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1.
English Teaching ; 2022.
Article in English | Scopus | ID: covidwho-1961314

ABSTRACT

Purpose: Adaptivity has long been recognized as a key aspect of teaching and shown to be particularly important for English Language Arts (ELA) teachers leading discussions about texts. Teachers' abilities to make such adjustments are especially important when facilitating discussions in digital contexts, as was made clear with the shift to virtual teaching caused by the COVID-19 pandemic. The purpose of this paper is to explore how the structure and process of teacher inquiry supported ELA teachers in enacting and cultivating adaptive repertoires for facilitating discussion in online contexts during the disruptions of the 2020–2021 school year. Design/methodology/approach: As an inquiry team comprising teacher-researchers from secondary and university-based contexts, the authors used practitioner inquiry methods in the context of a multi-year, multi-sited study involving, design-based and teacher-research methodologies. Findings: This paper shows how teachers’ engagement in digital teacher inquiry groups supported their willingness to be playful and adapt their practices in response to one another, creating conditions for powerful teacher learning through relational inquiry online. This paper identified three specific relational practices that were critical for cultivating adaptive repertories in teachers’ learning with and from each other: cultivating empathy;attuning to silences and actively listening;and decentering authority across multiple platforms and modalities. The authors discuss how teachers carried these practices to and from their digital discussions with their students and with each other, demonstrating how this recursive cycle of inquiry and practice deepened their learning, relationships and adaptive repertoires. Originality/value: The authors discuss the implications of these practices for equity-oriented and dialogic teacher learning that can transform classroom practice, illustrating the power of online teacher inquiry groups for developing ELA teachers’ adaptive expertise – something urgently important for teaching in digitally mediated contexts and through unsettled times. © 2022, Emerald Publishing Limited.

2.
Embase;
Preprint in English | EMBASE | ID: ppcovidwho-326710

ABSTRACT

Coronaviruses are a major infectious disease threat, and include the human pathogens of zoonotic origin SARS-CoV (“SARS-1”), SARS-CoV-2 (“SARS-2”) and MERS-CoV (“MERS”). Entry of coronaviruses into host cells is mediated by the viral spike (S) protein. Previously, we identified that the domain immediately downstream of the S2’ cleavage site is the bona fide FP (amino acids 798-835) for SARS-1 using ESR spectroscopy technology. We also found that the SARS-1 FP induces membrane ordering in a Ca2+ dependent fashion. In this study, we want to know which residues are involved in this Ca2+ binding, to build a topological model and to understand the role of the Ca2+. We performed a systematic mutation study on the negatively charged residues on the SARS-1 FP. While all six negatively charged residues contributes to the membrane ordering activity of the FP to some extent, D812 is the most important residue. We provided a topological model of how the FP binds Ca2+ ions: both FP1 and FP2 bind one Ca2+ ion, and there are two binding sites in FP1 and three in FP2. We also found that the corresponding residue D830 in the SARS-2 FP plays a similar critical role. ITC experiments show that the binding energies between the FP and Ca2+ as well as between the FP and membranes also decreases for all mutants. The binding of Ca2+, the folding of FP and the ordering activity correlated very well across the mutants, suggesting that the function of the Ca2+ is to help to folding of FP in membranes to enhance its activity. Using a novel pseudotyped virus particle (PP)-liposome methodology, we monitored the membrane ordering induced by the FPs in the whole S proteins in its trimer form in real time. We found that the SARS-1 and SARS-2 PPs also induce membrane ordering as the separate FPs do, and the mutations of the negatively charged residues also greatly reduce the membrane ordering activity. However, the difference in kinetic between the PP and FP indicates a possible role of FP trimerization. This finding could lead to therapeutic solutions that either target the FP-calcium interaction or block the Ca2+ channel to combat the ongoing COVID-19 pandemic.

3.
PubMed; 2021.
Preprint in English | PubMed | ID: ppcovidwho-296776

ABSTRACT

Coronaviruses are a major infectious disease threat, and include the human pathogens of zoonotic origin SARS-CoV ("SARS-1"), SARS-CoV-2 ("SARS-2") and MERS-CoV ("MERS"). Entry of coronaviruses into host cells is mediated by the viral spike (S) protein. Previously, we identified that the domain immediately downstream of the S2' cleavage site is the bona fide FP (amino acids 798-835) for SARS-1 using ESR spectroscopy technology. We also found that the SARS-1 FP induces membrane ordering in a Ca 2+ dependent fashion. In this study, we want to know which residues are involved in this Ca 2+ binding, to build a topological model and to understand the role of the Ca2+. We performed a systematic mutation study on the negatively charged residues on the SARS-1 FP. While all six negatively charged residues contributes to the membrane ordering activity of the FP to some extent, D812 is the most important residue. We provided a topological model of how the FP binds Ca 2+ ions: both FP1 and FP2 bind one Ca 2+ ion, and there are two binding sites in FP1 and three in FP2. We also found that the corresponding residue D830 in the SARS-2 FP plays a similar critical role. ITC experiments show that the binding energies between the FP and Ca 2+ as well as between the FP and membranes also decreases for all mutants. The binding of Ca 2+ , the folding of FP and the ordering activity correlated very well across the mutants, suggesting that the function of the Ca 2+ is to help to folding of FP in membranes to enhance its activity. Using a novel pseudotyped virus particle (PP)-liposome methodology, we monitored the membrane ordering induced by the FPs in the whole S proteins in its trimer form in real time. We found that the SARS-1 and SARS-2 PPs also induce membrane ordering as the separate FPs do, and the mutations of the negatively charged residues also greatly reduce the membrane ordering activity. However, the difference in kinetic between the PP and FP indicates a possible role of FP trimerization. This finding could lead to therapeutic solutions that either target the FP-calcium interaction or block the Ca 2+ channel to combat the ongoing COVID-19 pandemic.

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