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Search indexed NASA NTRS and DOE OSTI research on propulsion, heat transfer, battery materials and energy systems. Follow report and document links to the original sources.
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Inhibition of Fosfomycin Resistance Protein FosB from Gram-Positive Pathogens by Phosphonoformate
Not provided.
Pathogenic C9ORF72 Antisense Repeat RNA Forms a Double Helix with Tandem C:C Mismatches
Expansion of a GGGGCC/CCCCGG repeat sequence in the first intron of the C9ORF72 gene is a leading cause of frontotemporal dementia (FTD) and amyotrophic lateral sclerosis (ALS). In this combined disorder, called c9FTD/ALS, the expansion is bidirectionally transcribed into sense and antisense repeat RNA associated with disease. To better understand the role of C9ORF72 repeat RNA in molecular disease pathology, in this work we determined crystal structures of a [(CCCCGG) 3 (CCCC)] model antisense repeat RNA to 1.47 Å resolution. The RNA structure was an A-form-like double helix composed of repeating and regularly spaced tandem C:C mismatch pairs that perturbed helical geometry and surface charge. Solution studies revealed a preference for A-form-like helical conformations as the repeat number increased. Results provide a structural starting point for rationalizing the contribution of repeat RNA to c9FTD/ALS molecular disease mechanisms and for developing molecules to target C9ORF72 repeat RNA as potential therapeutics.
Structural and Functional Studies of Bacterial Enolase, a Potential Target against Gram-Negative Pathogens
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Benchmarking Concentration and Extraction Methods for Wastewater-Based Surveillance of Eight Human Respiratory Viruses: Implications for Rapid Application to Novel Pathogens
To provide early warning and support a rapid response to a novel virus through wastewater surveillance, it would be ideal to understand in advance which concentration and extraction methods are likely to be effective for dPCR-based methods, depending on virus characteristics. In this study, we spiked raw wastewater samples with eight human respiratory viruses and processed them with four methods that concentrate and/or extract nucleic acids from both liquid and solid fractions (Promega, Nanotrap, and InnovaPrep) or only the solid fraction of wastewater (Solids). Our findings provide encouraging evidence that all four methods combined with dPCR could detect an emerging virus in wastewater, although they differed in sensitivity. The pattern of recovery efficiency for adenoviruses, coronaviruses, and influenza A viruses was consistent across methods, with Promega producing higher median recovery efficiencies, while distinct patterns were observed for coxsackieviruses. We also normalized the concentration data with two endogenous fecal indicators, PMMoV and Carjivirus (formerly crAssphage). We found that normalization could reduce method-associated differences if the indicator exhibited a recovery pattern similar to that of the target virus. These findings can guide the selection of concentration and extraction methods for wastewater monitoring based on the properties of target viruses, thus enhancing pandemic preparedness.
Peptide Inhibitors of Bacterial Protein Synthesis with Broad Spectrum and SbmA-Independent Bactericidal Activity against Clinical Pathogens
Abstract not provided
DC Recruiter: A Pathogen-Agnostic Immune Enhancer for Broad-Spectrum Antimicrobial Protection
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Biosynthesis, Mechanism of Action, and Inhibition of the Enterotoxin Tilimycin Produced by the Opportunistic Pathogen Klebsiella oxytoca
Abstract not provided
Self-Assembly of Antimicrobial Peptoids Impacts Their Biological Effects on ESKAPE Bacterial Pathogens
Not Available
A [FeFe] Hydrogenase–Rubrerythrin Chimeric Enzyme Functions to Couple H 2 Oxidation to Reduction of H 2 O 2 in the Foodborne Pathogen Clostridium perfringens
[FeFe] hydrogenases are a diverse class of H 2 -activating enzymes with a wide range of utilities in nature. As H 2 is a promising renewable energy carrier, exploration of the increasingly realized functional diversity of [FeFe] hydrogenases is instrumental for understanding how these remarkable enzymes can benefit society and inspire new technologies. In this work, we uncover the properties of a highly unusual natural chimera composed of a [FeFe] hydrogenase and rubrerythrin as a single polypeptide. The unique combination of [FeFe] hydrogenase with rubrerythrin, an enzyme that functions in H 2 O 2 detoxification, raises the question of whether catalytic reactions, such as H 2 oxidation and H 2 O 2 reduction, are functionally linked. Herein, we express and purify a representative chimera from Clostridium perfringens (termed Cper HydR) and apply various electrochemical and spectroscopic approaches to determine its activity and confirm the presence of each of the proposed metallocofactors. The cumulative data demonstrate that the enzyme contains a surprising array of metallocofactors: the catalytic site of [FeFe] hydrogenase termed the H-cluster, two [4Fe-4S] clusters, two rubredoxin Fe(Cys) 4 centers, and a hemerythrin-like diiron site. The absence of an H 2 -evolution current in protein film voltammetry highlights an exceptional bias of this enzyme toward H 2 oxidation to the greatest extent that has been observed for a [FeFe] hydrogenase. Here, we demonstrate that Cper HydR uses H 2 , catalytically split by the hydrogenase domain, to reduce H 2 O 2 by the diiron site. Structural modeling suggests a homodimeric nature of the protein. Overall, this study demonstrates that Cper HydR is an H 2 -dependent H 2 O 2 reductase. Equipped with this information, we discuss the possible role of this enzyme as a part of the oxygen-stress response system, proposing that Cper HydR constitutes a new pathway for H 2 O 2 mitigation.
Structural Determination of a New Peptidolipid Family from Rhodococcus opacus and the Pathogen Rhodococcus equi by Multiple Stage Mass Spectrometry
Not provided.
Structure of the proton-gated urea channel from the gastric pathogen Helicobacter pylori
Abstract not provided
Rapid point-of-care detection of the tuberculosis pathogen using a BlaC-specific fluorogenic probe
Abstract not provided
Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein
Misfolded α-synuclein amyloid fibrils are the principal components of Lewy bodies and neurites, hallmarks of Parkinson's disease (PD). In this paper, we present a high-resolution structure of an α-synuclein fibril, in a form that induces robust pathology in primary neuronal culture, determined by solid-state NMR spectroscopy and validated by EM and X-ray fiber diffraction. Over 200 unique long-range distance restraints define a consensus structure with common amyloid features including parallel, in-register β-sheets and hydrophobic-core residues, and with substantial complexity arising from diverse structural features including an intermolecular salt bridge, a glutamine ladder, close backbone interactions involving small residues, and several steric zippers stabilizing a new orthogonal Greek-key topology. These characteristics contribute to the robust propagation of this fibril form, as supported by the structural similarity of early-onset-PD mutants. Finally, the structure provides a framework for understanding the interactions of α-synuclein with other proteins and small molecules, to aid in PD diagnosis and treatment.