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Jukka Hytönen

Researcher at Turku University Hospital

Publications -  62
Citations -  1463

Jukka Hytönen is an academic researcher from Turku University Hospital. The author has contributed to research in topics: Borrelia burgdorferi & Borrelia. The author has an hindex of 21, co-authored 57 publications receiving 1241 citations. Previous affiliations of Jukka Hytönen include University of Turku.

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Fluid- or Surface-Phase Human Salivary Scavenger Protein gp340 Exposes Different Bacterial Recognition Properties

TL;DR: Results suggest that salivary gp340 recognizes different bacterial receptors according to whether gp340 is present in the fluid phase or surface bound, and this phase-associated differential recognition by gp340 of streptococcal species of different levels of virulence and diverse origins may mediate alternative host responses to commensal or pathogenic bacterial phenotypes.
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The SpeB virulence factor of Streptococcus pyogenes, a multifunctional secreted and cell surface molecule with strepadhesin, laminin-binding and cysteine protease activity.

TL;DR: This work identifies strepadhesin, a novel glycoprotein‐binding activity in Streptococcus pyogenes, which is regulated by Mga, a regulator of streptococcal virulence factors, and finds that it is carried by SpeB, strethococcal pyrogenic exotoxin with cysteine protease activity.
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CXCL13 and neopterin concentrations in cerebrospinal fluid of patients with Lyme neuroborreliosis and other diseases that cause neuroinflammation.

TL;DR: CXCL13 outperformed neopterin and appears to be an excellent biomarker in differentiating LNB from viral CNS infections and from other neuroinflammatory conditions.
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Crowdsourcing-based nationwide tick collection reveals the distribution of Ixodes ricinus and I. persulcatus and associated pathogens in Finland

TL;DR: A national crowdsourcing-based tick collection campaign was organized in 2015 with the objective of producing novel data on tick distribution and tick-borne pathogens in Finland and demonstrates the overwhelming power of citizen science in accomplishing a collection effort that would have been impossible with the scientific community alone.
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Streptococcus pyogenes glycoprotein-binding strepadhesin activity is mediated by a surface-associated carbohydrate-degrading enzyme, pullulanase.

TL;DR: High strepadhesin activity in an S. pyogenes strain (NZ131rgg) lacking SpeB expression is carried by a surface-bound pullulanase, which combines glycoprotein-binding and carbohydrate-degrading activities in the same molecule.