In fighting the spread of COVID-19, the drastic measures undertaken by governments worldwide demonstrate a trade-off between public health and fundamental democratic principles. Yet this behaviour is not consistent across democracies, which motivates this paper to examine why some democracies were willing to constrain individual freedoms and concentrate power more than others during the pandemic's first wave. Creating two indices to measure the degree to which COVID-19 policies interfere with these democratic principles in 34 European countries, the analyses show that the large variation cannot be solely explained by pandemic-related factors. It is argued that the strong protection of democratic principles already established in 'normal' times makes governments more reluctant to opt for restrictive policies. By highlighting how differences in policy responses are attributed to provisions guaranteeing individual liberties, this paper contributes to a better understanding of how democracies handle the democratic dilemma in times of crises. KEYWORDS COVID-19; public health policies; democracy; fundamental rights; state of emergency; public health crisis The COVID-19 pandemic came fast and hit hard. After the virus spread in China in early 2020, it did not take long until Italy, as the first European country, had to deal with a strong rise in daily SARS-CoV-2 infections. When the situation got out of control, Italy's Prime Minister Giuseppe Conte proclaimed a nation-wide lockdown. Most European CONTACT Sarah Engler

We describe a procedure for the determination of the roots of functions satisfying secondorder ordinary differential equations, including the classical special functions. The scheme is based on a combination of the Pri.ifer transform with the classical Taylor series method for the solution of ordinary differential equations, and requires 0(1) operations for the determination of each root. When the functions in question are classical orthogonal polynomials (Legendre, Hermite, etc.), the techniques presented here also provide tools for the evaluation of the weights for the associated Gaussian quadratures. The performance of the scheme for several classical special functions (prolate spheroidal wave functions, Bessel functions, and Legendre, Hermite, and Laguerre polynomials) is illustrated with numerical examples.

We have identified thioredoxins (Trx) of Malassezia sympodialis, a yeast involved in the pathogenesis of atopic eczema, and of Aspergillus fumigatus, a fungus involved in pulmonary complications, as novel IgE-binding proteins. We show that these Trx, including the human enzyme, represent cross-reactive structures recognized by serum IgE from individuals sensitized to M. sympodialis Trx. Moreover, all three proteins were able to elicit immediate-type allergic skin reactions in sensitized individuals, indicating a humoral immune response based on molecular mimicry. To analyze structural elements involved in these reactions, the three-dimensional structure of M. sympodialis Trx (Mala s 13) has been determined at 1.4-Å resolution by x-ray diffraction analysis. The structure was solved by molecular replacement and refined to a crystallographic R factor of 14.0% and a free R factor of 16.8% and shows the typical Trx fold. Mala s 13 shares 45% sequence identity with human Trx and superposition of the solved Mala s 13 structure with those of human Trx reveals a high similarity with a root mean square deviation of 1.11 Å for all Cα atoms. In a detailed analysis of the molecular surface in combination with sequence alignment, we identified conserved solvent-exposed amino acids scattered over the surface in both structures which cluster to patches, thus forming putative conformational B cell epitopes potentially involved in IgE-mediated cross- and autoreactivity.

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Cyclophilins constitute a family of proteins involved in many essential cellular functions. They have also been identified as a panallergen family able to elicit IgE-mediated hypersensitivity reactions. Moreover, it has been shown that human cyclophilins are recognized by serum IgE from patients sensitized to environmental cyclophilins. IgE-mediated autoreactivity to self-antigens that have similarity to environmental allergens is often observed in atopic disorders. Therefore comparison of the crystal structure of human proteins with similarity to allergens should allow the identification of structural similarities to rationally explain autoreactivity. A new cyclophilin from Aspergillus fumigatus (Asp f 27) has been cloned, expressed and showed to exhibit cross-reactivity in vitro and in vivo. The three-dimensional structure of cyclophilin from the yeast Malassezia sympodialis (Mala s 6) has been determined at 1.5 A (1 A=0.1 nm) by X-ray diffraction. Crystals belong to space group P4(1)2(1)2 with unit cell dimensions of a=b=71.99 A and c=106.18 A. The structure was solved by molecular replacement using the structure of human cyclophilin A as the search model. The refined structure includes all 162 amino acids of Mala s 6, an active-site-bound Ala-Pro dipeptide and 173 water molecules, with a crystallographic R- and free R-factor of 14.3% and 14.9% respectively. The overall structure consists of an eight-stranded antiparallel beta-barrel and two alpha-helices covering the top and bottom of the barrel, typical for cyclophilins. We identified conserved solvent-exposed residues in the fungal and human structures that are potentially involved in the IgE-mediated cross-reactivity.