TY  - JOUR
A1  - Whisnant, Adam W.
A1  - Jürges, Christopher S.
A1  - Hennig, Thomas
A1  - Wyler, Emanuel
A1  - Prusty, Bhupesh
A1  - Rutkowski, Andrzej J.
A1  - L'hernault, Anne
A1  - Djakovic, Lara
A1  - Göbel, Margarete
A1  - Döring, Kristina
A1  - Menegatti, Jennifer
A1  - Antrobus, Robin
A1  - Matheson, Nicholas J.
A1  - Künzig, Florian W. H.
A1  - Mastrobuoni, Guido
A1  - Bielow, Chris
A1  - Kempa, Stefan
A1  - Liang, Chunguang
A1  - Dandekar, Thomas
A1  - Zimmer, Ralf
A1  - Landthaler, Markus
A1  - Grässer, Friedrich
A1  - Lehner, Paul J.
A1  - Friedel, Caroline C.
A1  - Erhard, Florian
A1  - Dölken, Lars
T1  - Integrative functional genomics decodes herpes simplex virus 1
JF  - Nature Communications
N2  - The predicted 80 open reading frames (ORFs) of herpes simplex virus 1 (HSV-1) have been intensively studied for decades. Here, we unravel the complete viral transcriptome and translatome during lytic infection with base-pair resolution by computational integration of multi-omics data. We identify a total of 201 transcripts and 284 ORFs including all known and 46 novel large ORFs. This includes a so far unknown ORF in the locus deleted in the FDA-approved oncolytic virus Imlygic. Multiple transcript isoforms expressed from individual gene loci explain translation of the vast majority of ORFs as well as N-terminal extensions (NTEs) and truncations. We show that NTEs with non-canonical start codons govern the subcellular protein localization and packaging of key viral regulators and structural proteins. We extend the current nomenclature to include all viral gene products and provide a genome browser that visualizes all the obtained data from whole genome to single-nucleotide resolution. Here, using computational integration of multi-omics data, the authors provide a detailed transcriptome and translatome of herpes simplex virus 1 (HSV-1), including previously unidentified ORFs and N-terminal extensions. The study also provides a HSV-1 genome browser and should be a valuable resource for further research.
KW  - infected-cell protein
KW  - messenger RNA
KW  - binding protein
KW  - type 1
KW  - identification
KW  - ICP27
KW  - translation
KW  - expression
KW  - sequence
KW  - domain
Y1  - 2020
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-229884
VL  - 11
ER  - 
TY  - JOUR
A1  - Scholz, Nicole
A1  - Gehring, Jennifer
A1  - Guan, Chonglin
A1  - Ljaschenko, Dmitrij
A1  - Fischer, Robin
A1  - Lakshmanan, Vetrivel
A1  - Kittel, Robert J.
A1  - Langenhan, Tobias
T1  - The adhesion GPCR Latrophilin/CIRL shapes mechanosensation
JF  - Cell Reports
N2  - G-protein-coupled receptors (GPCRs) are typically regarded as chemosensors that control cellular states in response to soluble extracellular cues. However, the modality of stimuli recognized through adhesion GPCR (aGPCR), the second largest class of the GPCR superfamily, is unresolved. Our study characterizes the Drosophila aGPCR Latrophilin/dCirl, a prototype member of this enigmatic receptor class. We show that dCirl shapes the perception of tactile, proprioceptive, and auditory stimuli through chordotonal neurons, the principal mechanosensors of Drosophila. dCirl sensitizes these neurons for the detection of mechanical stimulation by amplifying their input-output function. Our results indicate that aGPCR may generally process and modulate the perception of mechanical signals, linking these important stimuli to the sensory canon of the GPCR superfamily.
KW  - \(\alpha\)-latrotoxin
KW  - chordotonal organs
KW  - Johnstons organ
KW  - ligand CD55
KW  - hearing
KW  - binding
KW  - shear stress
KW  - protein-coupled receptors
KW  - drosophila larvae
KW  - domain
Y1  - 2015
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:bvb:20-opus-148626
VL  - 11
ER  -