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Innovative Ricin Toxin Detection: Unraveling Apurinic/Apyrimidinic Lyase Activity and Developing Fluorescence Sensors.
Anal Chem
January 2025
State Key Laboratory of Pathogen and Biosecurity, Academy of Military Medical Sciences, Beijing 100071, China.
Ricin toxin (RT) is a potential bioterrorism agent because of its high potency, extremely small lethal dose, ease of preparation, and notable stability. Therefore, a portable method is urgently required to efficiently detect and determine the presence of toxicity of RT and evaluate its potency for public health monitoring and counter-bioterrorism responses. Currently, enzyme-based assays for detecting RT mainly focus on its -glycosidase activity.
View Article and Find Full Text PDFOptimal nitrite degradation by isolated Bacillus subtilis sp. N4 and applied for intensive aquaculture water quality management with immobilized strains.
J Environ Manage
February 2025
Department of Chemical Engineering and Biotechnology, National Taipei University of Technology, Taipei, Taiwan. Electronic address:
The toxicity of nitrite is an issue that cannot be overlooked in nitrogen pollution within aquaculture. A highly efficient bacterium capable of simultaneous nitrification and denitrification was screened from natto, and its 16S rRNA gene sequence was compared to existing records, confirming its identification as Bacillus subtilis sp. N4.
View Article and Find Full Text PDFMechanism and Kinetics of HIV-1 Protease Activation.
Viruses
November 2024
Center for Proteomics and Bioinformatics, Department of Nutrition, School of Medicine, Case Western Reserve University, Cleveland, OH 44106, USA.
The HIV-1 protease is a critical enzyme for viral replication. Because protease activity is necessary to generate mature infectious virions, it is a primary target of antiretroviral treatment. Here, we provide an overview of the mechanisms regulating protease activation and the methods available to assess protease activity.
View Article and Find Full Text PDFA detailed kinetic model of Eastern equine encephalitis virus replication in a susceptible host cell.
bioRxiv
December 2024
Department of Computational and Systems Biology, University of Pittsburgh, Pittsburgh, Pennsylvania, United States of America.
Eastern equine encephalitis virus (EEEV) is an arthropod-borne, positive-sense RNA alphavirus posing a substantial threat to public health. Unlike similar viruses such as SARS-CoV-2, EEEV replicates efficiently in neurons, producing progeny viral particles as soon as 3-4 hours post-infection. EEEV infection, which can cause severe encephalitis with a human mortality rate surpassing 30%, has no licensed, targeted therapies, leaving patients to rely on supportive care.
View Article and Find Full Text PDFDynamic binding of the bacterial chaperone Trigger factor to translating ribosomes in .
Proc Natl Acad Sci U S A
January 2025
Department of Cell & Molecular Biology, Uppsala University, Uppsala SE-75124, Sweden.
The bacterial chaperone Trigger factor (TF) binds to ribosome-nascent chain complexes (RNCs) and cotranslationally aids the folding of proteins in bacteria. Decades of studies have given a broad, but often conflicting, description of the substrate specificity of TF, its RNC-binding dynamics, and competition with other RNC-binding factors, such as the Signal Recognition Particle (SRP). Previous RNC-binding kinetics experiments were commonly conducted on stalled RNCs in reconstituted systems, and consequently, may not be representative of the interaction of TF with ribosomes translating mRNA in the cytoplasm of the cell.
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