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5. Polymers as candidates for broad-spectrum antivirals--in vitro inhibition of Zika virus with sodium polyanethole sulfonate.

Author

Obłoza, Magdalena, Milewska, Aleksandra, Botwina, Paweł, Górecka, Magdalena, Szczepański, Artur, Medaj, Aneta, Bonarek, Piotr, Szczubiałka, Krzysztof, Pyrć, Krzysztof, and Nowakowska, Maria

Subjects
ZIKA virus, POLYMERS, ISOTHERMAL titration calorimetry, BLOOD proteins, SODIUM
Abstract

Zika virus (ZIKV), belonging to the family of flaviviruses, is an emerging mosquito-borne pathogen causing microcephaly and other congenital abnormalities in newborns as well as various neurologic pathologies in adults. The climate change and the lifestyle of current societies, involving global mobility, result in a rapid broadening of ZIKV geographic distribution. There are no vaccines or drugs available to protect against or cure the diseases caused by that virus. Our in vitro studies have demonstrated that sodium polyanethole sulfonate (PASNa), a degradable polymer used in various biomedical applications, acts as an efficient ZIKV inhibitor, both in animal and human cells. The mechanistic studies indicated that PASNa bound to the ZIKV particles thus hindering their attachment to the host cells and also interfered in the late steps of viral replication. PASNa is characterized by very low cytotoxicity and its antiviral activity can be achieved at a concentration much lower than that at which its anticoagulant activity has to be considered. Isothermal titration calorimetry (ITC) studies have shown that the interaction of PASNa with human serum albumin (HSA), the most abundant blood protein, is the endothermic, entropydriven process resulting in the formation of stoichiometric (1:1) PASNa-HSA complexes with a hydrodynamic diameter of 8.8 ± 0.8 nm and zeta potential (ζ) equal to -21.3 mV. The analysis of CD spectra indicated that PASNa did not significantly affect the HSA secondary structure on binding to that protein. [ABSTRACT FROM AUTHOR]

Published
2024
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22. Crystal structures of OrfX1, OrfX2, and the OrfX1–OrfX3 complex from the orfX gene cluster of botulinum neurotoxin E1

Author

Gao, Linfeng, Lam, Kwok‐ho, Liu, Shun, Przykopanski, Adina, Lübke, Johanna, Qi, Ruifeng, Krüger, Maren, Nowakowska, Maria B., Selby, Katja, Douillard, François P., Dorner, Martin B., Perry, Kay, Lindström, Miia, Dorner, Brigitte G., Rummel, Andreas, Jin, Rongsheng, and Food Hygiene and Environmental Health

Subjects
Botulinum neurotoxin, OrfX2, OrfX3, orfX gene cluster, Bacterial toxin, 413 Veterinary science, OrfX1
Abstract

Botulinum neurotoxins (BoNTs) are among the most lethal toxins known to humans, comprising seven established serotypes termed BoNT/A–G encoded in two types of gene clusters (ha and orfX) in BoNT-producing clostridia. The ha cluster encodes four non-toxic neurotoxin-associated proteins (NAPs) that assemble with BoNTs to protect and enhance their oral toxicity. However, the structure and function of the orfX-type NAPs remain largely unknown. Here, we report the crystal structures for OrfX1, OrfX2, and an OrfX1–OrfX3 complex, which are encoded in the orfX cluster of a BoNT/E1-producing Clostridium botulinum strain associated with human foodborne botulism. These structures lay the foundation for future studies on the potential roles of OrfX proteins in oral intoxication and pathogenesis of BoNTs.

Published
2023

38. Novel polymeric inhibitors of HCoV-NL63

Author

Milewska, Aleksandra, Ciejka, Justyna, Kaminski, Kamil, Karewicz, Anna, Bielska, Dorota, Zeglen, Slawomir, Karolak, Wojciech, Nowakowska, Maria, Potempa, Jan, Bosch, Berend Jan, Pyrc, Krzysztof, and Szczubialka, Krzysztof

Published
2013
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