Iodamoeba is a single-celled intestinal parasite, which is common in humans in certain parts of the world, and also in pigs. For the first time, we provide DNA-based evidence of goat, dromedary, fallow deer, and donkey as hosts of Iodamoeba and show that Iodamoeba-specific nucleotide sequences from these four hosts do not appear to overlap with those of humans, unlike those from pigs. We moreover show that similar strains of Iodamoeba can be found in Madagascar, Western Sahara, and Ecuador and that intra-sample diversity is typically extensive across even small fragments of DNA in both human and non-human hosts.
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http://dx.doi.org/10.1016/j.protis.2024.126058 | DOI Listing |
Appl Environ Microbiol
December 2024
Microbiological Sciences Department, North Dakota State University, Fargo, North Dakota, USA.
is an important bacterial pathogen implicated in infections such as mastitis, metritis, pneumonia, and liver abscesses in both domestic and wild animals, as well as endocarditis and prosthetic joint infections in humans. Understanding the genomic and metabolic features that enable to colonize different anatomical sites within a host and its inter-kingdom transmission and survival is important for the effective control of this pathogen. We employed whole-genome sequencing, phenotype microarrays, and antimicrobial susceptibility testing to identify genomic, metabolic and phenotypic features, and antimicrobial resistance (AMR) genes in recovered from different livestock, companion, and wildlife animals.
View Article and Find Full Text PDFJ Chem Phys
January 2025
Dipartimento di Fisica, Università degli Studi di Napoli Federico II, and INFN Napoli, Complesso Universitario di Monte Sant'Angelo, 80126 Naples, Italy.
In the last years, it has been proved that some viruses are able to re-structure chromatin organization and alter the epigenomic landscape of the host genome. In addition, they are able to affect the physical mechanisms shaping chromatin 3D structure, with a consequent impact on gene activity. Here, we investigate with polymer physics genome re-organization of the host genome upon SARS-CoV-2 viral infection and how it can impact structural variability within the population of single-cell chromatin configurations.
View Article and Find Full Text PDFJ Biol Chem
December 2024
Helmholtz Institute for Pharmaceutical Research Saarland (HIPS), Helmholtz Centre for Infection Research, D-66123 Saarbrücken, Germany; Deutsches Zentrum für Infektionsforschung (DZIF), Standort Hannover-Braunschweig; Department of Chemistry, PharmaScienceHub (PSH), Saarland University, D-66123 Saarbrücken, Germany.
Bacteria frequently employ carbohydrate-binding proteins, so-called lectins, to colonize and persist in a host. Thus, bacterial lectins are attractive targets for the development of new antiinfectives. To find new potential targets for antiinfectives against pathogenic bacteria, we searched for homologs of Pseudomonas aeruginosa lectins and identified homologs of LecA in Enterobacter species.
View Article and Find Full Text PDFPLoS One
December 2024
Laboratorio de Microbiología Experimental y Aplicada y Microbiología de Aguas (LAMEXA-LAMA), Universidad de Panamá, Panamá, Panamá.
The Enterobacter cloacae complex, a prominent bacterium responsible worldwide for most bloodstream infections in the hospital environment, has shown broad-spectrum antibiotic resistance, including carbapenems. Therefore, bacteriophages have again attracted the attention of the science and medical community as an alternative to control Multidrug resistant bacteria. In this study, water samples from Río Abajo River, in Panama City, Panama, were collected, for phage isolation, purification, characterization and propagation against the E.
View Article and Find Full Text PDFNat Commun
December 2024
Laboratory of Retrovirology, The Rockefeller University, New York, NY, 10065, USA.
ZAP is an antiviral protein that binds to and depletes viral RNA, which is often distinguished from vertebrate host RNA by its elevated CpG content. Two ZAP cofactors, TRIM25 and KHNYN, have activities that are poorly understood. Here, we show that functional interactions between ZAP, TRIM25 and KHNYN involve multiple domains of each protein, and that the ability of TRIM25 to multimerize via its RING domain augments ZAP activity and specificity.
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