Nosocomial transmission of multi-drug-resistant organisms in Ukrainian hospitals: results of a multi-centre study (2019-2021).

BACKGROUND: The increasing emergence and spread of multi-drug-resistant organisms (MDROs) in hospitals is a public health problem and continues to challenge infection control and hospital epidemiology practice worldwide. AIM: The aim of this study was to characterize the epidemiology of transmission of MDROs via healthcare workers (HCWs) and the environment in the hospital wards/patient rooms. METHODS: A multi-centre prospective observational study was conducted in 17 hospitals in Ukraine. Species identification was performed with standard microbial methods. ß-Lactamase genes were investigated by polymerase chain reaction. Pulsed-field gel electrophoresis (PFGE) was used to determine the genetic similarity between isolates. FINDINGS: Among 51,656 isolates, 19.5% were MDROs. The proportions of MDROs among isolates from patients with healthcare-associated infections, environmental surfaces and HCWs (hands, gown/gloves) were 29.2%, 16.3% and 24.2%, respectively. In 51.9% of the tested isolates, identical MDROs were found in clinical isolates, environmental samples and HCWs' hands. Meticillin resistance was found in 32.4% of Staphylococcus aureus (MRSA) isolates, and vancomycin resistance was found in 28.9% of enterococci (VRE). Resistance to third-generation cephalosporins was detected in 48.4% of Enterobacterales, and carbapenem resistance in 19.1%. Overall, 37.4% of MDROs had broad-spectrum ß-lactamase genes, including extended-spectrum ß-lactamase (35.8%), OXA-type (29.7%), AmpC-type (25.1%), KPC-type (25.7%) and metallo-ß-lactamases, including IMP-type (5.7%), VIM-type (31.7%) and NDM-1 (21.3%). CONCLUSIONS: In Ukrainian hospitals the prevalence of healthcare-associated infections caused by MDROs continues to increase, while infection control gaps in healthcare settings facilitate their transmission between patients.

Identification of heat shock factor binding protein in Plasmodium falciparum.

BACKGROUND: Heat shock factor binding protein (HSBP) was originally discovered in a yeast two-hybrid screen as an interacting partner of heat shock factor (HSF). It appears to be conserved in all eukaryotes studied so far, with yeast being the only exception. Cell biological analysis of HSBP in mammals suggests its role as a negative regulator of heat shock response as it appears to interact with HSF only during the recovery phase following exposure to heat stress. While the identification of HSF in the malaria parasite is still eluding biologists, this study for the first time, reports the presence of a homologue of HSBP in Plasmodium falciparum. METHODS: PfHSBP was cloned and purified as his-tag fusion protein. CD (Circular dichroism) spectroscopy was performed to predict the secondary structure. Immunoblots and immunofluorescence approaches were used to study expression and localization of HSBP in P. falciparum. Cellular fractionation was performed to examine subcellular distribution of PfHSBP. Immunoprecipitation was carried out to identify HSBP interacting partner in P. falciparum. RESULTS: PfHSBP is a conserved protein with a high helical content and has a propensity to form homo-oligomers. PfHSBP was cloned, expressed and purified. The in vivo protein expression profile shows maximal expression in trophozoites. The protein was found to exist in oligomeric form as trimer and hexamer. PfHSBP is predominantly localized in the parasite cytosol, however, upon heat shock, it translocates to the nucleus. This study also reports the interaction of PfHSBP with PfHSP70-1 in the cytoplasm of the parasite. CONCLUSIONS: This study emphasizes the structural and biochemical conservation of PfHSBP with its mammalian counterpart and highlights its potential role in regulation of heat shock response in the malaria parasite. Analysis of HSBP may be an important step towards identification of the transcription factor regulating the heat shock response in P. falciparum.