cometadata/datacite-titles-descriptions-related-identifiers huggingface dataset:
DOI: 10.17870/bathspa.14269337.v1
title: Fragile Stories - Contextualising Information

description: <i>Fragile Stories</i> explores the complexity of mark making on an intimate scale, using typographic punctuation and careful precision to create skeletal structures inspired by the natural world and textile samples. It responds to nature as lines, shapes and rhythms of contemplative repetition, and to stitching as text and language.This item contains the following contextualising information about the international dissemination of Mandy Bonnell's work between 2015 and 2020:1. Documentation of work-in-progress at the <b>Elam International Print Workshop</b>, Auckland, New Zealand, 30 January 2015 - 28 February 2015. Image courtesy of Mandy Bonnell. Used with permission.2. Online publicity for <b><i>Seeds and Syntax</i></b><i>, </i>Eagle Gallery EMH Arts, London, 6 February 2015 - 6 March 2015. Available via this link and also below under 'References'.3. Online publicity for <b><i>Imaginary Worlds, </i></b>Oriel Davies Gallery, Wales, 22 October 2016 - 25 February 2017. To view use this link or see below under 'References'.4. Online publicity for Bonnell's exhibition at <b>Scuola di Grafica Gallery</b>, Venice, Italy, 3-11 March 2017. To view use this link or see 'References' below.5. Online publicity for <b><i>From the Ground</i></b>, Drawing Projects UK, Trowbridge, 5 May - 28 June 2018. To view use this link or see 'References' below.6. Online publicity for a talk by Mandy Bonnell and James Brooks in association with <b><i>From the Ground</i></b>, Drawing Projects UK, Trowbridge, 5 May - 28 June 2018. View via this link or see 'References' below.7. Publicity documents for <b><i>Special Editions</i></b><i> </i>at Eagle Gallery EMH Arts, London, 28 March - 20 April 2019. See PDFs contained within this item. Documents courtesy of Eagle Gallery EMH Arts. Used with permission.8. Online publicity for <b><i>Homebody: New Prints 2020/Winter</i></b>, International Print Center New York (IPCNY), USA, 14 Jan - 21 March 2020. View via this link or see 'References' below.9. A virtual tour of the exhibition <b><i>Homebody: New Prints 2020/Winter</i></b>, International Print Center New York (IPCNY), USA, 14 Jan - 21 March 2020. View via this link or see 'References' below.<b>The work is under copyright and may not be used without permission. Use of this repository acknowledges cooperation with its policies and relevant copyright law.</b>
DOI: 10.17870/bathspa.14273078.v1
title: Fragile Stories - Statement of Cancellation due to COVID-19

description: <i>Fragile Stories</i> explores the complexity of mark making on an intimate scale, using typographic punctuation and careful precision to create skeletal structures inspired by the natural world and textile samples. It responds to nature as lines, shapes and rhythms of contemplative repetition, and to stitching as text and language.This item contains a statement detailing the reasons for the cancellation of Mandy Bonnell's solo exhibition <i>Fragile Stories</i> at Palazzo Mocenigo, Venice, Italy in 2020, due to the COVID-19 pandemic.<b>The work is under copyright and may not be used without permission. Use of this repository acknowledges cooperation with its policies and relevant copyright law.</b>
DOI: 10.17870/bathspa.14273078
title: Fragile Stories - Statement of Cancellation due to COVID-19

description: <i>Fragile Stories</i> explores the complexity of mark making on an intimate scale, using typographic punctuation and careful precision to create skeletal structures inspired by the natural world and textile samples. It responds to nature as lines, shapes and rhythms of contemplative repetition, and to stitching as text and language.This item contains a statement detailing the reasons for the cancellation of Mandy Bonnell's solo exhibition <i>Fragile Stories</i> at Palazzo Mocenigo, Venice, Italy in 2020, due to the COVID-19 pandemic.<b>The work is under copyright and may not be used without permission. Use of this repository acknowledges cooperation with its policies and relevant copyright law.</b>
DOI: 10.6084/m9.figshare.11798502
title: Influenza A virus protein PB1-F2 impairs innate immunity by inducing mitophagy

description: Influenza A virus (IAV) infection induces mitophagy, which is essential for the clearance of damaged mitochondria. Dysfunctional mitochondria can be selectively targeted by PINK1, which recruits PRKN/PARK2 and leads to subsequent mitochondrial sequestration within autophagosomes. The IAV PB1-F2 protein translocates to mitochondria, accelerates the mitochondrial fragmentation and impairs the innate immunity. However, whether PB1-F2 mediates IAV–induced mitophagy and the relation between mitophagy and PB1-F2-attenuated innate immunity remain obscure. Here, we showed that PB1-F2 translocated to mitochondria by interacting and colocalizing with TUFM (Tu translation elongation factor, mitochondrial). Further studies revealed that PB1-F2 induced complete mitophagy, which required the interactions of PB1-F2 with both TUFM and MAP1LC3B/LC3B that mediated the autophagosome formation. PB1-F2-induced mitophagy was critical for the MAVS (mitochondrial antiviral signaling protein) degradation and led to its suppression of the type I IFN production. Importantly, the C-terminal LIR motif of PB1-F2 protein was demonstrated to be essential for its mitophagy induction and attenuated innate immunity. In conclusion, PB1-F2-induced mitophagy strongly correlates with impaired cellular innate immunity, revealing it is a potential therapeutic target. <b>Abbreviations:</b> BCL2L13: BCL2 like 13; BECN1: beclin 1; BNIP3L/Nix: BCL2 interacting protein 3 like; CQ: chloroquine; DDX58: DExD/H-box helicase 58; eGFP: enhanced green fluorescent protein; hpi: hours post infection; IAV: influenza A virus; IFN: interferon; IP: immunoprecipitation; LIR: LC3-interacting region; MAP1LC3B/LC3B: microtubule associated protein 1 light chain 3 beta; MAVS: mitochondrial antiviral signaling protein; MMP: mitochondrial membrane potential; MOI, multiplicity of infection; mRFP: monomeric red fluorescent protein; NBR1: NBR1 autophagy cargo receptor; NC: negative control; NLRP3: NLR family pyrin domain containing 3; PINK1: PTEN induced kinase 1; PRKN/PARK2: parkin RBR E3 ubiquitin protein ligase; RLR: RIG-I-like-receptor; ROS: reactive oxygen species; SEV: sendai virus; SQSTM1/p62: sequestosome 1; TAX1BP1: Tax1 binding protein 1; TM: transmembrane; TOMM20/40: translocase of outer mitochondrial membrane 20/40; TUFM: Tu translation elongation factor, mitochondrial.
DOI: 10.6084/m9.figshare.11798502.v1
title: Influenza A virus protein PB1-F2 impairs innate immunity by inducing mitophagy

description: Influenza A virus (IAV) infection induces mitophagy, which is essential for the clearance of damaged mitochondria. Dysfunctional mitochondria can be selectively targeted by PINK1, which recruits PRKN/PARK2 and leads to subsequent mitochondrial sequestration within autophagosomes. The IAV PB1-F2 protein translocates to mitochondria, accelerates the mitochondrial fragmentation and impairs the innate immunity. However, whether PB1-F2 mediates IAV–induced mitophagy and the relation between mitophagy and PB1-F2-attenuated innate immunity remain obscure. Here, we showed that PB1-F2 translocated to mitochondria by interacting and colocalizing with TUFM (Tu translation elongation factor, mitochondrial). Further studies revealed that PB1-F2 induced complete mitophagy, which required the interactions of PB1-F2 with both TUFM and MAP1LC3B/LC3B that mediated the autophagosome formation. PB1-F2-induced mitophagy was critical for the MAVS (mitochondrial antiviral signaling protein) degradation and led to its suppression of the type I IFN production. Importantly, the C-terminal LIR motif of PB1-F2 protein was demonstrated to be essential for its mitophagy induction and attenuated innate immunity. In conclusion, PB1-F2-induced mitophagy strongly correlates with impaired cellular innate immunity, revealing it is a potential therapeutic target. <b>Abbreviations:</b> BCL2L13: BCL2 like 13; BECN1: beclin 1; BNIP3L/Nix: BCL2 interacting protein 3 like; CQ: chloroquine; DDX58: DExD/H-box helicase 58; eGFP: enhanced green fluorescent protein; hpi: hours post infection; IAV: influenza A virus; IFN: interferon; IP: immunoprecipitation; LIR: LC3-interacting region; MAP1LC3B/LC3B: microtubule associated protein 1 light chain 3 beta; MAVS: mitochondrial antiviral signaling protein; MMP: mitochondrial membrane potential; MOI, multiplicity of infection; mRFP: monomeric red fluorescent protein; NBR1: NBR1 autophagy cargo receptor; NC: negative control; NLRP3: NLR family pyrin domain containing 3; PINK1: PTEN induced kinase 1; PRKN/PARK2: parkin RBR E3 ubiquitin protein ligase; RLR: RIG-I-like-receptor; ROS: reactive oxygen species; SEV: sendai virus; SQSTM1/p62: sequestosome 1; TAX1BP1: Tax1 binding protein 1; TM: transmembrane; TOMM20/40: translocase of outer mitochondrial membrane 20/40; TUFM: Tu translation elongation factor, mitochondrial.
DOI: 10.6084/m9.figshare.11799945
title: Induction of autophagy increases the proteolytic activity of reservosomes during <i>Trypanosoma cruzi</i> metacyclogenesis

description: Cruzipain, the major cysteine protease of the pathogenic protozoa <i>Trypanosoma cruzi</i>, is an important virulence factor that plays a key role in the parasite nutrition, differentiation and host cell infection. Cruzipain is synthesized as a zymogen, matured, and delivered to reservosomes. These organelles that store proteins and lipids ingested by endocytosis undergo a dramatic decrease in number during the metacyclogenesis of <i>T. cruzi</i>. Autophagy is a process that digests the own cell components to supply energy under starvation or different stress situations. This pathway is important during cell growth, differentiation and death. Previously, we showed that the autophagy pathway of <i>T. cruzi</i> is induced during metacyclogenesis. This work aimed to evaluate the participation of macroautophagy/autophagy in the distribution and function of reservosomes and cruzipain during this process. We found that parasite starvation promotes the cruzipain delivery to reservosomes. Enhanced autophagy increases acidity and hydrolytic activity in these compartments resulting in cruzipain enzymatic activation and self- processing. Inhibition of autophagy similarly impairs cruzipain traffic and activity than protease inhibitors, whereas mutant parasites that exhibit increased basal autophagy, also display increased cruzipain processing under control conditions. Further experiments showed that autophagy induced cruzipain activation and self-processing promote <i>T. cruzi</i> differentiation and host cell infection. These findings highlight the key role of <i>T. cruzi</i> autophagy in these processes and reveal a potential new target for Chagas disease therapy. <b>Abbreviations:</b> Baf: bafilomycin A<sub>1</sub>; CTE: C-terminal extension; Cz: cruzipain; IIF: indirect immunofluorescence; K777: vinyl sulfone with specific Cz inhibitory activity; Prot Inh: broad-spectrum protease inhibitor; Spa1: spautin-1; Wort: wortmannin
DOI: 10.6084/m9.figshare.11799945.v1
title: Induction of autophagy increases the proteolytic activity of reservosomes during <i>Trypanosoma cruzi</i> metacyclogenesis

description: Cruzipain, the major cysteine protease of the pathogenic protozoa <i>Trypanosoma cruzi</i>, is an important virulence factor that plays a key role in the parasite nutrition, differentiation and host cell infection. Cruzipain is synthesized as a zymogen, matured, and delivered to reservosomes. These organelles that store proteins and lipids ingested by endocytosis undergo a dramatic decrease in number during the metacyclogenesis of <i>T. cruzi</i>. Autophagy is a process that digests the own cell components to supply energy under starvation or different stress situations. This pathway is important during cell growth, differentiation and death. Previously, we showed that the autophagy pathway of <i>T. cruzi</i> is induced during metacyclogenesis. This work aimed to evaluate the participation of macroautophagy/autophagy in the distribution and function of reservosomes and cruzipain during this process. We found that parasite starvation promotes the cruzipain delivery to reservosomes. Enhanced autophagy increases acidity and hydrolytic activity in these compartments resulting in cruzipain enzymatic activation and self- processing. Inhibition of autophagy similarly impairs cruzipain traffic and activity than protease inhibitors, whereas mutant parasites that exhibit increased basal autophagy, also display increased cruzipain processing under control conditions. Further experiments showed that autophagy induced cruzipain activation and self-processing promote <i>T. cruzi</i> differentiation and host cell infection. These findings highlight the key role of <i>T. cruzi</i> autophagy in these processes and reveal a potential new target for Chagas disease therapy. <b>Abbreviations:</b> Baf: bafilomycin A<sub>1</sub>; CTE: C-terminal extension; Cz: cruzipain; IIF: indirect immunofluorescence; K777: vinyl sulfone with specific Cz inhibitory activity; Prot Inh: broad-spectrum protease inhibitor; Spa1: spautin-1; Wort: wortmannin
DOI: 10.6084/m9.figshare.11730987
title: Autophagy regulates functional differentiation of mammary epithelial cells

description: Mitochondria operate as a central hub for many metabolic processes by sensing and responding to the cellular environment. Developmental cues from the environment have been implicated in selective autophagy, or mitophagy, of mitochondria during cell differentiation and tissue development. Mitophagy occurring in this context, termed programmed mitophagy, responds to cell state rather than mitochondrial damage and is often accompanied by a metabolic transition. However, little is known about the mechanisms that engage and execute mitophagy under physiological or developmental conditions. As the mammary gland undergoes post-natal development and lactation challenges mitochondrial homeostasis, we investigated the contribution of mitochondria to differentiation of mammary epithelial cells (MECs). Using lactogenic differentiation of the HC11 mouse MEC line, we demonstrated that HC11 cells transition to a highly energetic state during differentiation by engaging both oxidative phosphorylation and glycolysis. Interestingly, this transition was lost when autophagy was inhibited with bafilomycin A<sub>1</sub> or knockdown of <i>Atg7</i> (<i>autophagy related 7</i>). To evaluate the specific targeting of mitochondria, we traced mitochondrial oxidation and turnover <i>in vitro</i> with the fluorescent probe, <i>pMitoTimer</i>. Indeed, we found that differentiation engaged mitophagy. To further evaluate the requirement of mitophagy during differentiation, we knocked down the expression of <i>Prkn/parkin</i> in HC11 cells. We found that MEC differentiation was impaired in <i>shPrkn</i> cells, implying that PRKN is required for MEC differentiation. These studies suggest a novel regulation of MEC differentiation through programmed mitophagy and provide a foundation for future studies of development and disease associated with mitochondrial function in the mammary gland. <b>Abbreviations</b>: AA: antimycin A; ATG5: autophagy related 5; BAF: bafilomycin A<sub>1</sub>; BNIP3: BCL2 interacting protein 3; BNIP3L/NIX: BCL2 interacting protein 3 like; COX8A: cytochrome c oxidase subunit 8A; CQ: chloroquine; CSN2: casein beta; ECAR: extracellular acidification rate; FCCP: trifluoromethoxy carbonylcyanide phenylhydrazone; FUNDC1: FUN14 domain containing 1; HIF1A: hypoxia inducible factor 1 subunit alpha; L1: lactation day 1; MAP1LC3B: microtubule associated protein 1 light chain 3 beta; MEC: mammary epithelial cell; mitoQ: mitoquinol; mROS: mitochondrial reactive oxygen species; OCR: oxygen consumption rate; P: priming; P16: pregnancy day 16; PARP1: poly(ADP-ribose) polymerase 1; PINK1: PTEN induced kinase 1; PPARGC1A: PPARG coactivator 1 alpha; PRKN: parkin RBR E3 ubiquitin protein ligase; <i>shNT</i>: short hairpin non-targeting control; SQSTM1: sequestosome 1; STAT3: signal transducer and activator of transcription 3; TEM: transmission electron microscopy; TFAM: transcription factor A, mitochondrial; U: undifferentiated.
DOI: 10.6084/m9.figshare.11730987.v1
title: Autophagy regulates functional differentiation of mammary epithelial cells

description: Mitochondria operate as a central hub for many metabolic processes by sensing and responding to the cellular environment. Developmental cues from the environment have been implicated in selective autophagy, or mitophagy, of mitochondria during cell differentiation and tissue development. Mitophagy occurring in this context, termed programmed mitophagy, responds to cell state rather than mitochondrial damage and is often accompanied by a metabolic transition. However, little is known about the mechanisms that engage and execute mitophagy under physiological or developmental conditions. As the mammary gland undergoes post-natal development and lactation challenges mitochondrial homeostasis, we investigated the contribution of mitochondria to differentiation of mammary epithelial cells (MECs). Using lactogenic differentiation of the HC11 mouse MEC line, we demonstrated that HC11 cells transition to a highly energetic state during differentiation by engaging both oxidative phosphorylation and glycolysis. Interestingly, this transition was lost when autophagy was inhibited with bafilomycin A<sub>1</sub> or knockdown of <i>Atg7</i> (<i>autophagy related 7</i>). To evaluate the specific targeting of mitochondria, we traced mitochondrial oxidation and turnover <i>in vitro</i> with the fluorescent probe, <i>pMitoTimer</i>. Indeed, we found that differentiation engaged mitophagy. To further evaluate the requirement of mitophagy during differentiation, we knocked down the expression of <i>Prkn/parkin</i> in HC11 cells. We found that MEC differentiation was impaired in <i>shPrkn</i> cells, implying that PRKN is required for MEC differentiation. These studies suggest a novel regulation of MEC differentiation through programmed mitophagy and provide a foundation for future studies of development and disease associated with mitochondrial function in the mammary gland. <b>Abbreviations</b>: AA: antimycin A; ATG5: autophagy related 5; BAF: bafilomycin A<sub>1</sub>; BNIP3: BCL2 interacting protein 3; BNIP3L/NIX: BCL2 interacting protein 3 like; COX8A: cytochrome c oxidase subunit 8A; CQ: chloroquine; CSN2: casein beta; ECAR: extracellular acidification rate; FCCP: trifluoromethoxy carbonylcyanide phenylhydrazone; FUNDC1: FUN14 domain containing 1; HIF1A: hypoxia inducible factor 1 subunit alpha; L1: lactation day 1; MAP1LC3B: microtubule associated protein 1 light chain 3 beta; MEC: mammary epithelial cell; mitoQ: mitoquinol; mROS: mitochondrial reactive oxygen species; OCR: oxygen consumption rate; P: priming; P16: pregnancy day 16; PARP1: poly(ADP-ribose) polymerase 1; PINK1: PTEN induced kinase 1; PPARGC1A: PPARG coactivator 1 alpha; PRKN: parkin RBR E3 ubiquitin protein ligase; <i>shNT</i>: short hairpin non-targeting control; SQSTM1: sequestosome 1; STAT3: signal transducer and activator of transcription 3; TEM: transmission electron microscopy; TFAM: transcription factor A, mitochondrial; U: undifferentiated.
DOI: 10.6084/m9.figshare.11880732.v1
title: Trehalose limits opportunistic mycobacterial survival during HIV co-infection by reversing HIV-mediated autophagy block

description: Opportunistic bacterial infections amongst HIV–infected individuals contribute significantly to HIV-associated mortality. The role of HIV-mediated modulation of innate mechanisms like autophagy in promoting opportunistic infections, however, remains obscure. Here we show, HIV reactivation in or infection of macrophages inhibits autophagy and helps the survival of pathogenic <i>Mycobacterium tuberculosis (Mtb)</i> and nonpathogenic non-tuberculous mycobacterial strains (NTMs). The HIV-mediated impairment of xenophagy flux facilitated bacterial survival. Activation of autophagy by trehalose could induce xenophagy flux and kill intracellular <i>Mtb</i> or NTMs either during single or co-infections. Trehalose, we delineate, activates PIKFYVE leading to TFEB nuclear translocation in MCOLN1-dependent manner to induce autophagy. Remarkably, trehalose significantly reduced HIV-p24 levels in <i>ex–vivo</i>-infected PBMCs or PBMCs from treatment-naive HIV patients and also controlled mycobacterial survival within <i>Mtb</i>-infected animals. To conclude, we report leveraging of HIV-mediated perturbed host innate-immunity by opportunistic bacterial pathogens and show an attractive therapeutic strategy for HIV and associated co-morbidities. <b>Abbreviations:</b> AIDS: acquired immune deficiency syndrome; AMPK: AMP-activated protein kinase; ATG5: autophagy related 5; BafA1: bafilomycin A<sub>1</sub>; CFU: colony forming unit; CTSD: cathepsin D; CD63: CD63 molecule; EGFP: enhanced green fluorescent protein; FRET: Förster resonance energy transfer; GABARAP: gamma-aminobutyric acid receptor-associated protein; GAPDH: glyceraldehyde 3-phosphate dehydrogenase; GLUT: glucose transporter; HIV: human immunodeficiency virus; hMDMs: human monocyte derived macrophages; IL2: interleukin 2; LAMP1: lysosomal-associated membrane protein 1; LC3B-II: lipidated microtubule-associated proteins 1A/1B light chain 3B; Mtb: <i>Mycobacterium tuberculosis</i>; MTOR: mechanistic target of rapamycin; mRFP: monomeric red fluorescent protein; M6PR: mannose-6-phosphate receptor; NAC: N- acetyl- L –cysteine; NTM’s: non-tuberculous mycobacteria; PBMC: Peripheral Blood Mononuclear cells; PIKFYVE: phosphoinositide kinase; FYVE-Type Zinc Finger; PHA: phytohemagglutinin; PMA: phorbol 12-myristate 13-acetate; PtdIns(3,5)P2: Phosphatidylinositol 3,5-bisphosphate; <i>ptfLC3: pEGFP-mRFP-LC3</i>; ROS: reactive oxygen species; SQSTM1: sequestosome1; TFEB: transcription factor EB; MCOLN1/TRPML1: mucolipin 1; PIP4P1/TMEM55B: Human trans-membrane Protein 55B; UVRAG: UV Radiation Resistance Associate; VPS35: vacuolar protein sorting associated protein 35; WDR45: WD repeat domain 45; YCAM: Yellow Chameleon.