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Article ; Online: Secreted tissue inhibitor of matrix metalloproteinase restricts

Shilts, Jarrod / Broadie, Kendal

2017 Volume 130, Issue 14, Page(s) 2344–2358

Abstract: Synaptogenesis is coordinated ... ...

Abstract	Synaptogenesis is coordinated by
MeSH term(s)	Drosophila Proteins/metabolism ; Matrix Metalloproteinases/metabolism ; Neuromuscular Junction/metabolism ; Synapses/metabolism ; Synaptic Transmission
Chemical Substances	Drosophila Proteins ; Matrix Metalloproteinases (EC 3.4.24.-)
Language	English
Publishing date	2017-06-02
Publishing country	England
Document type	Journal Article
ZDB-ID	2993-2
ISSN	1477-9137 ; 0021-9533
ISSN (online)	1477-9137
ISSN	0021-9533
DOI	10.1242/jcs.200808
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Zs.MG 14: Show issues

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Article ; Online: No evidence for basigin/CD147 as a direct SARS-CoV-2 spike binding receptor

Shilts, Jarrod / Wright, Gavin J.

bioRxiv

Abstract: The spike protein of SARS-CoV-2 is known to enable viral invasion into human cells through direct binding to host receptors including ACE2. An alternate entry receptor for the virus was recently proposed to be basigin/CD147. These early studies have ... ...

Abstract	The spike protein of SARS-CoV-2 is known to enable viral invasion into human cells through direct binding to host receptors including ACE2. An alternate entry receptor for the virus was recently proposed to be basigin/CD147. These early studies have already prompted a clinical trial and multiple published hypotheses of the role of this host receptor in viral infection and pathogenesis. We sought to independently characterize the basigin-spike protein interaction. After conducting several lines of experiments, we report that we are unable to find evidence supporting the role of basigin as a putative spike-binding receptor. Recombinant forms of both the entire ectodomain and S1 domain of the SARS-CoV-2 spike protein that directly bind ACE2 do not interact with basigin expressed on the surface of human cells. Using specialized assays tailored to detect receptor interactions as weak or weaker than the proposed basigin-spike binding, we report no evidence for direct binding of the viral spike to either of the two common isoforms of basigin. Given the pressing need for clarity on which targets of SARS-CoV-2 may lead to promising therapeutics, we present these findings to allow more informed decisions about the translational relevance of this putative mechanism in the race to understand and treat COVID-19.
Keywords	covid19
Publisher	BioRxiv
Document type	Article ; Online
DOI	10.1101/2020.07.25.221036
Database	COVID19

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Article ; Online: No evidence for basigin/CD147 as a direct SARS-CoV-2 spike binding receptor

Shilts, Jarrod / Wright, Gavin James

bioRxiv

Abstract	The spike protein of SARS-CoV-2 is known to enable viral invasion into human cells through direct binding to host receptors including ACE2. An alternate entry receptor for the virus was recently proposed to be basigin/CD147. These early studies have already prompted a clinical trial and multiple published hypotheses of the role of this host receptor in viral infection and pathogenesis. We sought to independently characterize the basigin-spike protein interaction. After conducting several lines of experiments, we report that we are unable to find evidence supporting the role of basigin as a putative spike-binding receptor. Recombinant forms of both the entire ectodomain and S1 domain of the SARS-CoV-2 spike protein that directly bind ACE2 do not interact with basigin expressed on the surface of human cells. Using specialized assays tailored to detect receptor interactions as weak or weaker than the proposed basigin-spike binding, we report no evidence for direct binding of the viral spike to either of the two common isoforms of basigin. Given the pressing need for clarity on which targets of SARS-CoV-2 may lead to promising therapeutics, we present these findings to allow more informed decisions about the translational relevance of this putative mechanism in the race to understand and treat COVID-19.
Keywords	covid19
Language	English
Publishing date	2020-07-26
Publisher	Cold Spring Harbor Laboratory
Document type	Article ; Online
DOI	10.1101/2020.07.25.221036
Database	COVID19

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Article: Evidence for widespread dysregulation of circadian clock progression in human cancer.

Shilts, Jarrod / Chen, Guanhua / Hughey, Jacob J

PeerJ

2018 Volume 6, Page(s) e4327

Abstract: The ubiquitous daily rhythms in mammalian physiology are guided by progression of the circadian clock. In mice, systemic disruption of the clock can promote tumor growth. ...

Abstract	The ubiquitous daily rhythms in mammalian physiology are guided by progression of the circadian clock. In mice, systemic disruption of the clock can promote tumor growth.
Language	English
Publishing date	2018-01-31
Publishing country	United States
Document type	Journal Article
ZDB-ID	2703241-3
ISSN	2167-8359
ISSN	2167-8359
DOI	10.7717/peerj.4327
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Article ; Online: No evidence for basigin/CD147 as a direct SARS-CoV-2 spike binding receptor.

Shilts, Jarrod / Crozier, Thomas W M / Greenwood, Edward J D / Lehner, Paul J / Wright, Gavin J

Scientific reports

2021 Volume 11, Issue 1, Page(s) 413

Abstract	The spike protein of SARS-CoV-2 is known to enable viral invasion into human cells through direct binding to host receptors including ACE2. An alternate entry receptor for the virus was recently proposed to be basigin/CD147. These early studies have already prompted a clinical trial and multiple published hypotheses speculating on the role of this host receptor in viral infection and pathogenesis. Here, we report that we are unable to find evidence supporting the role of basigin as a putative spike binding receptor. Recombinant forms of the SARS-CoV-2 spike do not interact with basigin expressed on the surface of human cells, and by using specialized assays tailored to detect receptor interactions as weak or weaker than the proposed basigin-spike binding, we report no evidence for a direct interaction between the viral spike protein to either of the two common isoforms of basigin. Finally, removing basigin from the surface of human lung epithelial cells by CRISPR/Cas9 results in no change in their susceptibility to SARS-CoV-2 infection. Given the pressing need for clarity on which viral targets may lead to promising therapeutics, we present these findings to allow more informed decisions about the translational relevance of this putative mechanism in the race to understand and treat COVID-19.
MeSH term(s)	Basigin/metabolism ; COVID-19/metabolism ; COVID-19/virology ; Cell Line ; HEK293 Cells ; Host-Pathogen Interactions ; Humans ; Protein Binding ; Receptors, Virus/metabolism ; SARS-CoV-2/physiology ; Spike Glycoprotein, Coronavirus/metabolism ; Virus Internalization
Chemical Substances	Receptors, Virus ; Spike Glycoprotein, Coronavirus ; spike protein, SARS-CoV-2 ; Basigin (136894-56-9)
Language	English
Publishing date	2021-01-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2615211-3
ISSN	2045-2322 ; 2045-2322
ISSN (online)	2045-2322
ISSN	2045-2322
DOI	10.1038/s41598-020-80464-1
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Neuronal activity drives FMRP- and HSPG-dependent matrix metalloproteinase function required for rapid synaptogenesis.

Dear, Mary L / Shilts, Jarrod / Broadie, Kendal

Science signaling

2017 Volume 10, Issue 504

Abstract: Matrix metalloproteinase (MMP) functions modulate synapse formation and activity-dependent plasticity. Aberrant MMP activity is implicated in fragile X syndrome (FXS), a disease caused by the loss of the RNA-binding protein FMRP and characterized by ... ...

Abstract	Matrix metalloproteinase (MMP) functions modulate synapse formation and activity-dependent plasticity. Aberrant MMP activity is implicated in fragile X syndrome (FXS), a disease caused by the loss of the RNA-binding protein FMRP and characterized by neurological dysfunction and intellectual disability. Gene expression studies in
MeSH term(s)	Animals ; Disease Models, Animal ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster ; Fragile X Syndrome/genetics ; Fragile X Syndrome/metabolism ; Heparan Sulfate Proteoglycans/metabolism ; Matrix Metalloproteinase 1/metabolism ; Matrix Metalloproteinase 2/metabolism ; Neuromuscular Junction/metabolism ; Neurons/metabolism ; Neurons/physiology ; Presynaptic Terminals/metabolism ; Presynaptic Terminals/physiology ; Proteoglycans/genetics ; Proteoglycans/metabolism ; Wnt Signaling Pathway
Chemical Substances	Drosophila Proteins ; Heparan Sulfate Proteoglycans ; Proteoglycans ; dlp protein, Drosophila ; Matrix Metalloproteinase 2 (EC 3.4.24.24) ; Matrix Metalloproteinase 1 (EC 3.4.24.7)
Language	English
Publishing date	2017-11-07
Publishing country	United States
Document type	Journal Article
ZDB-ID	2417226-1
ISSN	1937-9145 ; 1945-0877
ISSN (online)	1937-9145
ISSN	1945-0877
DOI	10.1126/scisignal.aan3181
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Article ; Online: Evidence for widespread dysregulation of circadian clock progression in human cancer

Jarrod Shilts / Guanhua Chen / Jacob J. Hughey

PeerJ, Vol 6, p e

2018 Volume 4327

Abstract: The ubiquitous daily rhythms in mammalian physiology are guided by progression of the circadian clock. In mice, systemic disruption of the clock can promote tumor growth. In vitro, multiple oncogenes can disrupt the clock. However, due to the ... ...

Abstract	The ubiquitous daily rhythms in mammalian physiology are guided by progression of the circadian clock. In mice, systemic disruption of the clock can promote tumor growth. In vitro, multiple oncogenes can disrupt the clock. However, due to the difficulties of studying circadian rhythms in solid tissues in humans, whether the clock is disrupted within human tumors has remained unknown. We sought to determine the state of the circadian clock in human cancer using publicly available transcriptome data. We developed a method, called the clock correlation distance (CCD), to infer circadian clock progression in a group of samples based on the co-expression of 12 clock genes. Our method can be applied to modestly sized datasets in which samples are not labeled with time of day and coverage of the circadian cycle is incomplete. We used the method to define a signature of clock gene co-expression in healthy mouse organs, then validated the signature in healthy human tissues. By then comparing human tumor and non-tumor samples from twenty datasets of a range of cancer types, we discovered that clock gene co-expression in tumors is consistently perturbed. Subsequent analysis of data from clock gene knockouts in mice suggested that perturbed clock gene co-expression in human cancer is not caused solely by the inactivation of clock genes. Furthermore, focusing on lung cancer, we found that human lung tumors showed systematic changes in expression in a large set of genes previously inferred to be rhythmic in healthy lung. Our findings suggest that clock progression is dysregulated in many solid human cancers and that this dysregulation could have broad effects on circadian physiology within tumors. In addition, our approach opens the door to using publicly available data to infer circadian clock progression in a multitude of human phenotypes.
Keywords	Circadian clock ; Gene co-expression ; Cancer ; Transcriptome ; Medicine ; R ; Biology (General) ; QH301-705.5
Subject code	000
Language	English
Publishing date	2018-01-01T00:00:00Z
Publisher	PeerJ Inc.
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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Article ; Online: A physical wiring diagram for the human immune system.

Shilts, Jarrod / Severin, Yannik / Galaway, Francis / Müller-Sienerth, Nicole / Chong, Zheng-Shan / Pritchard, Sophie / Teichmann, Sarah / Vento-Tormo, Roser / Snijder, Berend / Wright, Gavin J

Nature

2022 Volume 608, Issue 7922, Page(s) 397–404

Abstract: The human immune system is composed of a distributed network of cells circulating throughout the body, which must dynamically form physical associations and communicate using interactions between their cell-surface ... ...

Abstract	The human immune system is composed of a distributed network of cells circulating throughout the body, which must dynamically form physical associations and communicate using interactions between their cell-surface proteomes
MeSH term(s)	Cell Communication/immunology ; Humans ; Immune System/cytology ; Immune System/immunology ; Immune System/metabolism ; Leukocytes/chemistry ; Leukocytes/immunology ; Leukocytes/metabolism ; Protein Binding ; Protein Interaction Maps ; Proteome/immunology ; Proteome/metabolism ; Receptors, Cell Surface/chemistry ; Receptors, Cell Surface/immunology ; Receptors, Cell Surface/metabolism
Chemical Substances	Proteome ; Receptors, Cell Surface
Language	English
Publishing date	2022-08-03
Publishing country	England
Document type	Journal Article
ZDB-ID	120714-3
ISSN	1476-4687 ; 0028-0836
ISSN (online)	1476-4687
ISSN	0028-0836
DOI	10.1038/s41586-022-05028-x
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Zs.A 26: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Zs.MO 244: Show issues

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Article ; Online: LRRC15 mediates an accessory interaction with the SARS-CoV-2 spike protein.

Shilts, Jarrod / Crozier, Thomas W M / Teixeira-Silva, Ana / Gabaev, Ildar / Gerber, Pehuén Pereyra / Greenwood, Edward J D / Watson, Samuel James / Ortmann, Brian M / Gawden-Bone, Christian M / Pauzaite, Tekle / Hoffmann, Markus / Nathan, James A / Pöhlmann, Stefan / Matheson, Nicholas J / Lehner, Paul J / Wright, Gavin J

PLoS biology

2023 Volume 21, Issue 2, Page(s) e3001959

Abstract: The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component ... ...

Abstract	The interactions between Severe Acute Respiratory Syndrome Coronavirus 2 (SARS-CoV-2) and human host factors enable the virus to propagate infections that lead to Coronavirus Disease 2019 (COVID-19). The spike protein is the largest structural component of the virus and mediates interactions essential for infection, including with the primary angiotensin-converting enzyme 2 (ACE2) receptor. We performed two independent cell-based systematic screens to determine whether there are additional proteins by which the spike protein of SARS-CoV-2 can interact with human cells. We discovered that in addition to ACE2, expression of LRRC15 also causes spike protein binding. This interaction is distinct from other known spike attachment mechanisms such as heparan sulfates or lectin receptors. Measurements of orthologous coronavirus spike proteins implied the interaction was functionally restricted to SARS-CoV-2 by accessibility. We localized the interaction to the C-terminus of the S1 domain and showed that LRRC15 shares recognition of the ACE2 receptor binding domain. From analyzing proteomics and single-cell transcriptomics, we identify LRRC15 expression as being common in human lung vasculature cells and fibroblasts. Levels of LRRC15 were greatly elevated by inflammatory signals in the lungs of COVID-19 patients. Although infection assays demonstrated that LRRC15 alone is not sufficient to permit viral entry, we present evidence that it can modulate infection of human cells. This unexpected interaction merits further investigation to determine how SARS-CoV-2 exploits host LRRC15 and whether it could account for any of the distinctive features of COVID-19.
MeSH term(s)	Humans ; COVID-19 ; SARS-CoV-2/metabolism ; Spike Glycoprotein, Coronavirus/metabolism ; Angiotensin-Converting Enzyme 2/metabolism ; Protein Binding ; Membrane Proteins/metabolism
Chemical Substances	spike protein, SARS-CoV-2 ; Spike Glycoprotein, Coronavirus ; Angiotensin-Converting Enzyme 2 (EC 3.4.17.23) ; LRRC15 protein, human ; Membrane Proteins
Language	English
Publishing date	2023-02-03
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2126776-5
ISSN	1545-7885 ; 1544-9173
ISSN (online)	1545-7885
ISSN	1544-9173
DOI	10.1371/journal.pbio.3001959
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Article ; Online: No evidence for basigin/CD147 as a direct SARS-CoV-2 spike binding receptor

Jarrod Shilts / Thomas W. M. Crozier / Edward J. D. Greenwood / Paul J. Lehner / Gavin J. Wright

Scientific Reports, Vol 11, Iss 1, Pp 1-

2021 Volume 10

Abstract: Abstract The spike protein of SARS-CoV-2 is known to enable viral invasion into human cells through direct binding to host receptors including ACE2. An alternate entry receptor for the virus was recently proposed to be basigin/CD147. These early studies ... ...

Abstract	Abstract The spike protein of SARS-CoV-2 is known to enable viral invasion into human cells through direct binding to host receptors including ACE2. An alternate entry receptor for the virus was recently proposed to be basigin/CD147. These early studies have already prompted a clinical trial and multiple published hypotheses speculating on the role of this host receptor in viral infection and pathogenesis. Here, we report that we are unable to find evidence supporting the role of basigin as a putative spike binding receptor. Recombinant forms of the SARS-CoV-2 spike do not interact with basigin expressed on the surface of human cells, and by using specialized assays tailored to detect receptor interactions as weak or weaker than the proposed basigin-spike binding, we report no evidence for a direct interaction between the viral spike protein to either of the two common isoforms of basigin. Finally, removing basigin from the surface of human lung epithelial cells by CRISPR/Cas9 results in no change in their susceptibility to SARS-CoV-2 infection. Given the pressing need for clarity on which viral targets may lead to promising therapeutics, we present these findings to allow more informed decisions about the translational relevance of this putative mechanism in the race to understand and treat COVID-19.
Keywords	Medicine ; R ; Science ; Q
Subject code	570
Language	English
Publishing date	2021-01-01T00:00:00Z
Publisher	Nature Portfolio
Document type	Article ; Online
Database	BASE - Bielefeld Academic Search Engine (life sciences selection)

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