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Bolz, H. J.

Publications and source records attributed to Bolz, H. J..

4 recordsLinked to original sources

Deep-intronic variants in USH2A: the importance of model selection in variant interpretation and pathogenicity assessment

Interpreting splice-altering USH2A variants is challenging when these result in the alteration of splicing in only a fraction of transcripts. We investigated two deep-intronic USH2A variants from a single case, the inherited variant c.5573-834A>G and the de novo variant c.11047+345A>G, using a minigene splice assay and transcript analysis in patient-derived photoreceptor precursor cells and nasal epithelial cells. The minigene assay revealed the inclusion of a pseudoexon in the presence of the c.11047+345A>G variant, but did not reproduce previously reported aberrant splicing for c.5573-834A>G. In patient-derived cells, c.5573-834A>G resulted in the inclusion of a pseudoexon in part of the transcripts, whereas c.11047+345A>G did not result in detectable levels of aberrantly spliced transcripts. To assess the impact of residual wildtype transcripts on retinal function, we used the previously developed humanized ush2aPE40+M1 knock-in zebrafish model which allows the modeling of the impact of mixed wildtype and pseudoexon-containing ush2a transcripts. This model demonstrated that detectable levels of usherin expression are maintained even when only a fraction of wildtype transcripts lacking pseudoexon inclusion remain. Collectively, these findings advocate for a more nuanced classification of partially splice-altering USH2A variants. The mere presence of alternative transcripts should not be considered sufficient evidence for pathogenicity. Within this framework, data on the c.5573-834A>G variant do not support a (likely) pathogenic classification, and findings related to the c.11047+345A>G variant are consistent with a likely benign classification.

genetics↗

High-speed whole-genome sequencing of a Whippet: Rapid chromosome-level assembly and annotation of an extremely fast dog's genome

BackgroundThe time required for sequencing and de novo assembly of genomes is highly dependent on the interaction between laboratory work, sequencing capacity, and the bioinformatics workflow. As a result, genome projects are often not only limited by financial, computational and sequencing platform resources, but also delayed by second party sequencing service providers. By bringing together academic biodiversity institutes and a medical diagnostics company with extensive sequencing capabilities and know-how, we aimed at generating a high-quality mammalian de novo genome in the shortest possible time period. Therefore, we streamlined all processes involved and chose a very fast dog as a model: The Whippet. FindingsWe present the first chromosome-level genome assembly of the Whippet. We used PacBio long-read HiFi sequencing and reference-guided scaffolding to generate a high-quality genome assembly. The final assembly has a contig N50 of 55 Mbp and a scaffold N50 of 65.7 Mbp. The total assembly length is 2.47 Gbp, of which 2.43 Gpb were scaffolded into 39 chromosome-length scaffolds. In addition, we used available mammalian genomes and transcriptome data to annotate the genome assembly. The annotation resulted in 28,383 transcripts resembling a total of 90.9% complete BUSCO genes and identified a repeat content of 36.5%. ConclusionsSequencing, assembling, and scaffolding the chromosome-level genome of the Whippet took less than a week and adds a high-quality reference genome to the list of domestic dog breeds sequenced to date.

genomics↗

Tectonic Complex Impedes Diffusion through the Ciliary Transition Zone to Ensure Proper Sorting of Membrane Proteins

The primary cilium is a signaling organelle with a unique membrane composition maintained by a diffusional barrier residing at the transition zone. Many transition zone proteins, such as the tectonic complex, are linked to preserving ciliary composition; however, whether these proteins regulate active transport or physically impede membrane diffusion remains unknown. To understand tectonics role, we generated a photoreceptor specific Tctn1 knockout mouse. Loss of Tctn1 resulted in an absence of the entire tectonic complex yet had minimal effects on transition zone structure. Interestingly, we found that protein composition of the photoreceptor cilium was disrupted as non-resident membrane proteins accumulated in the cilium over time, ultimately resulting in photoreceptor degeneration. We further show that membrane proteins moved faster through the transition zone illustrating that the tectonic complex acts as a physical barrier to slow diffusion of membrane proteins so they can be properly sorted by ciliary transport carriers.

cell biology↗

Loss of CEP162 function at the primary cilium delays ciliogenesis and causes retinal ciliopathy in humans

Defects in primary or motile cilia result in a variety of human pathologies, and retinal degeneration is frequently associated with these so-called ciliopathies. We show that homozygosity for a truncating variant in CEP162, a centrosome and microtubule-associated protein required for transition zone (TZ) assembly during ciliogenesis and neuronal differentiation in the retina, causes late-onset retinitis pigmentosa in 2 unrelated families. The mutant CEP162-E646R*5 protein is expressed and properly localized to the mitotic spindle but missing from the basal body in primary and photoreceptor cilia. This impairs recruitment of TZ components to the basal body and corresponds to complete loss of CEP162 function at the ciliary compartment, reflected by delayed formation of dysmorphic cilia. In contrast, rescue of increased cell death in the developing mouse retina after shRNA knockdown of Cep162 by expression of CEP162-E646R*5 indicates that the mutant retains its role for retinal neurogenesis. Human retinal degeneration thus results from specific loss of ciliary CEP162 function. Graphical abstract O_FIG O_LINKSMALLFIG WIDTH=134 HEIGHT=200 SRC="FIGDIR/small/469779v3_ufig1.gif" ALT="Figure 1"> View larger version (53K): org.highwire.dtl.DTLVardef@593dccorg.highwire.dtl.DTLVardef@e84d7forg.highwire.dtl.DTLVardef@137ce56org.highwire.dtl.DTLVardef@cba1f7_HPS_FORMAT_FIGEXP M_FIG C_FIG

genetics↗