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Hospital-acquired infections caused by Staphylococcus aureus and Enterococcus faecalis are significant global health challenges due to their biofilm-forming ability, also contributing to the derived antibiotic resistance and environmental persistence. This growing resistance poses serious global health challenges, emphasizing the need for better surveillance and new treatments. Plant-derived bioactives have emerged as possible therapeutics to such opportunistic pathogens and they are potential alternatives to traditional antimicrobials. This study investigates the in vitro activity of Murraya koenigii’s methanolic (MKM) leaf extract and its compounds against the growth and biofilm-forming ability of S. aureus and E. faecalis . Results revealed that the MKM extract effectively inhibited the growth of S. aureus and E. faecalis at their respective MIC levels. Furthermore, flow cytometry and confocal imaging demonstrated substantial membrane damage in MKM-treated cells compared to DMSO-treated and untreated controls. Additionally, the MKM extract significantly disrupts biofilm formation and leads to reduced extracellular polymeric substance (EPS) production. Scanning electron microscopy provided visual evidence of disrupted biofilm architecture following MKM extract treatment. HR-LC/MS analysis identified bioactive compounds within the extract, which were further evaluated for drug-likeness properties through ADME analysis. In silico molecular docking studies confirmed strong binding affinities of MKM-derived compounds with key biofilm-related receptor proteins, SpA in S. aureus and Esp in E. faecalis . These findings highlight the significant potential of MKM extract as a novel and effective phytotherapeutic resource for developing strategies to combat biofilm-associated infections.

The Indo-Pacific horseshoe crab, Tachypleus gigas is often referred to as a living fossil due to its 450 million years ancestry. It plays a critical ecological role in coastal ecosystems and offers unique insights into arthropod evolution. Despite being investigated for more than a century, its early embryonic development remains poorly understood. In this study, we identified and presented the first comprehensive proteomic characterization of the early-stage embryo of T. gigas from stage 2 to stage 5 using microscopy and mass spectrometry-based approaches, respectively. Peptides were analyzed in an EASY-nLC 1200 system coupled to an Orbitrap Fusion mass spectrometer, leading to the identification of 388 proteins. The dataset revealed enrichment in proteins associated with cellular growth, morphogenesis, cytoskeletal organization, and metabolic regulation. Functional annotation and pathway enrichment were performed using STRING v12.0, with Gene Ontology analysis highlighting key pathways related to energy metabolism, transcriptional control, and immune regulation. These findings provide new molecular perspectives on embryogenesis in T. gigas and offer a valuable reference point for future studies on chelicerate development, evolutionary biology, and species conservation.

Plastics count as one of the most potent threats to the habitats and survival of global flora and fauna. Reports keep accumulating globally about the ever-exploding load of plastic wastes, but the need and economics of multiple industrial and household processes compel the production of more plastic materials. It has always been imperative to look for natural sources of degradation of plastic. The identification of plastic-degrading microbes, therefore, remains a major focus of the microbial fraternity. While the discoveries of Ideonella sakaiensis or later, Rhizobacter gummiphilus were more out of providence, the structure determination of the enzyme responsible for PET degradation does provide a fillip to efforts towards the identification of more such prokaryotic entities. In this work, a comprehensive profiling of prokaryotic sequences has been undertaken to look for the presence of similar plastic-degradation abilities across the kingdom. The identification of twenty-seven such 'hits' across different bacterial species led us to believe in the natural diversity of plastic-degradation enzymes. Moreover, there seems to be conservation of the structural motif that renders such ability, as has been observed from the constructed models and analysis of their interfaces. Docking of BHET, one of the key products of PET, against these 27 entities showed considerable interactions with the above and pointed towards the possible roles of these bacteria as natural plastic degradation models. Eight of these proteins have very close similarity in binding interactions and surface properties to the PETase from I. sakaiensis and were shortlisted as prospective candidates. Of these eight, three PETases from Halopseudomonas pertucinogena, Halopseudomonas bauzanensis and Ketobacter sp. revealed significant similarity in structure and conformational stability to the PETase from I. sakaiensis, as was evident from the analysis of their molecular dynamics parameters. Principal Component Analysis and the free energy landscape during binding to BHET also validated the hypothesis, and these three PETases could be immediately explored for possible plastic degradation activity.

Plastics count as one of the most potent threats to the habitats and survival of global flora and fauna. Reports keep accumulating globally about the ever-exploding load of plastic wastes, but the need and economics of multiple industrial and household processes compels the production of more plastic materials. It has always been imperative to look for natural sources of degradation of plastic. The identification of plastic-degrading microbes, therefore remains a major focus of the microbial fraternity. While the discoveries of Ideonella sakaiensis or later, Rhizobacter gummiphilus were more out of providence, the structure determination of the enzyme responsible for PET degradation does provide a fillip to efforts towards identification of more such prokaryotic entities. In this work, a comprehensive profiling of prokaryotic sequences has been undertaken to look for the presence of similar plastic-degradation abilities across the kingdom. The identification of twenty-seven such ‘hits’ across different bacterial species led us to believe in the natural diversity of plastic-degradation enzymes. Moreover, there seems to be conservation of the structural motif that renders such ability as has been observed from the constructed models and analysis of their interfaces. Docking of BHET, one of the key products of PET, against these 27 entities showed considerable interactions with the above and pointed towards the possible roles of these bacteria as natural plastic degradation models. Eight of these proteins have very close similarity in binding interactions and surface properties to the PETase from I. sakaiensis and were shortlisted as prospective candidates. Of these eight, three PETases from Halopseudomonas pertucinogena Halopseudomonas bauzanensis and Ketobacter sp. revealed significant similarity in structure and conformational stability to the PETase from I. sakaiensis as was evident from the analysis of their molecular dynamics parameters. Principal Component Analysis and the free energy landscape during binding to BHET also validated the hypothesis and these three PETases could be immediately explored for possible plastic degradation activity.