The Gram-positive bacterium Staphylococcus aureus infects diverse tissues and causes a wide spectrum of diseases, suggesting that it possesses a repertoire of distinct molecular mechanisms promoting bacterial survival in disparate in vivo environments. Signature-tag transposon mutagenesis screening of a 1520-member library identified numerous S. aureus genetic loci affecting growth and survival in four complementary animal infection models including mouse abscess, bacteraemia and wound and rabbit endocarditis. Of a total of 237 in vivo attenuated mutants identified by the murine models, less than 10% showed attenuation in all three models, emphasizing the advantage of screening in diverse disease environments. The largest gene class identified by these analyses encoded peptide and amino acid transporters, some of which were important for S. aureus survival in all animal infection models tested. The identification of staphylococcal loci affecting growth, persistence and virulence in multiple tissue environments provides insight into the complexities of human infection and on the molecular mechanisms that could be targeted by new antibacterial therapies.
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http://dx.doi.org/10.1046/j.1365-2958.1998.01075.x | DOI Listing |
Ann Clin Microbiol Antimicrob
January 2025
Division of Infectious Diseases, Department of Internal Medicine, National Taiwan University Hospital, 7 Chung-Shan South Road, Taipei, 100, Taiwan.
Background: Nemonoxacin is a new quinolone with an antibacterial efficacy against methicillin-resistant Staphylococcus aureus (MRSA). Certain sequence types (STs) have been emerging in Taiwan, including fluoroquinolone-resistant ST8/USA300. It's an urgent need to determine nemonoxacin susceptibility against ST8/USA300 and other emerging lineages, if any.
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January 2025
Department of Molecular Biology & Bioinformatics, Tripura University, Suryamaninagar, Tripura 799022, India. Electronic address:
Int J Biol Macromol
January 2025
School of Veterinary Medicine, Jiangsu Co-innovation Center for Prevention and Control of Important Animal Infectious Diseases and Zoonoses, Yangzhou University, Yangzhou 225009, PR China; Joint International Research Laboratory of Agriculture and Agri-Product Safety, the Ministry of Education of China, Yangzhou University, Yangzhou, Jiangsu 225009, PR China. Electronic address:
Bacterial-infected wounds usually lead to slow wound healing due to increased inflammation, especially wounds infected by drug-resistant bacteria, which is a serious challenge in the biomedical field. Traditional antimicrobial strategies such as antibiotics lead to a significant increase in drug-resistant strains and have limited efficacy. Therefore, there is an urgent need to develop multifunctional dressings with excellent antibacterial activity and promotion of wound healing.
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January 2025
College of Pharmacy, Guangxi University of Chinese Medicine, Nanning, China. Electronic address:
Bacterial infections impede skin wound healing, and antibacterial hydrogels have garnered significant attention in the field of wound care due to their combined therapeutic effects. In this study, an intelligent, responsive AC-Gel@Cur-Au hydrogel was developed using temperature-sensitive agarose and pH-responsive chitosan as the structural framework, infused with Gel@Cur and AuNR. The AC-Gel@Cur-Au hydrogels demonstrated excellent mechanical properties, swelling capacity, tissue adhesion, and biodegradability.
View Article and Find Full Text PDFInt J Biol Macromol
January 2025
Division of Infectious Diseases and Immunology, Department of Microbiology, School of Medicine, Iwate Medical University, 1-1-1 Idaidori, Yahaba, Iwate 028-3694, Japan. Electronic address:
Chitinase plays a role in mammalian immune responses, particularly in the degradation of fungal cell walls. The aim of the present study was to express and characterize recombinant mouse chitotriosidase (Chit1) and acidic mammalian chitinase (AMCase) without the ZZ domain, a domain that may interfere with immunological analyses. We successfully expressed recombinant chitinases without the ZZ domain (Chit1-V5-His and AMCase-V5-His) as a soluble protein from an expression vector pET21a in the Escherichia coli Rosetta-gami B (DE3) strain.
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