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1.
Article in English | MEDLINE | ID: mdl-33915733

ABSTRACT

The coronavirus disease 2019 (COVID-19) pandemic results in a profound physical and mental burden on healthcare professionals. This study aims to evaluate burnout status and mood disorder of healthcare workers during this period. An online questionnaire was voluntarily answered by eligible adult employees in a COVID-19 specialized medical center. The major analysis included the burnout status and mood disorder. Factors related to more severe mood disorder were also identified. A total of 2029 participants completed the questionnaire. There were 901 (44.4%) and 923 (45.5%) participants with moderate to severe personal and work-related burnout status, respectively. Nurses working in the emergency room (ER), intensive care unit (ICU)/isolation wards, and general wards, as well as those with patient contact, had significantly higher scores for personal burnout, work-related burnout, and mood disorder. This investigation identified 271 participants (13.35%) with moderate to severe mood disorder linked to higher personal/work-related burnout scores and a more advanced burnout status. Univariate analysis revealed that nurses working in the ER and ICU/isolation wards were associated with moderate to severe mood disorder risk factors. Multivariate analysis demonstrated that working in the ER (OR, 2.81; 95% CI, 1.14-6.90) was the only independent risk factor. More rest, perquisites, and an adequate supply of personal protection equipment were the most desired assistance from the hospital. Compared with the non-pandemic period (2019), employees working during the COVID-19 pandemic (2020) have higher burnout scores and percentages of severe burnout. In conclusion, this study suggests that the COVID-19 pandemic has had an adverse impact on healthcare professionals. Adequate measures should be adopted as early as possible to support the healthcare system.


Subject(s)
Burnout, Professional , COVID-19 , Adult , Burnout, Professional/epidemiology , Delivery of Health Care , Health Personnel , Humans , Mood Disorders , Pandemics , SARS-CoV-2
2.
Proc Natl Acad Sci U S A ; 112(21): 6613-8, 2015 May 26.
Article in English | MEDLINE | ID: mdl-25964325

ABSTRACT

Spo0J (stage 0 sporulation protein J, a member of the ParB superfamily) is an essential component of the ParABS (partition system of ParA, ParB, and parS)-related bacterial chromosome segregation system. ParB (partition protein B) and its regulatory protein, ParA, act cooperatively through parS (partition S) DNA to facilitate chromosome segregation. ParB binds to chromosomal DNA at specific parS sites as well as the neighboring nonspecific DNA sites. Various ParB molecules can associate together and spread along the chromosomal DNA. ParB oligomer and parS DNA interact together to form a high-order nucleoprotein that is required for the loading of the structural maintenance of chromosomes proteins onto the chromosome for chromosomal DNA condensation. In this report, we characterized the binding of parS and Spo0J from Helicobacter pylori (HpSpo0J) and solved the crystal structure of the C-terminal domain truncated protein (Ct-HpSpo0J)-parS complex. Ct-HpSpo0J folds into an elongated structure that includes a flexible N-terminal domain for protein-protein interaction and a conserved DNA-binding domain for parS binding. Two Ct-HpSpo0J molecules bind with one parS. Ct-HpSpo0J interacts vertically and horizontally with its neighbors through the N-terminal domain to form an oligomer. These adjacent and transverse interactions are accomplished via a highly conserved arginine patch: RRLR. These interactions might be needed for molecular assembly of a high-order nucleoprotein complex and for ParB spreading. A structural model for ParB spreading and chromosomal DNA condensation that lead to chromosome segregation is proposed.


Subject(s)
Bacterial Proteins/chemistry , Amino Acid Sequence , Bacterial Proteins/genetics , Bacterial Proteins/metabolism , Base Sequence , Chromosome Segregation/genetics , Chromosome Segregation/physiology , Crystallography, X-Ray , DNA, Bacterial/chemistry , DNA, Bacterial/genetics , DNA, Bacterial/metabolism , Helicobacter pylori/genetics , Helicobacter pylori/metabolism , Models, Molecular , Molecular Sequence Data , Protein Binding , Protein Interaction Domains and Motifs , Protein Structure, Quaternary , Scattering, Small Angle , Sequence Homology, Amino Acid , Spores, Bacterial/genetics , Spores, Bacterial/metabolism , X-Ray Diffraction
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