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Article ; Online: Comprehensive analytical and clinical evaluation of a RNA extraction-free saliva-based molecular assay for SARS-CoV-2.

Schoeber, Joost P H / Schlaghecke, Juliëtte M / Meuwissen, Britt M J / van Heertum, Mara / van den Brule, Adriaan J C / Loonen, Anne J M

PloS one

2022 Volume 17, Issue 5, Page(s) e0268082

Abstract: Standard SARS-CoV-2 testing protocols using nasopharyngeal/throat (NP/T) swabs are invasive and require trained medical staff for reliable sampling. In addition, it has been shown that PCR is more sensitive as compared to antigen-based tests. Here we ... ...

Abstract	Standard SARS-CoV-2 testing protocols using nasopharyngeal/throat (NP/T) swabs are invasive and require trained medical staff for reliable sampling. In addition, it has been shown that PCR is more sensitive as compared to antigen-based tests. Here we describe the analytical and clinical evaluation of our in-house RNA extraction-free saliva-based molecular assay for the detection of SARS-CoV-2. Analytical sensitivity of the test was equal to the sensitivity obtained in other Dutch diagnostic laboratories that process NP/T swabs. In this study, 955 individuals participated and provided NP/T swabs for routine molecular analysis (with RNA extraction) and saliva for comparison. Our RT-qPCR resulted in a sensitivity of 82,86% and a specificity of 98,94% compared to the gold standard. A false-negative ratio of 1,9% was found. The SARS-CoV-2 detection workflow described here enables easy, economical, and reliable saliva processing, useful for repeated testing of individuals.
MeSH term(s)	COVID-19/diagnosis ; COVID-19 Testing ; Humans ; Nasopharynx ; RNA ; RNA, Viral/genetics ; SARS-CoV-2/genetics ; Saliva ; Sensitivity and Specificity ; Specimen Handling/methods
Chemical Substances	RNA, Viral ; RNA (63231-63-0)
Language	English
Publishing date	2022-05-05
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2267670-3
ISSN	1932-6203 ; 1932-6203
ISSN (online)	1932-6203
ISSN	1932-6203
DOI	10.1371/journal.pone.0268082
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article: Glow-in-the-Dark Infectious Disease Diagnostics Using CRISPR-Cas9-Based Split Luciferase Complementation.

van der Veer, Harmen J / van Aalen, Eva A / Michielsen, Claire M S / Hanckmann, Eva T L / Deckers, Jeroen / van Borren, Marcel M G J / Flipse, Jacky / Loonen, Anne J M / Schoeber, Joost P H / Merkx, Maarten

ACS central science

2023 Volume 9, Issue 4, Page(s) 657–667

Abstract: Nucleic acid detection methods based on CRISPR and isothermal amplification techniques show great potential for point-of-care diagnostic applications. However, most current methods rely on fluorescent or lateral flow assay readout, requiring external ... ...

Abstract	Nucleic acid detection methods based on CRISPR and isothermal amplification techniques show great potential for point-of-care diagnostic applications. However, most current methods rely on fluorescent or lateral flow assay readout, requiring external excitation or postamplification reaction transfer. Here, we developed a bioluminescent nucleic acid sensor (LUNAS) platform in which target dsDNA is sequence-specifically detected by a pair of dCas9-based probes mediating split NanoLuc luciferase complementation. LUNAS is easily integrated with recombinase polymerase amplification (RPA), providing attomolar sensitivity in a rapid one-pot assay. A calibrator luciferase is included for a robust ratiometric readout, enabling real-time monitoring of the RPA reaction using a simple digital camera. We designed an RT-RPA-LUNAS assay that allows SARS-CoV-2 RNA detection without the need for cumbersome RNA isolation and demonstrated its diagnostic performance for COVID-19 patient nasopharyngeal swab samples. Detection of SARS-CoV-2 from samples with viral RNA loads of ∼200 cp/μL was achieved within ∼20 min, showing that RPA-LUNAS is attractive for point-of-care infectious disease testing.
Language	English
Publishing date	2023-03-15
Publishing country	United States
Document type	Journal Article
ISSN	2374-7943
ISSN	2374-7943
DOI	10.1021/acscentsci.2c01467
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Article ; Online: Comprehensive analytical and clinical evaluation of a RNA extraction-free saliva-based molecular assay for SARS-CoV-2.

Joost P H Schoeber / Juliëtte M Schlaghecke / Britt M J Meuwissen / Mara van Heertum / Adriaan J C van den Brule / Anne J M Loonen

PLoS ONE, Vol 17, Iss 5, p e

2022 Volume 0268082

Abstract	Standard SARS-CoV-2 testing protocols using nasopharyngeal/throat (NP/T) swabs are invasive and require trained medical staff for reliable sampling. In addition, it has been shown that PCR is more sensitive as compared to antigen-based tests. Here we describe the analytical and clinical evaluation of our in-house RNA extraction-free saliva-based molecular assay for the detection of SARS-CoV-2. Analytical sensitivity of the test was equal to the sensitivity obtained in other Dutch diagnostic laboratories that process NP/T swabs. In this study, 955 individuals participated and provided NP/T swabs for routine molecular analysis (with RNA extraction) and saliva for comparison. Our RT-qPCR resulted in a sensitivity of 82,86% and a specificity of 98,94% compared to the gold standard. A false-negative ratio of 1,9% was found. The SARS-CoV-2 detection workflow described here enables easy, economical, and reliable saliva processing, useful for repeated testing of individuals.
Keywords	Medicine ; R ; Science ; Q
Language	English
Publishing date	2022-01-01T00:00:00Z
Publisher	Public Library of Science (PLoS)
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: Fast bioluminescent nucleic acid detection using one-pot isothermal amplification and dCas9-based split luciferase complementation

van der Veer, Harm J / van Aalen, Eva A / Michielsen, Claire M.S. / Hanckmann, Eva T.L. / Deckers, Jeroen / van Borren, Marcel M.G.J. / Flipse, Jacky / Loonen, Anne J.M. / Schoeber, Joost P.H. / Merkx, Maarten

bioRxiv

Abstract: Nucleic acid detection methods based on isothermal amplification techniques show great potential for point-of-care diagnostic applications. However, most current methods rely on fluorescent or lateral flow assay readout, requiring external excitation or ... ...

Abstract	Nucleic acid detection methods based on isothermal amplification techniques show great potential for point-of-care diagnostic applications. However, most current methods rely on fluorescent or lateral flow assay readout, requiring external excitation or post-amplification reaction transfer. Here, we developed a bioluminescent nucleic acid sensor (LUNAS) platform in which target dsDNA is sequence-specifically detected by a pair of dCas9-based probes mediating split NanoLuc luciferase complementation. Whereas LUNAS itself features a detection limit of ~1 pM for dsDNA targets, the LUNAS platform is easily integrated with recombinase polymerase amplification (RPA), providing attomolar sensitivity in a single-pot assay. We designed a one-pot RT-RPA-LUNAS assay for detecting SARS-CoV-2 RNA without the need for RNA isolation and demonstrated the diagnostic performance for COVID-19 patient nasopharyngeal swab samples using a digital camera to record the ratiometric signal. Detection of SARS-CoV-2 from samples with viral RNA loads of ~200 cp/microL was achieved within ~20 minutes, showing that RPA-LUNAS is attractive for point-of-care diagnostic applications.
Keywords	covid19
Language	English
Publishing date	2022-09-15
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2022.09.12.507659
Database	COVID19

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Article ; Online: Cystinosis: practical tools for diagnosis and treatment.

Wilmer, Martijn J / Schoeber, Joost P / van den Heuvel, Lambertus P / Levtchenko, Elena N

Pediatric nephrology (Berlin, Germany)

2010 Volume 26, Issue 2, Page(s) 205–215

Abstract: Cystinosis is the major cause of inherited Fanconi syndrome, and should be suspected in young children with failure to thrive and signs of renal proximal tubular damage. The diagnosis can be missed in infants, because not all signs of renal Fanconi ... ...

Abstract	Cystinosis is the major cause of inherited Fanconi syndrome, and should be suspected in young children with failure to thrive and signs of renal proximal tubular damage. The diagnosis can be missed in infants, because not all signs of renal Fanconi syndrome are present during the first months of life. In older patients cystinosis can mimic idiopathic nephrotic syndrome due to focal and segmental glomerulosclerosis. Measuring elevated white blood cell cystine content is the corner stone for the diagnosis. The diagnosis is confirmed by molecular analysis of the cystinosin gene. Corneal cystine crystals are invariably present in all patients with cystinosis after the age of 1 year. Treatment with the cystine depleting drug cysteamine should be initiated as soon as possible and continued lifelong to prolong renal function survival and protect extra-renal organs. This educational feature provides practical tools for the diagnosis and treatment of cystinosis.
MeSH term(s)	Cysteamine/therapeutic use ; Cystinosis/diagnosis ; Cystinosis/drug therapy ; Diagnosis, Differential ; Humans ; Kidney/pathology
Chemical Substances	Cysteamine (5UX2SD1KE2)
Language	English
Publishing date	2010-08-24
Publishing country	Germany
Document type	Journal Article ; Review
ZDB-ID	631932-4
ISSN	1432-198X ; 0931-041X
ISSN (online)	1432-198X
ISSN	0931-041X
DOI	10.1007/s00467-010-1627-6
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Article: Conditional fast expression and function of multimeric TRPV5 channels using Shield-1.

Schoeber, Joost P H / van de Graaf, Stan F J / Lee, Kyu Pil / Wittgen, Hanneke G M / Hoenderop, Joost G J / Bindels, René J M

American journal of physiology. Renal physiology

2009 Volume 296, Issue 1, Page(s) F204–11

Abstract: A recently described novel controllable method to regulate protein expression is based on a mutated FK506-binding protein-12 (mtFKBP) that is unstable and rapidly degraded in mammalian cells. This instability can be conferred to other proteins directly ... ...

Abstract	A recently described novel controllable method to regulate protein expression is based on a mutated FK506-binding protein-12 (mtFKBP) that is unstable and rapidly degraded in mammalian cells. This instability can be conferred to other proteins directly fused to mtFKBP. Binding of a synthetic cell-permeant ligand (Shield-1) to mtFKBP reverses the instability, allowing conditional expression of mtFKBP-fused proteins. We adapted this strategy to study multimeric plasma membrane proteins using the ion channel TRPV5 as model protein. mtFKBP-TRPV5 forms functional ion channels and its expression can be controlled in a time- and dose-dependent fashion using Shield-1. Moreover, in the presence of Shield-1, mtFKBP-TRPV5 formed heteromultimeric channels with untagged TRPV5, which were codegraded upon washout of Shield-1, providing a strategy to study multimeric plasma membrane protein complexes without the need to destabilize all individual subunits.
MeSH term(s)	Calcium Channels/genetics ; Calcium Channels/metabolism ; Cell Line ; Cell Membrane/metabolism ; Gene Expression Regulation/physiology ; Humans ; Kidney/cytology ; Kidney/embryology ; Kidney/metabolism ; Ligands ; Protein Engineering/methods ; Protein Multimerization ; Protein Structure, Tertiary ; Small Molecule Libraries/metabolism ; TRPV Cation Channels/genetics ; TRPV Cation Channels/metabolism ; Tacrolimus Binding Protein 1A/metabolism
Chemical Substances	Calcium Channels ; Ligands ; Small Molecule Libraries ; TRPV Cation Channels ; TRPV5 protein, human ; TRPV6 protein, human ; Tacrolimus Binding Protein 1A (EC 5.2.1.-)
Language	English
Publishing date	2009-01
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	603837-2
ISSN	1522-1466 ; 1931-857X ; 0363-6127
ISSN (online)	1522-1466
ISSN	1931-857X ; 0363-6127
DOI	10.1152/ajprenal.90473.2008
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Article ; Online: Activation of the Ca2+-sensing receptor stimulates the activity of the epithelial Ca2+ channel TRPV5.

Topala, Catalin N / Schoeber, Joost P H / Searchfield, Lydia E / Riccardi, Daniela / Hoenderop, Joost G J / Bindels, René J M

Cell calcium

2009 Volume 45, Issue 4, Page(s) 331–339

Abstract: The extracellular Ca(2+)-sensing receptor (CaR) is a key-player in plasma Ca(2+) homeostasis. It is essentially expressed in the parathyroid glands and along the kidney nephron. The distal convoluted tubules (DCT) and connecting tubules (CNT) in the ... ...

Abstract	The extracellular Ca(2+)-sensing receptor (CaR) is a key-player in plasma Ca(2+) homeostasis. It is essentially expressed in the parathyroid glands and along the kidney nephron. The distal convoluted tubules (DCT) and connecting tubules (CNT) in the kidney are involved in active Ca(2+) reabsorption, but the function of the CaR has remained unclear in these segments. Here, the Ca(2+)-selective Transient Receptor Potential Vanilloid-subtype 5 channel (TRPV5) determines active Ca(2+) reabsorption by forming the apical entry gate. In this study we show that the CaR and TRPV5 co-localize at the luminal membrane of DCT/CNT. Furthermore, by patch-clamp and Fura-2-ratiometric measurements we demonstrate that activation of the CaR leads to elevated TRPV5-mediated currents and increases intracellular Ca(2+) concentrations in cells co-expressing TRPV5 and CaR. Activation of CaR initiated a signaling cascade that activated phorbol-12-myristate-13-acetate (PMA)-insensitive protein kinase C (PKC) isoforms. Importantly, mutation of two putative PKC phosphorylation sites, S299 and S654, in TRPV5 prevented the stimulatory effect of CaR activation on channel activity, as did a dominant negative CaR construct, CaR(R185Q). Interestingly, the activity of TRPV6, TRPV5' closest homologue, was not affected by the activated CaR. We conclude that activation of the CaR stimulates TRPV5-mediated Ca(2+) influx via a PMA-insensitive PKC isoform pathway.
MeSH term(s)	Animals ; Cell Membrane/drug effects ; Cell Membrane/metabolism ; Cell Polarity/drug effects ; Epithelial Cells/cytology ; Epithelial Cells/drug effects ; Epithelial Cells/enzymology ; Epithelial Cells/metabolism ; Humans ; Ion Channel Gating ; Isoenzymes/metabolism ; Kidney Tubules, Distal/cytology ; Kidney Tubules, Distal/drug effects ; Kidney Tubules, Distal/metabolism ; Mice ; Mutant Proteins/metabolism ; Phosphorylation/drug effects ; Protein Kinase C/metabolism ; Protein Transport/drug effects ; Rabbits ; Receptors, Calcium-Sensing/metabolism ; Signal Transduction/drug effects ; TRPV Cation Channels/metabolism ; Tetradecanoylphorbol Acetate/pharmacology
Chemical Substances	Isoenzymes ; Mutant Proteins ; Receptors, Calcium-Sensing ; TRPV Cation Channels ; TRPV5 protein, human ; Protein Kinase C (EC 2.7.11.13) ; Tetradecanoylphorbol Acetate (NI40JAQ945)
Language	English
Publishing date	2009-04
Publishing country	Netherlands
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	757687-0
ISSN	1532-1991 ; 0143-4160
ISSN (online)	1532-1991
ISSN	0143-4160
DOI	10.1016/j.ceca.2008.12.003
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Article: Role of p-glycoprotein expression and function in cystinotic renal proximal tubular cells.

Peeters, Karen / Wilmer, Martijn J / Schoeber, Joost P / Reijnders, Dorien / Heuvel, Lambertus P van den / Masereeuw, Rosalinde / Levtchenko, Elena

Pharmaceutics

2011 Volume 3, Issue 4, Page(s) 782–792

Abstract: P-glycoprotein (P-gp) is an ATP-dependent transporter localized at the apical membrane ... waste products and xenobiotics, such as drugs, into urine. Studies in mice deficient in P-gp showed generalized ... depleting drug cysteamine. Here, we investigated whether the proximal tubular efflux transporter P-gp is ...

Abstract	P-glycoprotein (P-gp) is an ATP-dependent transporter localized at the apical membrane of the kidney proximal tubules, which plays a role in the efflux of cationic and amphipathic endogenous waste products and xenobiotics, such as drugs, into urine. Studies in mice deficient in P-gp showed generalized proximal tubular dysfunction similar to the phenotype of patients with cystinosis, an autosomal recessive disorder caused by mutations in the lysosomal cystine transporter cystinosin. Renal disease in cystinosis is characterized by generalized dysfunction of the apical proximal tubular influx transporters (so-called renal Fanconi syndrome) developing during infancy and gradually progressing towards end-stage renal disease before the 10th birthday in the majority of patients that are not treated with the cystine-depleting drug cysteamine. Here, we investigated whether the proximal tubular efflux transporter P-gp is affected in cystinosis and whether this might contribute to the development of renal Fanconi syndrome. We used conditionally immortalized (ci) proximal tubular epithelial cells (ciPTEC) derived from cystinotic patients and healthy volunteers. P-gp-mediated transport was measured by using the P-gp substrate calcein-AM in the presence and absence of the P-gp-inhibitor PSC833. P-gp activity was normal in cystinotic cells as compared to controls. Additionally, the effect of cysteamine on P-gp transport activity and phosphate uptake was determined; demonstrating increased P-gp activity in cystinotic cells, and further decrease of proximal tubular phosphate uptake. This observation is compatible with the persistence of renal Fanconi syndrome in vivo under cysteamine therapy. In summary, P-gp expression and activity are normal in cystinotic ciPTEC, indicating that P-gp dysfunction is not involved in the pathogenesis of cystinosis.
Language	English
Publishing date	2011-10-27
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2527217-2
ISSN	1999-4923
ISSN	1999-4923
DOI	10.3390/pharmaceutics3040782
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Article ; Online: Role of P-Glycoprotein Expression and Function in Cystinotic Renal Proximal Tubular Cells

Joost P. Schoeber / Elena Levtchenko / Lambertus P. van den Heuvel / Dorien Reijnders / Martijn J. Wilmer / Karen Peeters / Rosalinde Masereeuw

Pharmaceutics, Vol 3, Iss 4, Pp 782-

2011 Volume 792

Abstract	P-glycoprotein (P-gp) is an ATP-dependent transporter localized at the apical membrane of the kidney proximal tubules, which plays a role in the efflux of cationic and amphipathic endogenous waste products and xenobiotics, such as drugs, into urine. Studies in mice deficient in P-gp showed generalized proximal tubular dysfunction similar to the phenotype of patients with cystinosis, an autosomal recessive disorder caused by mutations in the lysosomal cystine transporter cystinosin. Renal disease in cystinosis is characterized by generalized dysfunction of the apical proximal tubular influx transporters (so-called renal Fanconi syndrome) developing during infancy and gradually progressing towards end-stage renal disease before the 10th birthday in the majority of patients that are not treated with the cystine-depleting drug cysteamine. Here, we investigated whether the proximal tubular efflux transporter P-gp is affected in cystinosis and whether this might contribute to the development of renal Fanconi syndrome. We used conditionally immortalized (ci) proximal tubular epithelial cells (ciPTEC) derived from cystinotic patients and healthy volunteers. P-gp-mediated transport was measured by using the P-gp substrate calcein-AM in the presence and absence of the P-gp-inhibitor PSC833. P-gp activity was normal in cystinotic cells as compared to controls. Additionally, the effect of cysteamine on P-gp transport activity and phosphate uptake was determined; demonstrating increased P-gp activity in cystinotic cells, and further decrease of proximal tubular phosphate uptake. This observation is compatible with the persistence of renal Fanconi syndrome in vivo under cysteamine therapy. In summary, P-gp expression and activity are normal in cystinotic ciPTEC, indicating that P-gp dysfunction is not involved in the pathogenesis of cystinosis.
Keywords	cystinosis ; P-glycoprotein ; renal proximal tubular cell ; cysteamine ; Pharmacy and materia medica ; RS1-441 ; Medicine ; R ; DOAJ:Pharmacy and materia medica ; DOAJ:Medicine (General) ; DOAJ:Health Sciences
Subject code	616
Language	English
Publishing date	2011-10-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article: RGS2 inhibits the epithelial Ca2+ channel TRPV6.

Schoeber, Joost P / Topala, Catalin N / Wang, Xinhua / Diepens, Robin J / Lambers, Tim T / Hoenderop, Joost G / Bindels, René J

The Journal of biological chemistry

2006 Volume 281, Issue 40, Page(s) 29669–29674

Abstract: The epithelial Ca(2+) channels TRPV5 and TRPV6 constitute the apical Ca(2+) entry pathway in the process of active Ca(2+) (re)absorption. By yeast two-hybrid and glutathione S-transferase pulldown analysis we identified RGS2 as a novel TRPV6-associated ... ...

Abstract	The epithelial Ca(2+) channels TRPV5 and TRPV6 constitute the apical Ca(2+) entry pathway in the process of active Ca(2+) (re)absorption. By yeast two-hybrid and glutathione S-transferase pulldown analysis we identified RGS2 as a novel TRPV6-associated protein. RGS proteins determine the inactivation kinetics of heterotrimeric G-protein-coupled receptor (GPCR) signaling by regulating the GTPase activity of G(alpha) subunits. Here we demonstrate that TRPV6 interacts with the NH(2)-terminal domain of RGS2 in a Ca(2+)-independent fashion and that overexpression of RGS2 reduces the Na(+) and Ca(2+) current of TRPV6 but not that of TRPV5-transfected human embryonic kidney 293 (HEK293) cells. In contrast, overexpression of the deletion mutant DeltaN-RGS2, lacking the NH(2)-terminal domain of RGS2, in TRPV6-expressing HEK293 cells did not show this inhibition. Furthermore, cell surface biotinylation indicated that the inhibitory effect of RGS2 on TRPV6 activity is not mediated by differences in trafficking or retrieval of TRPV6 from the plasma membrane. This effect probably results from the direct interaction between RGS2 and TRPV6, affecting the gating properties of the channel. Finally, the scaffolding protein spinophilin, shown to recruit RGS2 and regulate GPCR-signaling via G(alpha), did not affect RGS2 binding and electrophysiological properties of TRPV6, indicating a GPCR-independent mechanism of TRPV6 regulation by RGS2.
MeSH term(s)	Animals ; Calcium Channels/metabolism ; Cell Line ; Epithelium/metabolism ; Humans ; Mice ; RGS Proteins/physiology ; TRPV Cation Channels/antagonists & inhibitors ; TRPV Cation Channels/metabolism
Chemical Substances	Calcium Channels ; RGS Proteins ; RGS2 protein, human ; TRPV Cation Channels ; TRPV6 protein, human
Language	English
Publishing date	2006-08-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2997-x
ISSN	1083-351X ; 0021-9258
ISSN (online)	1083-351X
ISSN	0021-9258
DOI	10.1074/jbc.M606233200
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