Emergency nurses' attitudes, perceptions about personal protective equipment and willingness to care for COVID-19 patients: A descriptive, cross-sectional study.

AIMS: This study investigated emergency nurses' attitudes and perceptions about personal protective equipment and their association with the willingness to care for COVID-19 patients. BACKGROUND: Emergency nurses are at increased risk for COVID-19 infection as frontline workers and must wear personal protective equipment while attending suspected and confirmed COVID-19 patients. METHODS: In September 2021, 188 nurses in four emergency departments completed online questionnaires. RESULTS: Multivariable logistic regression demonstrated that as perceptions of COVID-19 infection risk increased by 1 point, 26% of nurses were willing to care of COVID-19 patients. The willingness to care for COVID-19 patients increased in their attitudes by 1.16 point and perceptions by 1.08 points about PPE. CONCLUSIONS: Perceptions of the risk of infection exposure and confidence in safety of personal protective equipment are associated with nurses' willingness to care for COVID-19 patients. IMPLICATIONS FOR NURSING MANAGEMENT: Nurse managers need to assess nurses' needs for safety and provide a supportive climate to mitigate their concerns regarding infection risk and encourage nurses' willingness to care for patients. Nurse managers should provide precise guidelines on correct personal protective equipment use. Repetitive training on personal protective equipment should be provided to encourage nurses' adaptation to its use.

Concanavalin A: coordination diversity to xenobiotic metal ions and biological consequences.

The binding ability of lectins has gained attention owing to the carbohydrate-specific interactions of these proteins. Such interactions can be applied to diverse fields of biotechnology, including the detection, isolation, and concentration of biological target molecules. The physiological aspects of the lectin concanavalin A (ConA) have been intensively studied through structural and functional investigations. X-ray crystallography studies have proven that ConA has two ß-sheets and a short α-helix and that it exists in the form of a metalloprotein containing Mn2+ and Ca2+. These heterometals are coordinated with side chains located in a metal-coordinated domain (MCD), and they affect the structural environment in the carbohydrate-binding domain (CBD), which interacts with carbohydrates through hydrogen bonds. Recent studies have shown that ConA can regulate biophysical interactions with glycoproteins in virus envelopes because it specifically interacts with diverse polysaccharides through its CBD (Tyr, Asn, Asp, and Arg residues positioned next to the MCD). Owing to their protein-protein interaction abilities, ConA can form diverse self-assembled complexes including monomers, dimers, trimers, and tetramers, thus affording unique results in different applications. In this regard, herein, we present a review of the structural modifications in ConA through metal-ion coordination and their effect on complex formation. In recent approaches, ConA has been applied for viral protein detection, on the basis of the interactions of ConA. These aspects indicate that lectins should be thoroughly investigated with respect to their biophysical interactions, for avoiding unexpected changes in their interaction abilities.

Concanavalin A targeting N-linked glycans in spike proteins influence viral interactions.

Lectins, which exhibit viral-interaction abilities, have garnered attention in the current pandemic era as potential neutralizing agents and vaccine candidates. Viral invasion through envelope proteins is modulated by N-linked glycosylation in the spike (S) protein. This study demonstrates the biophysical aspects between lectins and high-mannose and -galactose N-glycans to provide insights into binding events.

MMOD-induced structural changes of hydroxylase in soluble methane monooxygenase.

Soluble methane monooxygenase in methanotrophs converts methane to methanol under ambient conditions. The maximum catalytic activity of hydroxylase (MMOH) is achieved through the interplay of its regulatory protein (MMOB) and reductase. An additional auxiliary protein, MMOD, functions as an inhibitor of MMOH; however, its inhibitory mechanism remains unknown. Here, we report the crystal structure of the MMOH-MMOD complex from Methylosinus sporium strain 5 (2.6 Å). Its structure illustrates that MMOD associates with the canyon region of MMOH where MMOB binds. Although MMOD and MMOB recognize the same binding site, each binding component triggers different conformational changes toward MMOH, which then respectively lead to the inhibition and activation of MMOH. Particularly, MMOD binding perturbs the di-iron geometry by inducing two major MMOH conformational changes, i.e., MMOH ß subunit disorganization and subsequent His147 dissociation with Fe1 coordination. Furthermore, 1,6-hexanediol, a mimic of the products of sMMO, reveals the substrate access route.