospholipid membranes – a combined multiscale MD and NMR study.
Schahl A, Réat V, Malaga W, Birbes C, Czaplicki G, Jolibois F, Yamamoto E, Ramos P, Milon A, Saurel O, Atkinson RA, Astarie-Dequeker C, Guilhot C, Ferré G, Chavent M, Haanappel E.
Biophys J. 2025 Aug 5:S0006-3495(25)00489-8.
doi: 10.1016/j.bpj.2025.07.040. Epub ahead of print.
PMID: 40770879.
Phenolic glycolipids (PGLs) partition to a preferred interfacial depth that balances hydrophobic anchoring and headgroup interactions.
MD/NMR to define orientation, insertion depth, and local membrane perturbations.
The positioning explains PGL‑driven nanoscale organization and potential curvature effects: clarifies how mycobacterial lipids modulate host and bacterial membranes.
Passive Membrane Transport Analysis of Drug Mixtures.
Strutt R, Berlanda SF, Dittrich PS.
Anal Chem. 2025 Aug 5.
doi: 10.1021/acs.analchem.5c02264. Online ahead of print.
PMID: 40763075.
Label‑free HPLC‑MS method coupled to droplet‑interface bilayers to quantify passive transport from drug mixtures.
Classification of permeability across diverse FDA‑approved compounds + correlation of transport with properties such as retention time, H‑bond donor count, lipophilicity, and predicted gut absorption.
Data support coexistence of simple and facilitated diffusion in the presence of proteins.
Statin drugs and lipid modulation: Mechanistic basis considering lipid rafts, kinase signaling, myopathy, and cancer.
Karthikeyan S, Somasundaram P, Karimi I, Lagunas-Rangel FA, Alsehli AM, Fredriksson R, Jonsson J, Schiöth HB.
Pharmacol Res. 2025 Aug 14:107912.
doi: 10.1016/j.phrs.2025.107912. Online ahead of print.
PMID: 40818822 Review.
Evidence that statins modulate membrane nanodomains and downstream signaling beyond LDL lowering.
Authors discuss raft composition, prenylation, kinase pathways, and how these relate to myopathy risk and cancer contexts.
Exploring lipid diversity and minimalism to define membrane requirements for synthetic cells.
Gan S, Scarpelli V, Exterkate M.
FEBS Lett. 2025 Aug 11.
doi: 10.1002/1873-3468.70131. Online ahead of print.
PMID: 40787853.
Lipid compositional diversity vs minimal sets needed for robust, controllable synthetic-cell membranes (charge, chain unsaturation, and curvature lipids define permeability and protein compatibility).
Structure and dynamics of asymmetric membranes: general discussion.
Andreghetti D, Barrera FN, Conboy JC, Connell S, Cooney A, Deng Z, Deserno M, Dimova R, Doktorova M, Enoki TA, Farago O, Feigenson GW, Fellows AP, Fiorin G, Giacomello A, Golani G, Goni FM, Heerklotz H, Heuer A, Huster D, Jin D, John B, Kaltenegger M, Kaur M, Kaur S, Khalid S, Kozlov MM, Law RV, Levental I, Li Z, Lipowsky R, Lolicato F, London E, Losada Pérez P, Lu T, Lyman E, Mirzajani N, Nickel W, Pabst G, Rao M, Reagle T, Roke S, Schwieger C, Seddon JM, Swiderska I, Vacha R, Varma M, Villanueva ME, Voigt A.
Faraday Discuss. 2025 Aug 1.
doi: 10.1039/d5fd90020d. Epub ahead of print.
PMID: 40748040.
Discussion about the advances in modeling and measuring leaflet‑asymmetric bilayers, from MD to scattering and surface spectroscopy.
Need fo standardized asymmetric models and cross‑validated experimental benchmarks.
Study of Protein-Protein Interactions in Septin Assembly: Multiple amphipathic helix domains cooperate in binding to the lipid membrane.
Mahsa Mofidi, Abhilash Sahoo, Christopher Edelmaier, Stepehen Klawa, Ronit Freeman, Amy Gladfelter, Mark Gregory Forest, Ehssan Nazockdast, Sonya M Hanson.
bioRxiv 2025.08.08.669402.
doi: https://doi.org/10.1101/2025.08.08.669402.
How several amphipathic helices within septin assemblies cooperate to bind lipids and sense membrane curvature.
Cooperative action tunes affinity and spatial patterning => filament organization and higher‑order assembly.
Modeling and experiments converge on multivalent helix–lipid engagement as a key design.
Lipid Bilayer Membranes with Asymmetrically Distributed LPC and DAG.
Chang Liu, Zhongjie Han, Rui Ma, and Chen Song.
bioRxiv posted 16 August 2025.
doi:10.1101/2025.08.13.670206.
Asymmetric enrichment of lysophosphatidylcholine and diacylglycerol => pronounced leaflet stress and changes in bilayer mechanics.
Quantification of the effects on thickness, order, and curvature tendencies relevant to signaling and remodeling.
Molecules
Detergent Choice Shapes the Solution Structures of Photosystems I and II: Implications for Crystallization and High-Resolution Studies.
Golub M, Boyka J, Gätcke J, Hart O, Haupt S, Wieland DCF, Blanchet CE, Zouni A, Pieper J.
J Phys Chem B. 2025 Aug 8.
doi: 10.1021/acs.jpcb.5c00767. Epub ahead of print.
PMID: 40779708.
SAXS and CD to compare PSI/PSII solubilized in C12E8 versus DDM.
C12E8 produces a more compact belt and distinct thermal behavior relative to DDM.
=> influence solution conformation and stability, with practical consequences for crystallization and high‑resolution studies.
Methods
SOuLMuSiC, a novel tool for predicting the impact of mutations on protein solubility.
Attanasio S, Kwasigroch J, Rooman M, Pucci F.
Sci Rep. 2025 Jul 29;15(1):27531.
doi: 10.1038/s41598-025-11326-x.
PMID: 40721931.
SOuLMuSiC = sequence/structure features and supervised learning to score solubility changes upon mutation.
Improved performance over prior predictors on curated datasets.
Microbio
Functional interplay between RND efflux pumps and GacS in Pseudomonas aeruginosa.
Adamiak JW, Bergen C, Ajmal L, Reddy S, Anderson PG, Rybenkov VV, Zgurskaya HI.
Appl Environ Microbiol. 2025 Aug 18:e0122325.
doi: 10.1128/aem.01223-25. Online ahead of print.
PMID: 40824111.
Link between RND efflux activity and GacS signaling in virulence and biofilm traits.
Feedback between envelope transport and two‑component regulation.
Phenotypic assays demonstrate consequences for antibiotic tolerance and community behavior.
MexR and NalD are pyocyanin-responsive transcriptional repressors of the efflux pump MexAB-OprM in Pseudomonas aeruginosa.
Cancan Wu, Maofeng Wang, Yumeng Xiao, Shubao Zhao, Xiaoqiong Jiang, Kundi Zhang, Hongwei Wang, Hongjie Dong, Sujuan Xu, Tiantian Su, Lichuan Gu.
Nucleic Acids Research, Volume 53, Issue 14, 12 August 2025, gkaf747,.
https://doi.org/10.1093/nar/gkaf747.
Pyocyanin modulates MexR and NalD, altering repression of MexAB‑OprM.
Structural/biochemical data link redox‑active ligand sensing to DNA‑binding and transcriptional output.
Changes in MexAB‑OprM levels influence resistance profiles under metabolite exposure.
Accurate antibiotic accumulation in Enterobacteriaceae isolates expressing efflux pumps.
Tabcheh J, Vergalli J, Pagès JM, Brunel JM.
Biochim Biophys Acta Biomembr. 2025 Aug 8:184441.
doi: 10.1016/j.bbamem.2025.184441. Epub ahead of print.
PMID: 40784404.
Rapid, gentle lysis protocol to quantify intracellular antibiotic levels without altering the drugs: precise, reproducible accumulation measurements suited to mechanism‑of‑resistance studies.
Ceftazidime-Induced Overexpression of MexJK-OprM Confers Resistance to Ceftolozane/Tazobactam in an Isolate of Pseudomonas aeruginosa.
Sato T, Tamura M, Kaimori K, Okumura F, Ikejima S, Nakai H, Kawamura M, Fujimura S.
Infect Drug Resist. 2025 Aug 8;18:3947-3956.
doi: 10.2147/IDR.S540567. eCollection 2025.
PMID: 40799953.
Exposure to ceftazidime => upregulation of MexJK‑OprM in a clinical isolate.
=> elevated MICs to ceftolozane/tazobactam = collateral resistance route.
Gene expression and susceptibility assays substantiate the mechanism.
Beyond Gatekeeping: Efflux Pumps Remotely Destabilize Cytoplasmic Drug–Target Interactions by Limiting Rebinding.
Subrata Dev, Keiran Stevenson, Dai Le, Minsu Kim.
bioRxiv 2025.08.06.668934.
doi: https://doi.org/10.1101/2025.08.06.668934.
Modeling and experiments: active efflux reduces intracellular drug target occupancy not only by export but by preventing local rebinding.
“Remote destabilization” lowers effective target engagement even when influx is substantial.
The effect depends on pump kinetics and intracellular diffusion constraints.
Galleria mellonella as an Infection and Antibiotic Treatment Model for Acinetobacter baumannii.
White D, Sykes EME, Kumar A.
J Vis Exp. 2025 Jul 25;(221). doi: 10.3791/68625.
PMID: 40788840.
JoVE protocol detailing infection, readouts, and antibiotic testing in Galleria larvae challenged with A. baumannii. Survival, burden, and histology endpoints are standardized for reproducibility.
Loss of cardiolipin and porins bypasses the essentiality of the sigma E cell envelope stress response in Escherichia coli.
Yang Z, Goodall ECA, Zhang B, Torres VV, Rooke JL, Pullela K, Da Costa RM, Icke C, Blaskovich MA, Legood S, Cunningham AF, Vollmer W, Bryant JA, Henderson IR.
mBio. 2025 Aug 18:e0161325.
doi: 10.1128/mbio.01613-25. Online ahead of print.
PMID: 40823832.
∆CL + ∆OmpC => suppression of periplasmic stress, rendering sigma E nonessential.
The natural diversity of E. coli transporter-dependent capsules.
Carine Roese Mores, Samuel Miravet-Verde, Elisabetta Cacace, Christoph Rutschmann, Chia-Wei Lin, Hans J Ruscheweyh, Aline Cuenod, Elisa Cappio Barazzone, Enora Marrec, Kateryna Vershynina, Raffael Schumann, Dan J Bower, Mario Schubert, Adrian Egli, Timm Fiebig, Emma Slack, Shinichi Sunagawa, and Timothy G Keys.
bioRxiv posted 10 August 2025.
doi:10.1101/2025.08.07.669119.
Genome‑to‑phenotype mapping => unexpectedly broad diversity in capsules whose assembly depends on dedicated transporters.
Authors chart capsule chemotypes, transporter associations, and ecological distribution across strains.
Miscellaneous
Cancelling mRNA studies is the highest irresponsibility.
Nature. 2025 Aug;644(8077):579.
doi: 10.1038/d41586-025-02612-9.
PMID: 40817197.
The decision announced by US health secretary Robert F. Kennedy Jr to cancel federal funding for a slate of mRNA research projects is the highest irresponsibility, argues a Nature editorial. “Shock and disbelief does not even begin to describe the reaction from mRNA and public-health researchers” as the world’s one-time science superpower turns away from the Nobel-prizewinning technology, which saved millions of lives during the COVID-19 pandemic and shows promise for doing so much more. Now other countries must forge ahead, argues the editorial.
Why chocolate tastes so good: microbes that fine-tune its flavour.
Kavanagh K.
Nature. 2025 Aug 18.
doi: 10.1038/d41586-025-02659-8. Epub ahead of print.
PMID: 40826287.
Researchers investigating how to fine-tune the process of fermenting cocoa beans have discovered that pH, temperature and microbial species all influence how the resulting chocolate tastes. Unlike wine, beer and cheese, cacao fermentation is a natural process that usually takes place without adding specific microbes — so less is known about exactly how it happens. A panel of trained food tasters helped determine that unique microbial communities influenced the flavour.
Mechanisms underlying the influence of “roe rubbing” and “salt mixing” on the qualitative transformation of fish roe into caviar: focusing on membrane phospholipids and proteins.
Zhang W, Shen J, Liu T, Chen C, Wang J, Bai F, Xu P, Gao R, Zhao Y, Xu X.
Food Chem. 2025 Jul 28;493(Pt 2):145747.
doi: 10.1016/j.foodchem.2025.145747. Online ahead of print.
PMID: 40774214.
Mechanistic insight into how artisanal practices drive the biochemical transformation of roe into high-quality caviar.
Traditional processing steps (rubbing fish roe to separate eggs and mixing with salt) alter roe quality at the molecular level.
Lipidomic and proteomic => these treatments restructure membrane phospholipids, leading to changes in membrane fluidity and stability.
Protein conformations are modified, influencing texture, color, and flavor development during caviar maturation.