daniehat

• Meuskens, Ina; Kristiansen, Per Eugen; Bardiaux, Benjamin; Koynarev, Vladimir Rosenov; Hatlem, Daniel & Prydz, Kristian [Show all 9 contributors for this article] (2023). A poly-proline II helix in YadA from Yersinia enterocolitica serotype O:9 facilitates heparin binding through electrostatic interactions. The FEBS Journal. ISSN 1742-464X. 291(4), p. 761–777. doi: 10.1111/febs.17001. Full text in Research Archive
• Hatlem, Daniel; Christensen, Mikkel; Broeker, Nina; Kristiansen, Per Eugen; Lund, Reidar & Barbirz, Stefanie [Show all 7 contributors for this article] (2023). A trimeric coiled-coil motif binds bacterial lipopolysaccharides with picomolar affinity. Frontiers in Cellular and Infection Microbiology. ISSN 2235-2988. 13. doi: 10.3389/fcimb.2023.1125482. Full text in Research Archive
• Hatlem, Daniel; Trunk, Thomas; Linke, Dirk & Leo, Jack Christopher (2020). Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins. In Leitao, JH (Eds.), Microbial Virulence Factors. MDPI. ISSN 978-3-03936-946-1. p. 371–400. doi: 10.3390/ijms20092129. Full text in Research Archive
• Hatlem, Daniel; Trunk, Thomas; Linke, Dirk & Leo, Jack Christopher (2019). Catching a SPY: Using the SpyCatcher-SpyTag and Related Systems for Labeling and Localizing Bacterial Proteins. International Journal of Molecular Sciences. ISSN 1661-6596. 20(9), p. 1–19. doi: 10.3390/ijms20092129. Full text in Research Archive Show summary

  The SpyCatcher-SpyTag system was developed seven years ago as a method for protein ligation. It is based on a modified domain from a Streptococcus pyogenes surface protein (SpyCatcher), which recognizes a cognate 13-amino-acid peptide (SpyTag). Upon recognition, the two form a covalent isopeptide bond between the side chains of a lysine in SpyCatcher and an aspartate in SpyTag. This technology has been used, among other applications, to create covalently stabilized multi-protein complexes, for modular vaccine production, and to label proteins (e.g., for microscopy). The SpyTag system is versatile as the tag is a short, unfolded peptide that can be genetically fused to exposed positions in target proteins; similarly, SpyCatcher can be fused to reporter proteins such as GFP, and to epitope or purification tags. Additionally, an orthogonal system called SnoopTag-SnoopCatcher has been developed from an S. pneumoniae pilin that can be combined with SpyCatcher-SpyTag to produce protein fusions with multiple components. Furthermore, tripartite applications have been produced from both systems allowing the fusion of two peptides by a separate, catalytically active protein unit, SpyLigase or SnoopLigase. Here, we review the current state of the SpyCatcher-SpyTag and related technologies, with a particular emphasis on their use in vaccine development and in determining outer membrane protein localization and topology of surface proteins in bacteria.

• Chauhan, Nandini; Hatlem, Daniel; Rydmark, Marcella Orwick; Schneider, Kenneth; Flötenmeyer, Matthias & Van Rossum, Barth-J [Show all 8 contributors for this article] (2019). Insights into the autotransport process of a trimeric autotransporter, Yersinia Adhesin A (YadA). Molecular Microbiology. ISSN 0950-382X. 111(3), p. 844–862. doi: 10.1111/mmi.14195. Full text in Research Archive
• Hatlem, Daniel; Heggelund, Julie Elisabeth; Burschowsky, Daniel; Krengel, Ute & Kristiansen, Per Eugen (2017). 1H, 13C, 15N backbone assignment of the human heat-labile enterotoxin B-pentamer and chemical shift mapping of neolactotetraose binding. Biomolecular NMR Assignments. ISSN 1874-2718. 11(1), p. 99–104. doi: 10.1007/s12104-017-9728-9. Full text in Research Archive

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• Meuskens, Ina; Kristiansen, Per Eugen; Bardiaux, Benjamin; Koynarev, Vladimir Rosenov; Hatlem, Daniel & Prydz, Kristian [Show all 9 contributors for this article] (2023). Strain variations in a bacterial adhesin lead to different binding partners in the pathogen Yersinia enterocolitica .
• Hatlem, Daniel; Linke, Dirk Bernd Kurt & Andersen, Elisabeth K. (2022). Forskerprosjekt på antibiotika og blodforgiftning. [Internet]. Website Oslo Cancer Cluster.
• Røsjø, Bjarne; Orwick-Rydmark, Marcella; Linke, Dirk; Leo, Jack Christopher & Hatlem, Daniel (2019). Ny antibiotika-idé: Vil hindre bakteriene i å feste seg. [Internet]. TITAN.NO.
• Hatlem, Daniel; Chauhan, Nandini; Orwick-Rydmark, Marcella; Schneider, Kenneth; Flötenmeyer, Matthias & Van Rossum, Barth-J [Show all 8 contributors for this article] (2019). Insights into the autotransport of a trimeric autotransporter.
• Chauhan, Nandini; Hatlem, Daniel; Orwick-Rydmark, Marcella; Schneider, Kenneth; Linke, Dirk & Leo, Jack Christopher (2019). Using the SpyCatcher-SpyTag technology for topology mapping of outer membrane proteins in Gram-negative bacteria.
• Hatlem, Daniel; Chauhan, Nandini; Rydmark, Marcella Orwick; Schneider, Kenneth; Floetenmeyer, Matthias & Leo, Jack Christopher [Show all 7 contributors for this article] (2018). Insights into the autotransporter process of a trimeric autotransporter, Yersinia Adhesin A (YadA).
• Hatlem, Daniel & Linke, Dirk (2018). Insights into the autotransporter process of a trimeric autotransporter, Yersinia Adhesin A (YadA).
• Hatlem, Daniel; Leo, Jack Christopher; Saragliadis, Athanasios; Krengel, Ute & Linke, Dirk (2017). Bacterial adhesion: Characterization of trimeric autotransporter binding.
• Hatlem, Daniel; Kempf, Volkhard A.J.; Krengel, Ute & Linke, Dirk (2016). Bacterial adhesion: Characterization of trimeric autotransporter binding.
• Hatlem, Daniel; Saragliadis, Athanasios; Leo, Jack Christopher; Shahid, Shakeel; van Rossum, Barth & Linke, Dirk (2015). TAAs: fibrous adhesins on the bacterial cell surface.
• Hatlem, Daniel (2015). Studying lipopolysaccharide binding to the heat-labile enterotoxin.
• Hatlem, Daniel; Linke, Dirk & Krengel, Ute (2022). Probing the role of lipopolysaccharides in Gram-negative protein secretion and biogenesis. Universitetet i Oslo.
• Hatlem, Daniel (2018). Bacterial Protein Export (Conference Report). NBS.
• Hatlem, Daniel (2015). Sequential Assignment of the Heat-labile Enterotoxin Backbone for Lipopolysaccharide Interaction Studies. Universitetet i Oslo.

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