Staphylococcus aureus is an important pathogen of man, but is also able to colonize and cause disease in a wide variety of mammals and birds. An extended multilocus sequencing approach, involving multilocus sequence typing (MLST), sas typing, spa typing and agr typing, was used to examine the molecular diversity of 118 S. aureus isolates recovered from a range of host species and to compare these data with the known diversity of human-derived isolates. MLST revealed that the commonest animal-associated MLST types were ST133, ST5, ST71, ST97, ST126 and ST151. ST133 appears to be an ungulate-animal-specific genotype, as no evidence of ST133 associating with humans has yet been found in the literature. Novel and unique sas alleles were identified in the animal-associated strains that may represent animal-associated sas alleles. However, sas typing exhibited a lower typeability than MLST for the animal strains (91.3 %). Phylogenetic analyses using neighbour-joining and maximum-parsimony trees localized ruminant-associated MLST lineages to both previously identified S. aureus subspecies aureus subgroups, thus explaining the finding of all four agr types within the ruminant-associated strains. S. aureus isolates recovered from chickens and rabbits were genotypically more similar to known human genotypes than the ruminant-associated lineages.
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http://dx.doi.org/10.1099/jmm.0.009837-0 | 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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