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Wei Sheng Wu Xue Bao
Institute of Hygiene and Environmental Medicine, Academy of Military Medical Sciences, Tianjin 300050, China.
Published: September 2010
Objective: To identify the exotoxin-specific motifs/domains in bacterial exotoxin sequences, and to expand understanding of bacterial exotoxins pathogenic mechanisms.
Methods: We constructed a non-pathogenic bacterial proteins database and collected 89 bacterial exotoxin sequences from Virulence factor database (VFDB), then we analyzed these protein sequences by motif/domain search using InterProScan (www.ebi.ac.uk/Tools/InterProScan/).
Results: We identified 39 exotoxin-specific motifs/domains in 89 bacterial exotoxin sequences.
Conclusion: The identified exotoxin-specific motifs/domains were closely related to the functions of the exotoxins and could be used as template to search for new exotoxins by mining pathogenic bacterial genomes. The analysis of the acquired Gene Ontology (GO) items was to further expend our understanding of bacterial exotoxin pathogenic mechanisms.
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Commun Biol
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Department of Life Sciences, University of Bath, Bath, UK.
Mono-ADP-ribosyl transferase (mART) proteins are secreted virulence factors produced by several human pathogens, the founding member being diphtheria toxin (DT). Pseudomonas aeruginosa can also secrete a mART toxin, known as exotoxin A (PE), but with an organization of its three functional domains (receptor, translocation, and enzymatic elements) that is opposite to DT. Two additional PE-like toxins (PLTs) have been identified from Vibrio cholerae and Aeromonas hydrophila, suggesting more PLT family members may exist.
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Department of Animal and Veterinary Sciences, University of Vermont, Burlington, VT, USA.
Background: Staphylococcus aureus is a leading cause of mastitis in dairy livestock and is a pathogen with unknown but potential impact on public and herd health in Maine. The primary objective of this study was to describe retrospective trends in S. aureus detection at the University of Maine Cooperative Extension Veterinary Diagnostic Laboratory (UMVDL) for milk samples submitted between July 2017 and June 2022.
View Article and Find Full Text PDFXi Bao Yu Fen Zi Mian Yi Xue Za Zhi
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State Key Laboratory of Pathogen and Biosecurity, Academy of Military Medical Sciences, Beijing 100071, China. *Corresponding authors, E-mail:
Objective To evaluate whether Vibrio vulnificus secreted exotoxin-hemolysin (VVH) can activate platelet, an important blood immune cell, and to explore the possible molecular mechanism of platelet activation by VVH. Methods Transcriptomics and immunohistochemistry were used to analyze whether Vibrio vulnificus infection caused platelet activation in mice. Then, flow cytometry was used to identify whether VVH was the main stimulator of platelet activation.
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Laboratory of Veterinary Pharmacology, Faculty of Veterinary Medicine, Okayama University of Science, Ehime, Japan.
Streptolysin O (SLO), a bacterial toxin produced by common hemolytic streptococci, including Streptococcus pyogenes and resident microbiota, may be associated with inflammation in the cardiovascular system. We previously reported that short-term treatment with SLO at relatively high concentrations (10-1000 ng/mL) diminished acetylcholine-induced, endothelial-dependent relaxation in a concentration-dependent manner. However, the vascular function effects of long-term exposure to SLO at lower concentrations are poorly understood.
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Department of Clinical Sciences Lund, Infection Medicine, Faculty of Medicine, Lund University, 221 84 Lund, Sweden.
Antibodies are critical to the host's immune defense against bacterial pathogens. Understanding the mechanisms of antibody-antigen interactions is essential for developing new targeted immunotherapies. Building computational workflows that can identify where an antibody binds its cognate antigen and deconvoluting the interaction interface in a high-throughput manner are critical for advancing this field.
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