@article{WelkeSperberBergmannetal.2022,
  author    = {Welke, Robert-William and Sperber, Hannah Sabeth and Bergmann, Ronny and Koikkarah, Amit and Menke, Laura and Sieben, Christian and Kr{\"u}ger, Detlev H. and Chiantia, Salvatore and Herrmann, Andreas and Schwarzer, Roland},
  title     = {Characterization of hantavirus N protein intracellular dynamics and localization},
  series = {Viruses},
  volume    = {14},
  journal   = {Viruses},
  number    = {3},
  publisher = {MDPI},
  address   = {Basel},
  issn      = {1999-4915},
  doi       = {10.3390/v14030457},
  pages     = {14},
  year      = {2022},
  abstract  = {Hantaviruses are enveloped viruses that possess a tri-segmented, negative-sense RNA genome. The viral S-segment encodes the multifunctional nucleocapsid protein (N), which is involved in genome packaging, intracellular protein transport, immunoregulation, and several other crucial processes during hantavirus infection. In this study, we generated fluorescently tagged N protein constructs derived from Puumalavirus (PUUV), the dominant hantavirus species in Central, Northern, and Eastern Europe. We comprehensively characterized this protein in the rodent cell line CHO-K1, monitoring the dynamics of N protein complex formation and investigating co-localization with host proteins as well as the viral glycoproteins Gc and Gn. We observed formation of large, fibrillar PUUV N protein aggregates, rapidly coalescing from early punctate and spike-like assemblies. Moreover, we found significant spatial correlation of N with vimentin, actin, and P-bodies but not with microtubules. N constructs also co-localized with Gn and Gc albeit not as strongly as the glycoproteins associated with each other. Finally, we assessed oligomerization of N constructs, observing efficient and concentration-dependent multimerization, with complexes comprising more than 10 individual proteins.},
  language  = {en}
}
@article{WawrzinekWessigMoellnitzetal.2012,
  author    = {Wawrzinek, Robert and Wessig, Pablo and M{\"o}llnitz, Kristian and Nikolaus, Joerg and Schwarzer, Roland and M{\"u}ller, Peter and Herrmann, Andreas},
  title     = {DBD dyes as fluorescent probes for sensing lipophilic environments},
  series = {Bioorganic \& medicinal chemistry letters : a Tetrahedron publication for rapid dissemination of preliminary communications on all aspects of bioorganic chemistry, medicinal chemistry and related disciplines},
  volume    = {22},
  journal   = {Bioorganic \& medicinal chemistry letters : a Tetrahedron publication for rapid dissemination of preliminary communications on all aspects of bioorganic chemistry, medicinal chemistry and related disciplines},
  number    = {17},
  publisher = {Elsevier},
  address   = {Oxford},
  issn      = {0960-894X},
  doi       = {10.1016/j.bmcl.2012.07.056},
  pages     = {5367 -- 5371},
  year      = {2012},
  abstract  = {Small fluorescent organic molecules based on [1,3]dioxolo[4,5-f][1,3]benzodioxole (DBD) could be used as probes for lipophillic microenvironments in aqueous solutions by indicating the critical micelles concentration of detergents and staining cell organelles. Their fluorescence lifetime decreases drastically by the amount of water in their direct environment. Therefore they are potential probes for fluorescence lifetime imaging microscopy (FLIM).},
  language  = {en}
}
@article{SperberWelkePetazzietal.2019,
  author    = {Sperber, Hannah Sabeth and Welke, Robert-William and Petazzi, Roberto Arturo and Bergmann, Ronny and Schade, Matthias and Shai, Yechiel and Chiantia, Salvatore and Herrmann, Andreas and Schwarzer, Roland},
  title     = {Self-association and subcellular localization of Puumala hantavirus envelope proteins},
  series = {Scientific reports},
  volume    = {9},
  journal   = {Scientific reports},
  publisher = {Nature Publ. Group},
  address   = {London},
  issn      = {2045-2322},
  doi       = {10.1038/s41598-018-36879-y},
  pages     = {15},
  year      = {2019},
  abstract  = {Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number\&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential.},
  language  = {en}
}
@misc{SperberWelkePetazzietal.2019,
  author    = {Sperber, Hannah Sabeth and Welke, Robert-William and Petazzi, Roberto Arturo and Bergmann, Ronny and Schade, Matthias and Shai, Yechiel and Chiantia, Salvatore and Herrmann, Andreas and Schwarzer, Roland},
  title     = {Self-association and subcellular localization of Puumala hantavirus envelope proteins},
  series = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  journal   = {Postprints der Universit{\"a}t Potsdam : Mathematisch-Naturwissenschaftliche Reihe},
  number    = {648},
  issn      = {1866-8372},
  doi       = {10.25932/publishup-42504},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus4-425040},
  pages     = {15},
  year      = {2019},
  abstract  = {Hantavirus assembly and budding are governed by the surface glycoproteins Gn and Gc. In this study, we investigated the glycoproteins of Puumala, the most abundant Hantavirus species in Europe, using fluorescently labeled wild-type constructs and cytoplasmic tail (CT) mutants. We analyzed their intracellular distribution, co-localization and oligomerization, applying comprehensive live, single-cell fluorescence techniques, including confocal microscopy, imaging flow cytometry, anisotropy imaging and Number\&Brightness analysis. We demonstrate that Gc is significantly enriched in the Golgi apparatus in absence of other viral components, while Gn is mainly restricted to the endoplasmic reticulum (ER). Importantly, upon co-expression both glycoproteins were found in the Golgi apparatus. Furthermore, we show that an intact CT of Gc is necessary for efficient Golgi localization, while the CT of Gn influences protein stability. Finally, we found that Gn assembles into higher-order homo-oligomers, mainly dimers and tetramers, in the ER while Gc was present as mixture of monomers and dimers within the Golgi apparatus. Our findings suggest that PUUV Gc is the driving factor of the targeting of Gc and Gn to the Golgi region, while Gn possesses a significantly stronger self-association potential.},
  language  = {en}
}
@inproceedings{HaralampievMertensSchwarzeretal.2015,
  author    = {Haralampiev, Ivan and Mertens, Monique and Schwarzer, Roland and Herrmann, Andreas and Volkmer, Rudolf and Wessig, Pablo and M{\"u}ller, Peter},
  title     = {A palmitic acid functionalized with a maleimide group is used to recruit SH-containing peptides to lipid and biological membranes},
  series = {The FEBS journal},
  volume    = {282},
  booktitle = {The FEBS journal},
  publisher = {Wiley-Blackwell},
  address   = {Hoboken},
  issn      = {1742-464X},
  pages     = {204 -- 204},
  year      = {2015},
  language  = {en}
}
@article{HaralampievMertensSchwarzeretal.2015,
  author    = {Haralampiev, Ivan and Mertens, Monique and Schwarzer, Roland and Herrmann, Andreas and Volkmer, Rudolf and Wessig, Pablo and Mueller, Peter},
  title     = {Recruitment of SH-Containing peptides to lipid and biological membranes through the use of a palmitic acid functionalized with a Maleimide Group},
  series = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  volume    = {54},
  journal   = {Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition},
  number    = {1},
  publisher = {Wiley-VCH},
  address   = {Weinheim},
  issn      = {1433-7851},
  doi       = {10.1002/anie.201408089},
  pages     = {323 -- 326},
  year      = {2015},
  abstract  = {This study presents a novel and easily applicable approach to recruit sulfhydryl-containing biomolecules to membranes by using a palmitic acid which is functionalized with a maleimide group. Notably, this strategy can also be employed with preformed (biological) membranes. The applicability of the assay is demonstrated by characterizing the binding of a Rhodamine-labeled peptide to lipid and cellular membranes using methods of fluorescence spectroscopy, lifetime measurement, and microscopy. Our approach offers new possibilities for preparing biologically active liposomes and manipulating living cells.},
  language  = {en}
}