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Iskalni niz: "avtor" (Marjetka Podobnik) .

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Structural basis for the multitasking nature of the potato virus Y coat protein
Andreja Kežar, Luka Kavčič, Martin Pólak, Jiři Nováček, Ion Gutiérrez-Aguirre, Magda Tušek-Žnidarič, Anna Coll Rius, Katja Stare, Kristina Gruden, Maja Ravnikar, David Pahovnik, Ema Žagar, Franci Merzel, Gregor Anderluh, Marjetka Podobnik, 2019, izvirni znanstveni članek

Povzetek: Potato virus Y (PVY) is among the most economically important plant pathogens. Using cryoelectron microscopy, we determined the near-atomic structure of PVY’s flexuous virions, revealing a previously unknown lumenal interplay between extended carboxyl-terminal regions of the coat protein units and viral RNA. RNA–coat protein interactions are crucial for the helical configuration and stability of the virion, as revealed by the unique near-atomic structure of RNA-free virus-like particles. The structures offer the first evidence for plasticity of the coat protein’s amino- and carboxyl-terminal regions. Together with mutational analysis and in planta experiments, we show their crucial role in PVY infectivity and explain the ability of the coat protein to perform multiple biological tasks. Moreover, the high modularity of PVY virus-like particles suggests their potential as a new molecular scaffold for nanobiotechnological applications.
Ključne besede: plant pathogens, potato virus Y, viral RNA
Objavljeno v DiRROS: 23.07.2024; Ogledov: 30; Prenosov: 5
.pdf Celotno besedilo (4,43 MB)
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Nanoscale transformations of amphiboles within human alveolar epithelial cells
Ruggero Vigliaturo, Maja Jamnik, Goran Dražić, Marjetka Podobnik, Magda Tušek-Žnidarič, Giancarlo Della Ventura, Günther Redhammer, Nada Žnidaršič, Simon Caserman, Reto Gieré, 2022, izvirni znanstveni članek

Povzetek: Amphibole asbestos is related to lung fibrosis and several types of lung tumors. The disease-triggering mechanisms still challenge our diagnostic capabilities and are still far from being fully understood. The literature focuses primarily on the role and formation of asbestos bodies in lung tissues, but there is a distinct lack of studies on amphibole particles that have been internalized by alveolar epithelial cells (AECs). These internalized particles may directly interact with the cell nucleus and the organelles, exerting a synergistic action with asbestos bodies (AB) from a different location. Here we document the near-atomic- to nano-scale transformations induced by, and taking place within, AECs of three distinct amphiboles (anthophyllite, grunerite, “amosite”) with different Fe-content and morphologic features. We show that: (i) an Fe-rich layer is formed on the internalized particles, (ii) particle grain boundaries are transformed abiotically by the internal chemical environment of AECs and/or by a biologically induced mineralization mechanism, (iii) the Fe-rich material produced on the particle surface does not contain large amounts of P, in stark contrast to extracellular ABs, and (iv) the iron in the Fe-rich layer is derived from the particle itself. Internalized particles and ABs follow two distinct formation mechanisms reaching different physicochemical end-states.
Ključne besede: amphiboles, human alveolar epithelial cells, asbestos, lung cancer, nanoscale investigation, acS/TEM-EDXS, dual-EELS, asbestos-related tumors
Objavljeno v DiRROS: 16.07.2024; Ogledov: 57; Prenosov: 22
.pdf Celotno besedilo (4,53 MB)
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Bacillus thuringiensis toxin Cyt2Aa forms filamentous oligomers when exposed to lipid membranes or detergents
Gašper Šolinc, Gregor Anderluh, Marjetka Podobnik, 2023, izvirni znanstveni članek

Objavljeno v DiRROS: 11.07.2023; Ogledov: 490; Prenosov: 300
.pdf Celotno besedilo (1,89 MB)
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Design of protein logic gate system operating on lipid membranes
Neža Omersa, Saša Rezelj, Matic Kisovec, Marjetka Podobnik, Gregor Anderluh, 2020, izvirni znanstveni članek

Ključne besede: pore-forming toxin, listeriolysin O, protein logic gates, lipid membrane, DARPin, pH
Objavljeno v DiRROS: 25.11.2020; Ogledov: 1705; Prenosov: 935
.pdf Celotno besedilo (4,48 MB)
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