is a prevalent opportunistic pathogen responsible for a wide range of infections in livestock and wildlife, such as in cattle, pigs, European bison and forest musk deer. Much of the successful infection of relies on its virulence factors, including pyolysin as well as adhesion factors. The swift rise of bacterial resistance has highlighted the urgent need for developing new therapeutic strategies. Currently, virulence factor-mediated vaccine development and other therapeutic approaches are widely regarded as the primary interventions for addressing diseases associated with this pathogen. This review examines the broader virulence potential of , focusing on haemolysin, host cell adhesion proteins, the prevalence of antibiotic resistance, and the development of vaccines mediated by virulence factors. Additionally, it discusses current and future approaches aimed at improving therapeutic interventions.
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http://dx.doi.org/10.1080/21505594.2025.2467161 | DOI Listing |
PLoS One
March 2025
Dr. Panjwani Center for Molecular Medicine and Drug Research, International Center for Chemical and Biological Sciences, University of Karachi, Karachi, Pakistan.
Gardnerella vaginalis is the most frequently identified bacterium in approximately 95% of bacterial vaginosis (BV) cases. This species often exhibits resistance to multiple antibiotics, posing challenges for treatment. Therefore, there is an urgent need to develop and explore alternative therapeutic strategies for managing bacterial vaginosis.
View Article and Find Full Text PDFPLoS One
March 2025
Department of Veterinary Medicine, University of Bari Aldo Moro, Valenzano, Bari, Italy.
Reptiles may act as reservoirs or spreaders of potential pathogenic microorganisms including Candida yeasts. While the epidemiology of yeast species has been thoroughly studied, the virulence profile of isolated species is not well investigated. Therefore, this study aimed to assess the haemolytic, phospholipase, lipase activities and biofilm formation of yeasts isolated from the cloacal swabs of venomous snakes from Marrakech, Morocco (Group I, n = 40) and from non-venomous snakes from Cocullo, Italy (Group II, n = 32).
View Article and Find Full Text PDFMicrobiology (Reading)
March 2025
School of Science and Technology, Nottingham Trent University, Nottingham, UK.
Novel treatment options are needed for the gastric pathogen due to its increasing antibiotic resistance. The vitamin K analogue menadione has been extensively studied due to interest in its anti-bacterial and anti-cancer properties. Here, we investigated the effects of menadione on growth, viability, antibiotic resistance, motility and gene expression using clinical isolates.
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March 2025
Department of Clinical Laboratory, People's Hospital of Dayi County, Chengdu Sichuan, China.
Introduction: Carbapenem-resistant hypervirulent Klebsiella pneumoniae (CR-hvKP) is a highly pathogenic, drug-resistant, and transmissible "superbug" that causes infections in hospitals and communities. Because of the lack of effective antimicrobial treatment options, morbidity and mortality from CR-hvKP infections have increased dramatically, and outbreaks and the rapid spread of CR-hvKP in hospitals have become a major global public health challenge.
Methods: The mechanisms of molecular evolution in CR-hvKP include the acquisition of a hypervirulent plasmid encoding a virulence gene by carbapenemase-producing K pneumoniae, the horizontal transfer of plasmids carrying carbapenem resistance genes to hvKP, and the acquisition of fusion plasmids carrying both carbapenem resistance genes and hypervirulent genes by classic K pneumoniae.
Proteomics
March 2025
Department of Clinical Biochemistry OE4340, Hannover Medical School, Hannover, Germany.
Protein N-glycosylation influences protein folding, stability, and trafficking, and has prominent functions in cell-cell adhesion and recognition. For the parasite Toxoplasma gondii, N-glycosylation of proteins is crucial for initial adhesion to host cells, parasite motility, and consequently, its ability to invade host cells. However, the glycoproteome of T.
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