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Article ; Online: A Tetrameric Assembly of Saposin A: Increasing Structural Diversity in Lipid Transfer Proteins.

Shamin, Maria / Spratley, Samantha J / Graham, Stephen C / Deane, Janet E

Contact (Thousand Oaks (Ventura County, Calif.))

2021 Volume 4, Page(s) 251525642110523

Abstract: Saposins are lipid transfer proteins required for the degradation of sphingolipids in the lysosome. These small proteins bind lipids by transitioning from a closed, monomeric state to an open conformation exposing a hydrophobic surface that binds and ... ...

Abstract	Saposins are lipid transfer proteins required for the degradation of sphingolipids in the lysosome. These small proteins bind lipids by transitioning from a closed, monomeric state to an open conformation exposing a hydrophobic surface that binds and shields hydrophobic lipid tails from the aqueous environment. Saposins form a range of multimeric assemblies to encompass these bound lipids and present them to hydrolases in the lysosome. This lipid-binding property of human saposin A has been exploited to form lipoprotein nanodiscs suitable for structural studies of membrane proteins. Here we present the crystal structure of a unique tetrameric assembly of murine saposin A produced serendipitously, following modifications of published protocols for making lipoprotein nanodiscs. The structure of this new saposin oligomer highlights the diversity of tertiary arrangement that can be adopted by these important lipid transfer proteins.
Language	English
Publishing date	2021-11-17
Publishing country	United States
Document type	Journal Article
ZDB-ID	2964312-0
ISSN	2515-2564 ; 2515-2564
ISSN (online)	2515-2564
ISSN	2515-2564
DOI	10.1177/25152564211052382
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Article ; Online: Can baseline features predict a reduction in pain and disability following neck-specific exercise in people with chronic non-specific neck pain?: A systematic review and meta-analysis protocol.

Chen, Ziyan / Falla, Deborah / Elgueta Cancino, Edith / A Deane, Janet

BMJ open

2023 Volume 13, Issue 7, Page(s) e074494

Abstract: Introduction: Neck-specific exercises (NSEs) are commonly used for the treatment of chronic non-specific neck pain (CNSNP). However, it remains unclear whether baseline features can predict the response to neck-specific exercise (NSE) in people with ... ...

Abstract	Introduction: Neck-specific exercises (NSEs) are commonly used for the treatment of chronic non-specific neck pain (CNSNP). However, it remains unclear whether baseline features can predict the response to neck-specific exercise (NSE) in people with CNSNP. This systematic review aims to assess whether baseline features such as age, gender, muscle activity, fatigability, endurance and fear of movement can predict pain and disability reduction following a NSE intervention. Methods and analysis: This systematic review and meta-analysis will be reported in line with the Preferred Reporting Items for Systematic Reviews and Meta-Analyses (PRISMA) Protocols guidelines checklist. The Web of Science, PubMed, Scopus, MEDLINE, Embase and CINAHL databases; key journals; and grey literature will be searched up until June 2023, including medical subject heading terms and keywords combinations. Included studies will investigate an association between the baseline features and pain and disability outcomes following NSE in people with CNSNP. Two independent reviewers will oversee the searching, screening, data extraction and assessment of risk of bias. The risk of bias will be assessed using the Risk Of Bias In Non-randomised Studies of Interventions (ROBINS-I) and Risk-Of-Bias tool for randomised trials 2 (ROB 2). The quality of evidence will be assessed using the Grading of Recommendations Assessment, Development and Evaluation approach (GRADE). Using standardised forms, details regarding study characteristics, baseline features (predictive factors), intervention, primary outcome and effect size (OR and 95% CI of each predictive factor and p value) will be extracted from included studies. Meta-analyses will be considered, if the studies are sufficiently homogeneous and if three or more studies investigate the same or comparable factors that predict the same response (pain intensity or disability). In the event that less than three studies investigated the same factors, a narrative synthesis will be conducted. Ethics and dissemination: Ethical approval will not be required as this review will be based on published studies. The results of this study will be submitted to a peer-reviewed journal and presented at conferences. Prospero registration number: CRD42023408332.
MeSH term(s)	Humans ; Checklist ; Databases, Factual ; Exercise Therapy ; Meta-Analysis as Topic ; Neck Pain/therapy ; Systematic Reviews as Topic
Language	English
Publishing date	2023-07-10
Publishing country	England
Document type	Journal Article
ZDB-ID	2599832-8
ISSN	2044-6055 ; 2044-6055
ISSN (online)	2044-6055
ISSN	2044-6055
DOI	10.1136/bmjopen-2023-074494
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Article ; Online: The crystal structure of vaccinia virus protein E2 and perspectives on the prediction of novel viral protein folds.

Gao, William N D / Gao, Chen / Deane, Janet E / Carpentier, David C J / Smith, Geoffrey L / Graham, Stephen C

The Journal of general virology

2022 Volume 103, Issue 1

Abstract: The morphogenesis of vaccinia virus (VACV, ... ...

Abstract	The morphogenesis of vaccinia virus (VACV, family
MeSH term(s)	Binding Sites ; Crystallography, X-Ray ; Poxviridae/metabolism ; Protein Binding ; Protein Conformation ; Vaccinia virus/chemistry ; Vaccinia virus/genetics ; Vaccinia virus/physiology ; Viral Proteins/chemistry ; Viral Proteins/genetics ; Viral Proteins/metabolism ; Virus Replication
Chemical Substances	Viral Proteins
Language	English
Publishing date	2022-02-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	219316-4
ISSN	1465-2099 ; 0022-1317
ISSN (online)	1465-2099
ISSN	0022-1317
DOI	10.1099/jgv.0.001716
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Article: The lipid transfer protein Saposin B does not directly bind CD1d for lipid antigen loading.

Shamin, Maria / Benedyk, Tomasz H / Graham, Stephen C / Deane, Janet E

Wellcome open research

2019 Volume 4, Page(s) 117

Abstract: Background: ...

Abstract	Background:
Language	English
Publishing date	2019-10-18
Publishing country	England
Document type	Journal Article
ISSN	2398-502X
ISSN	2398-502X
DOI	10.12688/wellcomeopenres.15368.2
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Article: The Bicyclic Form of

Viuff, Agnete / Salamone, Stéphane / McLoughlin, Joseph / Deane, Janet E / Jensen, Henrik H

ACS medicinal chemistry letters

2020 Volume 12, Issue 1, Page(s) 56–59

Abstract: Competitive inhibitors of galactocerebrosidase (GALC) could be candidates for pharmacological chaperone therapy of patients with Krabbe disease. The known and selective nortropane-type ... ...

Abstract	Competitive inhibitors of galactocerebrosidase (GALC) could be candidates for pharmacological chaperone therapy of patients with Krabbe disease. The known and selective nortropane-type iminosugar
Language	English
Publishing date	2020-12-18
Publishing country	United States
Document type	Journal Article
ISSN	1948-5875
ISSN	1948-5875
DOI	10.1021/acsmedchemlett.0c00377
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Article ; Online: Molecular models should not be published without the corresponding atomic coordinates.

Graham, Stephen C / Nagar, Bhushan / Privé, Gilbert G / Deane, Janet E

Proceedings of the National Academy of Sciences of the United States of America

2019 Volume 116, Issue 23, Page(s) 11099–11100

MeSH term(s)	Deep Learning ; Gaucher Disease ; Glucosylceramidase ; Humans ; Molecular Dynamics Simulation ; Protein Conformation
Chemical Substances	Glucosylceramidase (EC 3.2.1.45)
Language	English
Publishing date	2019-06-04
Publishing country	United States
Document type	Letter ; Comment
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1904409116
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Article ; Online: Molecular mechanism of Afadin substrate recruitment to the receptor phosphatase PTPRK via its pseudophosphatase domain.

Hay, Iain M / Mulholland, Katie E / Lai, Tiffany / Graham, Stephen C / Sharpe, Hayley J / Deane, Janet E

eLife

2022 Volume 11

Abstract: Protein tyrosine phosphatase receptor-type kappa (PTPRK) is a transmembrane receptor that links extracellular homophilic interactions to intracellular catalytic activity. Previously we showed that PTPRK promotes cell-cell adhesion by selectively ... ...

Abstract	Protein tyrosine phosphatase receptor-type kappa (PTPRK) is a transmembrane receptor that links extracellular homophilic interactions to intracellular catalytic activity. Previously we showed that PTPRK promotes cell-cell adhesion by selectively dephosphorylating several cell junction regulators including the protein Afadin (Fearnley et al, 2019). Here, we demonstrate that Afadin is recruited for dephosphorylation by directly binding to the PTPRK D2 pseudophosphatase domain. We mapped this interaction to a putative coiled coil (CC) domain in Afadin that is separated by more than 100 amino acids from the substrate pTyr residue. We identify the residues that define PTP specificity, explaining how Afadin is selectively dephosphorylated by PTPRK yet not by the closely related receptor tyrosine phosphatase PTPRM. Our work demonstrates that PTP substrate specificity can be determined by protein-protein interactions distal to the active site. This explains how PTPRK and other PTPs achieve substrate specificity despite a lack of specific sequence context at the substrate pTyr. Furthermore, by demonstrating that these interactions are phosphorylation-independent and mediated via binding to a non-catalytic domain, we highlight how receptor PTPs could function as intracellular scaffolds in addition to catalyzing protein dephosphorylation.
MeSH term(s)	Microfilament Proteins/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatases/metabolism ; Substrate Specificity
Chemical Substances	afadin ; Microfilament Proteins ; Protein Tyrosine Phosphatases (EC 3.1.3.48)
Language	English
Publishing date	2022-10-20
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2687154-3
ISSN	2050-084X ; 2050-084X
ISSN (online)	2050-084X
ISSN	2050-084X
DOI	10.7554/eLife.79855
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Article ; Online: New therapeutic approaches for Krabbe disease: The potential of pharmacological chaperones.

Spratley, Samantha J / Deane, Janet E

Journal of neuroscience research

2016 Volume 94, Issue 11, Page(s) 1203–1219

Abstract: Missense mutations in the lysosomal hydrolase β-galactocerebrosidase (GALC) account for at least 40% of known cases of Krabbe disease (KD). Most of these missense mutations are predicted to disrupt the fold of the enzyme, preventing GALC in sufficient ... ...

Abstract	Missense mutations in the lysosomal hydrolase β-galactocerebrosidase (GALC) account for at least 40% of known cases of Krabbe disease (KD). Most of these missense mutations are predicted to disrupt the fold of the enzyme, preventing GALC in sufficient amounts from reaching its site of action in the lysosome. The predominant central nervous system (CNS) pathology and the absence of accumulated primary substrate within the lysosome mean that strategies used to treat other lysosomal storage disorders (LSDs) are insufficient in KD, highlighting the still unmet clinical requirement for successful KD therapeutics. Pharmacological chaperone therapy (PCT) is one strategy being explored to overcome defects in GALC caused by missense mutations. In recent studies, several small-molecule inhibitors have been identified as promising chaperone candidates for GALC. This Review discusses new insights gained from these studies and highlights the importance of characterizing both the chaperone interaction and the underlying mutation to define properly a responsive population and to improve the translation of existing lead molecules into successful KD therapeutics. We also highlight the importance of using multiple complementary methods to monitor PCT effectiveness. Finally, we explore the exciting potential of using combination therapy to ameliorate disease through the use of PCT with existing therapies or with more generalized therapeutics, such as proteasomal inhibition, that have been shown to have synergistic effects in other LSDs. This, alongside advances in CNS delivery of recombinant enzyme and targeted rational drug design, provides a promising outlook for the development of KD therapeutics. © 2016 The Authors. Journal of Neuroscience Research Published by Wiley Periodicals, Inc.
MeSH term(s)	Animals ; Enzyme Replacement Therapy ; Galactosylceramidase/genetics ; Galactosylceramidase/metabolism ; Humans ; Leukodystrophy, Globoid Cell/drug therapy ; Leukodystrophy, Globoid Cell/genetics ; Molecular Chaperones/chemistry ; Molecular Chaperones/therapeutic use
Chemical Substances	Molecular Chaperones ; Galactosylceramidase (EC 3.2.1.46)
Language	English
Publishing date	2016-11
Publishing country	United States
Document type	Journal Article ; Review
ZDB-ID	195324-2
ISSN	1097-4547 ; 0360-4012
ISSN (online)	1097-4547
ISSN	0360-4012
DOI	10.1002/jnr.23762
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Article ; Online: Attenuation hotspots in neurotropic human astroviruses.

Ali, Hashim / Lulla, Aleksei / Nicholson, Alex S / Hankinson, Jack / Wignall-Fleming, Elizabeth B / O'Connor, Rhian L / Vu, Diem-Lan / Graham, Stephen C / Deane, Janet E / Guix, Susana / Lulla, Valeria

PLoS biology

2023 Volume 21, Issue 7, Page(s) e3001815

Abstract: During the last decade, the detection of neurotropic astroviruses has increased dramatically. The MLB genogroup of astroviruses represents a genetically distinct group of zoonotic astroviruses associated with gastroenteritis and severe neurological ... ...

Abstract	During the last decade, the detection of neurotropic astroviruses has increased dramatically. The MLB genogroup of astroviruses represents a genetically distinct group of zoonotic astroviruses associated with gastroenteritis and severe neurological complications in young children, the immunocompromised, and the elderly. Using different virus evolution approaches, we identified dispensable regions in the 3' end of the capsid-coding region responsible for attenuation of MLB astroviruses in susceptible cell lines. To create recombinant viruses with identified deletions, MLB reverse genetics (RG) and replicon systems were developed. Recombinant truncated MLB viruses resulted in imbalanced RNA synthesis and strong attenuation in iPSC-derived neuronal cultures confirming the location of neurotropism determinants. This approach can be used for the development of vaccine candidates using attenuated astroviruses that infect humans, livestock animals, and poultry.
MeSH term(s)	Child ; Animals ; Humans ; Child, Preschool ; Aged ; Mamastrovirus/genetics ; Astroviridae Infections/veterinary ; Astroviridae Infections/diagnosis ; Gastroenteritis ; Capsid Proteins/genetics ; Capsid ; Phylogeny
Chemical Substances	Capsid Proteins
Language	English
Publishing date	2023-07-17
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.3001815
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Article ; Online: Altered plasma membrane abundance of the sulfatide-binding protein NF155 links glycosphingolipid imbalances to demyelination.

McKie, Shannon J / Nicholson, Alex S / Smith, Emily / Fawke, Stuart / Caroe, Eve R / Williamson, James C / Butt, Benjamin G / Kolářová, Denisa / Peterka, Ondřej / Holčapek, Michal / Lehner, Paul J / Graham, Stephen C / Deane, Janet E

Proceedings of the National Academy of Sciences of the United States of America

2023 Volume 120, Issue 14, Page(s) e2218823120

Abstract: Myelin is a multilayered membrane that tightly wraps neuronal axons, enabling efficient, high-speed signal propagation. The axon and myelin sheath form tight contacts, mediated by specific plasma membrane proteins and lipids, and disruption of these ... ...

Abstract	Myelin is a multilayered membrane that tightly wraps neuronal axons, enabling efficient, high-speed signal propagation. The axon and myelin sheath form tight contacts, mediated by specific plasma membrane proteins and lipids, and disruption of these contacts causes devastating demyelinating diseases. Using two cell-based models of demyelinating sphingolipidoses, we demonstrate that altered lipid metabolism changes the abundance of specific plasma membrane proteins. These altered membrane proteins have known roles in cell adhesion and signaling, with several implicated in neurological diseases. The cell surface abundance of the adhesion molecule neurofascin (NFASC), a protein critical for the maintenance of myelin-axon contacts, changes following disruption to sphingolipid metabolism. This provides a direct molecular link between altered lipid abundance and myelin stability. We show that the NFASC isoform NF155, but not NF186, interacts directly and specifically with the sphingolipid sulfatide via multiple binding sites and that this interaction requires the full-length extracellular domain of NF155. We demonstrate that NF155 adopts an S-shaped conformation and preferentially binds sulfatide-containing membranes in
MeSH term(s)	Humans ; Sulfoglycosphingolipids ; Glycosphingolipids/metabolism ; Carrier Proteins/metabolism ; Nerve Growth Factors/metabolism ; Myelin Sheath/metabolism ; Cell Adhesion Molecules/metabolism ; Demyelinating Diseases/pathology
Chemical Substances	Sulfoglycosphingolipids ; Glycosphingolipids ; Carrier Proteins ; Nerve Growth Factors ; Cell Adhesion Molecules
Language	English
Publishing date	2023-03-30
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.2218823120
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