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Preparation of the immobilized α-adrenoceptor column by the ultra-high affinity protein pair CL7/Im7 and its application in drug-protein interaction analysis.
J Chromatogr B Analyt Technol Biomed Life Sci
January 2025
Northwest University Chang An Hospital, Faculty of Life Sciences and Medicine, Northwest University, Xi'an, Shaanxi 710069, China; Department of Clinical Pharmaceutics, Chang An District Hospital, Xi'an, Shaanxi 710118, China. Electronic address:
Immobilizing the target protein on a solid surface with controlled orientation, high specificity, and maintained activity is a proven strategy to enhance the stability of the protein. In this study, we employed an ultra-high affinity protein pair consisting of a mutant of colicin E7 Dnase and its corresponding inhibitor, immunity protein 7(Im7), to develop an immobilized α-adrenoceptor (α-AR) column. Briefly, we expressed α-AR fused with CL7 as a tag at its C-terminus in Escherichia coli cells.
View Article and Find Full Text PDFA historical perspective on the multifunctional outer membrane channel protein TolC in Escherichia coli.
NPJ Antimicrob Resist
January 2025
College of Biological Sciences, Department of Molecular and Cellular Biology, University of Guelph, 50 Stone Rd E, Guelph, ON, Canada.
Since its discovery nearly 60 years ago, TolC has been associated with various cellular functions in Escherichia coli, including the efflux of environmental stressors and virulence factors. It also acts as a receptor for specific bacteriophages and the colicin E1 toxin. This review highlights key discoveries over the past six decades and emphasizes the remaining gaps in understanding how TolC contributes to physiological functions in E.
View Article and Find Full Text PDFA Conjugated Oligomer with Drug Efflux Pump Inhibition and Photodynamic Therapy for Synergistically Combating Resistant Bacteria.
ACS Appl Mater Interfaces
January 2025
Key Laboratory of Analytical Chemistry for Life Science of Shaanxi Province, School of Chemistry and Chemical Engineering, Key Laboratory of Applied Surface and Colloid Chemistry, Ministry of Education, Shaanxi Normal University, Xi'an 710119, P. R. China.
High expression of drug efflux pump makes antibiotics ineffective against bacteria, leading to drug-resistant strains and even the emergence of "superbugs". Herein, we design and synthesize a dual functional o-nitrobenzene (NB)-modified conjugated oligo-polyfluorene vinylene (OPFV) photosensitizer, OPFV-NB, which can depress efflux pump activity and also possesses photodynamic therapy (PDT) for synergistically overcoming drug-resistant bacteria. Upon light irradiation, the OPFV-NB can produce aldehyde active groups to covalently bind outer membrane proteins, such as tolerant colicin (TolC), blocking drug efflux of bacteria.
View Article and Find Full Text PDFScreening and Genomic Profiling of Antimicrobial Bacteria Sourced from Poultry Slaughterhouse Effluents: Bacteriocin Production and Safety Evaluation.
Genes (Basel)
December 2024
Departamento de Nutrición y Ciencia de los Alimentos (NUTRYCIAL), Sección Departamental de Nutrición y Ciencia de los Alimentos (SD-NUTRYCIAL), Facultad de Veterinaria, Universidad Complutense de Madrid (UCM), Avenida Puerta de Hierro, s/n, 28040 Madrid, Spain.
Antimicrobial-resistant (AMR) pathogens represent a serious threat to public health, particularly in food production systems where antibiotic use remains widespread. As a result, alternative antimicrobial treatments to antibiotics are essential for effectively managing bacterial infections. This study aimed to identify and characterize novel antimicrobial peptides produced by bacteria, known as bacteriocins, as well as to recognize safe bacteriocin-producing strains, sourced from poultry slaughterhouse effluents.
View Article and Find Full Text PDFThe Actinobacillus pleuropneumoniae apxIV operon encodes an antibacterial toxin-immunity pair.
Microbiol Res
March 2025
Institute of Microbiology of the Czech Academy of Sciences, Videnska 1083, Prague 142 00, Czech Republic. Electronic address:
The ApxIVA protein belongs to a distinct class of a "clip and link" activity of Repeat-in-ToXin (RTX) exoproteins. Along with the three other pore-forming RTX toxins (ApxI, ApxII and ApxIII), ApxIVA serves as a major virulence factor of Actinobacillus pleuropneumoniae, the causative agent of porcine pneumonia. The gene encoding ApxIVA is located on a bicistronic operon downstream of the orf1 gene and is expressed exclusively under in vivo conditions.
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