Latest Publications
From the lens of early-career researchers: bridging science, technology, arts, and humanities to tackle antimicrobial resistance
Nikhil Bhalla, Mojgan Rabiey, Prachi Bendale, Katie Lawther, Janice Spencer, Alberto Longo, Lucky Lucky, Vishal Chaudhary, Paul McCormack, Saikat Jana, Patrick S. M. Dunlop, Linda Oyama
Antimicrobial resistance (AMR) is a silent pandemic that presents a global challenge, urging researchers to develop innovative and transdisciplinary solutions. Our initiative aims to promote collaboration across science, engineering, economics, social sciences, and the arts to address the complex dimensions of AMR. We highlight the unique role of early-career researchers (ECRs) in advancing such cross-cutting approaches and conclude that empowering ECRs through equitable support and recognition is essential to sustaining innovation and mobilising communities against AMR.
Identification of evidence gaps and future research needs in food safety
Neuroimmune Regulation by TRPM2 Channels
Xuming Zhang, Mitali Malhotra
Mutual interaction between the nervous and immune systems underpins many pathophysiological processes. Transient Receptor Potential Melastatin 2 (TRPM2) channels are abundantly expressed in both systems, acting as a critical interface of neuroimmune interaction. TRPM2 channels in immune cells participate in innate immunity and immune inflammation by acting as an oxidative stress and metabolic sensor. TRPM2 in neurons functions not only as an oxidative sensor but also a temperature sensor and a pain transducer critical to neuronal death, temperature sensing, thermoregulation, and chronic pain. Cooperation between immune and neuronal TRPM2 influences the outcome of neuroimmune interaction and many diseases such as infection, inflammation, ischemic stroke, pain, and neurodegenerative diseases. Improved understanding of neuronal and immune TRPM2 interaction is essential for therapeutic interventions for the treatment of diseases mediated by TRPM2 channels.
A holistic view on disease-modifying aspects, comorbidities, and contemporary neuroprotective approaches
Piotr Walczak, Shen Li, Xunming Ji, Johannes Boltze
Most conditions of the central nervous system (CNS) and the peripheral nervous system are not stand-alone disorders but are modulated and influenced by other pathobiological processes. For instance, the impact of frequent comorbidities such as hypertension or dyslipidemia as factors contributing to and aggravating CNS diseases has been much better understood in recent years. Another prominent disease-modifying factor is the gut microbiome which can exert both protective and detrimental effects on the nervous system in health and disease. An even better understanding of these factors will contribute to the development of individualized treatment approaches, a major research objective in the era of precision medicine. The current issue of Neuroprotection presents articles focusing on disease-modifying factors or novel treatment approaches for a broad spectrum of conditions. This provides a wide perspective but also novel insights into disease mechanisms and targeted treatment approaches. Priority has been given to articles reporting, reviewing or meta-analyzing clinical data as well as articles providing results of translationally relevant preclinical work.
Bioconversion kinetics and valorisation of oil palm empty fruit bunches for biomethane production and lignin derived compounds
Irnia Nurika, Eka Nur Shabrina, Nurul Azizah, Sri Suhartini, Guy C. Barker, Timothy D.H. Bugg
This study assesses the facultative anaerobe Comamonas testosteroni as a mild, chemical-free pre-treatment for valorising oil palm empty fruit bunches (OPEFB) into biomethane and lignin-derived aromatics. Incubation with 2 % (v/v) C. testosteroni for 7 days at 30 °C, reduced lignin to 15.67 % (33.42 % removal), while retaining high cellulose (53.48–56.19 %) and hemicellulose (up to 16.21 %). Pre-treated OPEFB showed 20 % weight loss (vs 8 % in controls) and a 51 % rise in total soluble phenols, evidencing active lignin depolymerisation. GC–MS of liquor and solids qualitatively confirmed lignin breakdown and identified representative low-molecular-weight products (e.g., phenol, betulin, acetic acid and benzoxazole), supporting co-product potential. In biochemical methane potential tests, the pre-treated residue achieved a specific methane potential of 0.173 m³ CH4 kg⁻¹ VS, an 85 % increase over the abiotic residue and higher than non-treated OPEFB. Kinetic fitting with Transference, Modified Gompertz and Logistic models yielded good agreement (R2 up to 0.92), with Modified Gompertz best capturing cumulative methane production and the shortest lag phases. A simple energy check indicates a favourable margin: the incremental methane (ΔSMP ≈ 0.08 m³ CH₄ kg⁻¹ VS) equates ∼0.8 kWh kg⁻¹ VS, whereas estimated mixing for pre-treatment is ∼0.017–0.034 kWh kg⁻¹ VS. Overall C. testosteroni pre-treatment enables dual valorisation (biomethane plus aromatics) under mesophilic conditions, offering a practical route for integrated OPEFB biorefineries.
Streptococcus pneumoniae S protein activates PBP1a to regulate peptidoglycan remodelling and cell division
Hugo Millat, Cassandra Falcou, Cassandra Lenoir, Nicholas S. Briggs, Jack Stone, Pierre Simon Garcia, Sylvie Manuse, Caroline Cluzel, André Zapun, Cécile Morlot, David I. Roper, Adrien Ducret, Christophe Grangeasse
Class A penicillin-binding proteins (aPBPs) are involved in the biosynthesis and remodelling of peptidoglycan (PG). The human bacterial pathogen Streptococcus pneumoniae produces three aPBPs, which are regulated to maintain the bacterium’s ovoid shape. Evidence suggests that PBP1a and PBP2a activities are closely coordinated; however, their precise functions remain unclear. Here we characterized the pneumococcal S protein, which contains a LysM-PG-binding domain and a GpsB-interacting domain. Using S protein fusion constructs or mutant bacterial strains, we show that S protein localizes to the division ring and is required to prevent premature cell lysis and minicell formation due to aberrant division site placement. S protein interacts with PBP1a and activates its PG synthesis activity. Co-immunoprecipitation experiments combined with biochemical, genetic, structural prediction and microscopy analyses suggest that S protein is part of a larger multiprotein complex containing aPBPs and PG-modifying enzymes, and coordinated by the scaffolding protein GpsB. Together, these findings suggest that a GpsB-associated complex orchestrates PG biosynthesis and remodelling in S. pneumoniae.