Invasive beta-haemolytic streptococcal infections, Finland, 2006 to 2020: increase in Lancefield group C/G infections.

BackgroundInvasive infections with beta-haemolytic streptococci of Lancefield groups A (iGAS), B (iGBS) and C/G (iGCGS) are a major cause of morbidity and mortality worldwide.AimWe studied incidence trends of invasive beta-haemolytic streptococcal infections in Finland, focusing on iGCGS.MethodsWe conducted a retrospective register-based study.

Typhimurium outbreak associated with frozen tomato cubes at a restaurant in western Finland, January to February 2021.

Several individuals reported gastrointestinal symptoms following meals consumed in late January 2021 at a restaurant in western Finland. We conducted a retrospective cohort study and defined a case as a person who ate at the lunch restaurant between 27 and 29 January 2021 and had stomach pain, vomiting or diarrhoea and/or a laboratory-confirmed Typhimurium infection within 2 weeks after the exposure. We collected faecal and food samples for microbiological analysis.

Chitinase Expression in Listeria monocytogenes Is Influenced by , Which Encodes an Internalin-Like Protein.

The chitinolytic system of thus far comprises two chitinases, ChiA and ChiB, and a lytic polysaccharide monooxygenase, Lmo2467. The role of the system in the bacterium appears to be pleiotropic, as besides mediating the hydrolysis of chitin, the second most ubiquitous carbohydrate in nature, the chitinases have been deemed important for the colonization of unicellular molds, as well as mammalian hosts. To identify additional components of the chitinolytic system, we screened a transposon mutant library for mutants exhibiting impaired chitin hydrolysis.

Chitinase expression in Listeria monocytogenes is positively regulated by the Agr system.

The food-borne pathogen Listeria monocytogenes encodes two chitinases, ChiA and ChiB, which allow the bacterium to hydrolyze chitin, the second most abundant polysaccharide in nature. Intriguingly, despite the absence of chitin in human and mammalian hosts, both of the chitinases have been deemed important for infection, through a mechanism that, at least in the case of ChiA, involves modulation of host immune responses. In this study, we show that the expression of the two chitinases is subject to regulation by the listerial agr system, a homologue of the agr quorum-sensing system of Staphylococcus aureus, that has so far been implicated in virulence and biofilm formation.

Bacillus subtilis BY-kinase PtkA controls enzyme activity and localization of its protein substrates.

Bacillus subtilis BY-kinase PtkA was previously shown to phosphorylate, and thereby regulate the activity of two classes of protein substrates: UDP-glucose dehydrogenases and single-stranded DNA-binding proteins. Our recent phosphoproteome study identified nine new tyrosine-phosphorylated proteins in B. subtilis.