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Katrien Vandersteegen

Researcher at Katholieke Universiteit Leuven

Publications -  9
Citations -  444

Katrien Vandersteegen is an academic researcher from Katholieke Universiteit Leuven. The author has contributed to research in topics: Bacteriophage & Phage therapy. The author has an hindex of 8, co-authored 9 publications receiving 392 citations.

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Feasibility of spray drying bacteriophages into respirable powders to combat pulmonary bacterial infections

TL;DR: Even though the parameters were not optimized for spray drying all phages, it was demonstrated that spray drying phages with this industrial relevant and scalable set up was possible and the resulting powders had desirable size ranges for pulmonary delivery of phage with dry powder inhalers (DPIs).
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Microbiological and Molecular Assessment of Bacteriophage ISP for the Control of Staphylococcus aureus

TL;DR: The microbiological and molecular characterization of ISP supports its application in a phage cocktail for therapeutic purposes and was proven to be stable in relevant in vivo conditions and subcutaneous as well as nasal and oral ISP administration to rabbits appeared to cause no adverse effects.
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Romulus and Remus, Two Phage Isolates Representing a Distinct Clade within the Twortlikevirus Genus, Display Suitable Properties for Phage Therapy Applications

TL;DR: Romulus and Remus can be proposed as isolates of a new species within the Twortlikevirus genus, with double-stranded DNA genomes of 131,333 bp and 134,643 bp, with unique distribution of group I introns compared to that in other staphylococcal myoviruses.
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CIM® monolithic anion-exchange chromatography as a useful alternative to CsCl gradient purification of bacteriophage particles

TL;DR: It is concluded that anion-exchange chromatography with monoliths is a valid alternative to the more traditional CsCl purification, has upscaling advantages, but it requires more extensive optimization.
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Listeria phage A511, a model for the contractile tail machineries of SPO1-related bacteriophages

TL;DR: The identification of Gp108 as the host receptor‐binding protein of the broad host‐range, virulent Listeria phage A511 is reported, which reveals key elements in the infection process of large phages infecting Gram‐positive bacteria and generates insights into the complex adsorption process of phages A511 to its bacterial host.