TY  - GEN
A1  - Memczak, Henry
A1  - Lauster, Daniel
A1  - Kar, Parimal
A1  - Di Lella, Santiago
A1  - Volkmer, Rudolf
A1  - Knecht, Volker
A1  - Herrmann, Andreas
A1  - Ehrentreich-Förster, Eva
A1  - Bier, Frank Fabian
A1  - Stöcklein, Walter F. M.
T1  - Anti-hemagglutinin antibody derived lead peptides for inhibitors of influenza virus binding
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
N2  - Antibodies against spike proteins of influenza are used as a tool for characterization of viruses and therapeutic approaches. However, development, production and quality control of antibodies is expensive and time consuming. To circumvent these difficulties, three peptides were derived from complementarity determining regions of an antibody heavy chain against influenza A spike glycoprotein. Their binding properties were studied experimentally, and by molecular dynamics simulations. Two peptide candidates showed binding to influenza A/Aichi/2/68 H3N2. One of them, termed PeB, with the highest affinity prevented binding to and infection of target cells in the micromolar region without any cytotoxic effect. PeB matches best the conserved receptor binding site of hemagglutinin. PeB bound also to other medical relevant influenza strains, such as human-pathogenic A/California/7/2009 H1N1, and avian-pathogenic A/MuteSwan/Rostock/R901/2006 H7N1. Strategies to improve the affinity and to adapt specificity are discussed and exemplified by a double amino acid substituted peptide, obtained by substitutional analysis. The peptides and their derivatives are of great potential for drug development as well as biosensing.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 536 
KW  - receptor-binding
KW  - A viruses
KW  - neutralizing antibody
KW  - avian influenza
KW  - origin
KW  - neuraminidase
KW  - invection
KW  - entry
KW  - sites
KW  - identification
Y1  - 2019
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-410872
SN  - 1866-8372
IS  - 536
ER  - 
TY  - GEN
A1  - Sperber, Hannah Sabeth
A1  - Welke, Robert-William
A1  - Petazzi, Roberto Arturo
A1  - Bergmann, Ronny
A1  - Schade, Matthias
A1  - Shai, Yechiel
A1  - Chiantia, Salvatore
A1  - Herrmann, Andreas
A1  - Schwarzer, Roland
T1  - Self-association and subcellular localization of Puumala hantavirus envelope proteins
T2  - Postprints der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe
N2  - 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.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - 648 
KW  - Sin-Nombre-Virus
KW  - nucleocapsid protein
KW  - cytoplasmic tails
KW  - electron cryotomography
KW  - autophagic clearance
KW  - glycoprotein
KW  - Gn
KW  - G1
KW  - brightness
KW  - fever
Y1  - 2019
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus4-425040
SN  - 1866-8372
IS  - 648
ER  -