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Book: Alphaherpesviruses

Weller, Sandra K.

molecular virology

2011

Author's details	ed. by Sandra K. Weller
Language	English
Size	X, 448 S. : Ill., graph. Darst.
Publisher	Caister
Publishing place	Norfolk
Publishing country	Great Britain
Document type	Book
HBZ-ID	HT016399238
ISBN	978-1-904455-76-9 ; 1-904455-76-X
Database	Catalogue ZB MED Medicine, Health

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Article ; Online: Retracer l’origine des réponses immunitaires indépendantes des lymphocytes T chez l’homme.

Weller, Sandra / Weill, Jean-Claude / Reynaud, Claude-Agnès

Medecine sciences : M/S

2023 Volume 39, Issue 6-7, Page(s) 490–492

Title translation	Tracing the origin of T lymphocyte-independent responses.
MeSH term(s)	Humans ; T-Lymphocytes
Language	French
Publishing date	2023-06-30
Publishing country	France
Document type	Journal Article
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2023068
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Article ; Online: B cell diversification in gut-associated lymphoid tissues: From birds to humans.

Weill, Jean-Claude / Weller, Sandra / Reynaud, Claude-Agnès

The Journal of experimental medicine

2023 Volume 220, Issue 11

Abstract: Several species generate their preimmune repertoire in gut-associated lymphoid tissues (GALT), compensating a reduced germline V gene repertoire by post-rearrangement diversification mechanisms (gene conversion and/or somatic hypermutation) in these ... ...

Abstract	Several species generate their preimmune repertoire in gut-associated lymphoid tissues (GALT), compensating a reduced germline V gene repertoire by post-rearrangement diversification mechanisms (gene conversion and/or somatic hypermutation) in these environments that act as primary lymphoid organs. We summarize here these processes for three different species (chickens, sheep, and rabbits) and further discuss the analogous process that T-independent B cell responses in humans represent: we indeed recently showed that response against bacterial polysaccharides mobilize marginal zone B cells that prediversified against gut antigens. While the initial diversification strategy differs in these two cases, i.e., repertoire formation driven by gut-derived mitotic signals vs. response against gut antigens, the common feature of these two processes is the mobilization of a B cell compartment prediversified in GALT for immune responses against distinct systemic antigens.
MeSH term(s)	Humans ; Animals ; Rabbits ; Sheep/genetics ; Antibody Diversity ; Genes, Immunoglobulin ; Chickens/genetics ; B-Lymphocytes ; Lymphoid Tissue
Language	English
Publishing date	2023-10-12
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218343-2
ISSN	1540-9538 ; 0022-1007
ISSN (online)	1540-9538
ISSN	0022-1007
DOI	10.1084/jem.20231501
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Article ; Online: New model integrates innate responses, PML-NB formation, epigenetic control and reactivation from latency.

Weller, Sandra K / Deluca, Neal A

EMBO reports

2021 Volume 22, Issue 9, Page(s) e53496

Abstract: The dynamic nature of interactions between invading viral pathogens and their hosts has fascinated scientists for several decades. The well-known capacity of herpes simplex virus (HSV) to establish life-long infections in humans reflects a dynamic ... ...

Abstract	The dynamic nature of interactions between invading viral pathogens and their hosts has fascinated scientists for several decades. The well-known capacity of herpes simplex virus (HSV) to establish life-long infections in humans reflects a dynamic balance between maintaining a latent state in which viral genomes are silenced and re-entry into the lytic phase during reactivation. Silencing of the viral genome has been shown to be a function of innate immune signalling, intrinsic cellular antiviral mechanisms and epigenetic repression. Thus, although many important observations have been made identifying cellular processes that contribute to the repression of the viral genome and latency, the field has lacked an understanding of how these factors work together. In this issue of EMBO Reports, Suzich et al (2021) present convincing evidence that brings together individual observations into a cohesive model that explains many of these outstanding mysteries. Here, we will review the background data that lead to this outstanding piece of work.
MeSH term(s)	Epigenetic Repression ; Genome, Viral ; Herpesvirus 1, Human/genetics ; Humans ; Virus Latency/genetics
Language	English
Publishing date	2021-07-27
Publishing country	England
Document type	Journal Article ; Comment
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.15252/embr.202153496
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Book ; Online ; Thesis: Der BCL-2 Inhibitor ABT-199/Venetoclax transaktiviert NOXA und wirkt mit Proteasom-Inhibition bei der Zelltod-Induktion synergistisch

Weller, Sandra [Verfasser] / Rapaport, Doron [Akademischer Betreuer]

2023

Author's details	Sandra Katharina Weller ; Betreuer: Doron Rapaport
Keywords	Naturwissenschaften ; Science
Subject code	sg500
Language	German
Publisher	Universitätsbibliothek Tübingen
Publishing place	Tübingen
Document type	Book ; Online ; Thesis
Database	Digital theses on the web

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Article ; Online: Viral Nucleases from Herpesviruses and Coronavirus in Recombination and Proofreading: Potential Targets for Antiviral Drug Discovery.

Wright, Lee R / Wright, Dennis L / Weller, Sandra K

Viruses

2022 Volume 14, Issue 7

Abstract: In this review, we explore recombination in two very different virus families that have become major threats to human health. The Herpesviridae are a large family of pathogenic double-stranded DNA viruses involved in a range of diseases affecting both ... ...

Abstract	In this review, we explore recombination in two very different virus families that have become major threats to human health. The Herpesviridae are a large family of pathogenic double-stranded DNA viruses involved in a range of diseases affecting both people and animals. Coronaviridae are positive-strand RNA viruses (CoVs) that have also become major threats to global health and economic stability, especially in the last two decades. Despite many differences, such as the make-up of their genetic material (DNA vs. RNA) and overall mechanisms of genome replication, both human herpes viruses (HHVs) and CoVs have evolved to rely heavily on recombination for viral genome replication, adaptation to new hosts and evasion of host immune regulation. In this review, we will focus on the roles of three viral exonucleases: two HHV exonucleases (alkaline nuclease and PolExo) and one CoV exonuclease (ExoN). We will review the roles of these three nucleases in their respective life cycles and discuss the state of drug discovery efforts against these targets.
MeSH term(s)	Animals ; Antiviral Agents/pharmacology ; Antiviral Agents/therapeutic use ; Coronavirus/genetics ; Coronavirus Infections ; Drug Discovery ; Exonucleases ; Humans ; Mutation ; Recombination, Genetic ; Simplexvirus ; Virus Replication
Chemical Substances	Antiviral Agents ; Exonucleases (EC 3.1.-)
Language	English
Publishing date	2022-07-16
Publishing country	Switzerland
Document type	Journal Article ; Review ; Research Support, N.I.H., Extramural
ZDB-ID	2516098-9
ISSN	1999-4915 ; 1999-4915
ISSN (online)	1999-4915
ISSN	1999-4915
DOI	10.3390/v14071557
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Article ; Online: The B-box1 domain of PML mediates SUMO E2-E3 complex formation through an atypical interaction with UBC9.

Bregnard, Thomas / Ahmed, Affrin / Semenova, Irina V / Weller, Sandra K / Bezsonova, Irina

Biophysical chemistry

2022 Volume 287, Page(s) 106827

Abstract: The small, ubiquitin-like modifier SUMO is covalently attached to substrates by the enzyme UBC9. SUMO conjugation of substrates often requires an E3 ligase, which ensures substrate specificity by simultaneously binding UBC9 and the substrate. E3 SUMO ... ...

Abstract	The small, ubiquitin-like modifier SUMO is covalently attached to substrates by the enzyme UBC9. SUMO conjugation of substrates often requires an E3 ligase, which ensures substrate specificity by simultaneously binding UBC9 and the substrate. E3 SUMO ligases commonly use a RING domain to engage UBC9. The Promyelocytic Leukemia protein (PML) has been implicated as a probable SUMO ligase. Although PML does contain a RING domain, which is expected to recruit UBC9, we demonstrate that PML RING does not bind UBC9 in vitro. Instead, we show that isolated PML B-box1 possesses UBC9-binding activity and map the B-box1 binding site on UBC9. This site also binds the upstream E1 enzyme that transfers SUMO to UBC9. The overlap of these two binding sites suggests that UBC9 cannot interact with its E1 and E3 partners simultaneously. Furthermore, we present a model of the PML dimer that supports the accessibility of B-box1 for UBC9 binding in the context of the full-length PML.
MeSH term(s)	Binding Sites ; Substrate Specificity ; Transcription Factors/metabolism ; Ubiquitin/chemistry ; Ubiquitin-Conjugating Enzymes/chemistry ; Ubiquitin-Conjugating Enzymes/metabolism
Chemical Substances	Transcription Factors ; Ubiquitin ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23)
Language	English
Publishing date	2022-05-18
Publishing country	Netherlands
Document type	Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Research Support, N.I.H., Extramural
ZDB-ID	185052-0
ISSN	1873-4200 ; 0301-4622
ISSN (online)	1873-4200
ISSN	0301-4622
DOI	10.1016/j.bpc.2022.106827
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Article ; Online: Conformational exchange at a C

Bregnard, Thomas A / Fairchild, Daniel / Erlandsen, Heidi / Semenova, Irina V / Szczepaniak, Renata / Ahmed, Affrin / Weller, Sandra K / Korzhnev, Dmitry M / Bezsonova, Irina

Structure (London, England : 1993)

2023 Volume 31, Issue 9, Page(s) 1086–1099.e6

Abstract: The promyelocytic leukemia protein, PML, plays a vital role in the cellular response to oxidative stress; however, the molecular mechanism of its action remains poorly understood. Here, we identify redox-sensitive sites of PML. A molecule of PML is ... ...

Abstract	The promyelocytic leukemia protein, PML, plays a vital role in the cellular response to oxidative stress; however, the molecular mechanism of its action remains poorly understood. Here, we identify redox-sensitive sites of PML. A molecule of PML is cysteine-rich and contains three zinc-binding domains including RING, B-box1, and B-box2. Using in vitro assays, we have compared the sensitivity of the isolated RING and B-box1 domains and shown that B-box1 is more sensitive to oxidation. NMR studies of PML dynamics showed that one of the Zn-coordination sites within the B-box1 undergoes significant conformational exchange, revealing a hotspot for exposure of reactive cysteines. In agreement with the in vitro data, enhancement of the B-box1 Zn-coordination dynamics led to more efficient recruitment of PML into PML nuclear bodies in cells. Overall, our results suggest that the increased sensitivity of B-box1 to oxidative stress makes this domain an important redox-sensing component of PML.
MeSH term(s)	Nuclear Proteins/metabolism ; Zinc/metabolism ; Promyelocytic Leukemia Protein/genetics ; Promyelocytic Leukemia Protein/metabolism ; Binding Sites ; Oxidation-Reduction
Chemical Substances	Nuclear Proteins ; Zinc (J41CSQ7QDS) ; Promyelocytic Leukemia Protein
Language	English
Publishing date	2023-07-19
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
ZDB-ID	1213087-4
ISSN	1878-4186 ; 0969-2126
ISSN (online)	1878-4186
ISSN	0969-2126
DOI	10.1016/j.str.2023.06.014
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Article ; Online: ATF3 characterizes aggressive drug-tolerant persister cells in HGSOC.

Böpple, Kathrin / Oren, Yaara / Henry, Whitney S / Dong, Meng / Weller, Sandra / Thiel, Julia / Kleih, Markus / Gaißler, Andrea / Zipperer, Damaris / Kopp, Hans-Georg / Aylon, Yael / Oren, Moshe / Essmann, Frank / Liang, Chunguang / Aulitzky, Walter E

Cell death & disease

2024 Volume 15, Issue 4, Page(s) 290

Abstract: High-grade serous ovarian cancer (HGSOC) represents the most common and lethal subtype of ovarian cancer. Despite initial response to platinum-based standard therapy, patients commonly suffer from relapse that likely originates from drug-tolerant ... ...

Abstract	High-grade serous ovarian cancer (HGSOC) represents the most common and lethal subtype of ovarian cancer. Despite initial response to platinum-based standard therapy, patients commonly suffer from relapse that likely originates from drug-tolerant persister (DTP) cells. We generated isogenic clones of treatment-naïve and cisplatin-tolerant persister HGSOC cells. In addition, single-cell RNA sequencing of barcoded cells was performed in a xenograft model with HGSOC cell lines after platinum-based therapy. Published single-cell RNA-sequencing data from neo-adjuvant and non-treated HGSOC patients and patient data from TCGA were analyzed. DTP-derived cells exhibited morphological alterations and upregulation of epithelial-mesenchymal transition (EMT) markers. An aggressive subpopulation of DTP-derived cells showed high expression of the stress marker ATF3. Knockdown of ATF3 enhanced the sensitivity of aggressive DTP-derived cells to cisplatin-induced cell death, implying a role for ATF3 stress response in promoting a drug tolerant persister cell state. Furthermore, single cell lineage tracing to detect transcriptional changes in a HGSOC cell line-derived xenograft relapse model showed that cells derived from relapsed solid tumors express increased levels of EMT and multiple endoplasmic reticulum (ER) stress markers, including ATF3. Single cell RNA sequencing of epithelial cells from four HGSOC patients also identified a small cell population resembling DTP cells in all samples. Moreover, analysis of TCGA data from 259 HGSOC patients revealed a significant progression-free survival advantage for patients with low expression of the ATF3-associated partial EMT genes. These findings suggest that increased ATF3 expression together with partial EMT promote the development of aggressive DTP, and thereby relapse in HGSOC patients.
MeSH term(s)	Humans ; Activating Transcription Factor 3/metabolism ; Activating Transcription Factor 3/genetics ; Female ; Cisplatin/pharmacology ; Cisplatin/therapeutic use ; Cell Line, Tumor ; Drug Resistance, Neoplasm/genetics ; Drug Resistance, Neoplasm/drug effects ; Epithelial-Mesenchymal Transition/drug effects ; Epithelial-Mesenchymal Transition/genetics ; Ovarian Neoplasms/drug therapy ; Ovarian Neoplasms/genetics ; Ovarian Neoplasms/pathology ; Ovarian Neoplasms/metabolism ; Animals ; Mice ; Xenograft Model Antitumor Assays ; Gene Expression Regulation, Neoplastic/drug effects
Chemical Substances	Activating Transcription Factor 3 ; Cisplatin (Q20Q21Q62J) ; ATF3 protein, human
Language	English
Publishing date	2024-04-24
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't ; Research Support, N.I.H., Extramural
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-024-06674-x
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Article ; Online: The Herpes Simplex Virus 1 Immediate Early Protein ICP22 Is a Functional Mimic of a Cellular J Protein.

Adlakha, Mitali / Livingston, Christine M / Bezsonova, Irina / Weller, Sandra K

Journal of virology

2020 Volume 94, Issue 4

Abstract: Molecular chaperones and cochaperones are the most abundant cellular effectors of protein homeostasis, assisting protein folding and preventing aggregation of misfolded proteins. We have previously shown that herpes simplex virus 1 (HSV-1) infection ... ...

Abstract	Molecular chaperones and cochaperones are the most abundant cellular effectors of protein homeostasis, assisting protein folding and preventing aggregation of misfolded proteins. We have previously shown that herpes simplex virus 1 (HSV-1) infection results in the drastic spatial reorganization of the cellular chaperone Hsc70 into nuclear domains called VICE (
MeSH term(s)	Animals ; Cell Nucleus/metabolism ; Chlorocebus aethiops ; HEK293 Cells ; HSP40 Heat-Shock Proteins/metabolism ; Herpes Simplex/virology ; Herpesvirus 1, Human/metabolism ; Herpesvirus 1, Human/pathogenicity ; Herpesvirus 1, Human/physiology ; Humans ; Immediate-Early Proteins/genetics ; Immediate-Early Proteins/metabolism ; Molecular Chaperones/metabolism ; Phosphorylation ; Protein Folding ; RNA Polymerase II/metabolism ; Vero Cells ; Viral Proteins/metabolism
Chemical Substances	HSP40 Heat-Shock Proteins ; ICP22 protein, human herpesvirus 1 ; Immediate-Early Proteins ; Molecular Chaperones ; Viral Proteins ; RNA Polymerase II (EC 2.7.7.-)
Language	English
Publishing date	2020-01-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.01564-19
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