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Article ; Online: Select targeting of intracellular Toll-interleukin-1 receptor resistance domains for protection against influenza-induced disease.

Shirey, Kari Ann / Lai, Wendy / Brown, Lindsey J / Blanco, Jorge C G / Beadenkopf, Robert / Wang, Yajing / Vogel, Stefanie N / Snyder, Greg A

Innate immunity

2019 Volume 26, Issue 1, Page(s) 26–34

MeSH term(s)	Animals ; Crystallography, X-Ray ; Cysteine/genetics ; HEK293 Cells ; Humans ; Immunity, Innate ; Influenza A Virus, H1N1 Subtype/physiology ; Influenza, Human/drug therapy ; Influenza, Human/immunology ; Mice ; Mice, Inbred C57BL ; Models, Molecular ; Mutation/genetics ; Orthomyxoviridae Infections/drug therapy ; Orthomyxoviridae Infections/immunology ; Protein Conformation ; Protein Domains/genetics ; Sulfonamides/pharmacology ; Sulfonamides/therapeutic use ; Toll-Like Receptor 4/antagonists & inhibitors ; Toll-Like Receptor 4/genetics ; Toll-Like Receptor 4/metabolism
Chemical Substances	Sulfonamides ; Toll-Like Receptor 4 ; ethyl 6-(N-(2-chloro-4-fluorophenyl)sulfamoyl)cyclohex-1-ene-1-carboxylate ; Cysteine (K848JZ4886)
Language	English
Publishing date	2019-12-18
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2381250-3
ISSN	1753-4267 ; 1753-4259
ISSN (online)	1753-4267
ISSN	1753-4259
DOI	10.1177/1753425919846281
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: p47 licenses activation of the immune deficiency pathway in the tick

McClure Carroll, Erin E / Wang, Xiaowei / Shaw, Dana K / O'Neal, Anya J / Oliva Chávez, Adela S / Brown, Lindsey J / Boradia, Vishant Mahendra / Hammond, Holly L / Pedra, Joao H F

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

2018 Volume 116, Issue 1, Page(s) 205–210

Abstract: The E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) acts as a molecular rheostat for the immune deficiency (IMD) pathway of the ... ...

Abstract	The E3 ubiquitin ligase X-linked inhibitor of apoptosis (XIAP) acts as a molecular rheostat for the immune deficiency (IMD) pathway of the tick
MeSH term(s)	Adaptor Proteins, Signal Transducing/metabolism ; Adaptor Proteins, Signal Transducing/physiology ; Anaplasma ; Animals ; Arthropod Proteins/metabolism ; Arthropod Proteins/physiology ; Borrelia burgdorferi ; Drosophila ; Gene Knockout Techniques ; Ixodes/immunology ; Ixodes/microbiology ; Ixodes/physiology ; NF-kappa B/metabolism ; Protein Domains ; X-Linked Inhibitor of Apoptosis Protein/metabolism ; X-Linked Inhibitor of Apoptosis Protein/physiology
Chemical Substances	Adaptor Proteins, Signal Transducing ; Arthropod Proteins ; NF-kappa B ; X-Linked Inhibitor of Apoptosis Protein
Language	English
Publishing date	2018-12-17
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	209104-5
ISSN	1091-6490 ; 0027-8424
ISSN (online)	1091-6490
ISSN	0027-8424
DOI	10.1073/pnas.1808905116
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Article ; Online: Using S-adenosyl-L-homocysteine capture compounds to characterize S-adenosyl-L-methionine and S-adenosyl-L-homocysteine binding proteins.

Brown, Lindsey J / Baranowski, Matthias / Wang, Yun / Schrey, Anna K / Lenz, Thomas / Taverna, Sean D / Cole, Philip A / Sefkow, Michael

Analytical biochemistry

2014 Volume 467, Page(s) 14–21

Abstract: S-Adenosyl-l-methionine (SAM) is recognized as an important cofactor in a variety of biochemical reactions. As more proteins and pathways that require SAM are discovered, it is important to establish a method to quickly identify and characterize SAM ... ...

Abstract	S-Adenosyl-l-methionine (SAM) is recognized as an important cofactor in a variety of biochemical reactions. As more proteins and pathways that require SAM are discovered, it is important to establish a method to quickly identify and characterize SAM binding proteins. The affinity of S-adenosyl-l-homocysteine (SAH) for SAM binding proteins was used to design two SAH-derived capture compounds (CCs). We demonstrate interactions of the proteins COMT and SAHH with SAH-CC with biotin used in conjunction with streptavidin-horseradish peroxidase. After demonstrating SAH-dependent photo-crosslinking of the CC to these proteins, we used a CC labeled with a fluorescein tag to measure binding affinity via fluorescence anisotropy. We then used this approach to show and characterize binding of SAM to the PR domain of PRDM2, a lysine methyltransferase with putative tumor suppressor activity. We calculated the Kd values for COMT, SAHH, and PRDM2 (24.1 ± 2.2 μM, 6.0 ± 2.9 μM, and 10.06 ± 2.87 μM, respectively) and found them to be close to previously established Kd values of other SAM binding proteins. Here, we present new methods to discover and characterize SAM and SAH binding proteins using fluorescent CCs.
MeSH term(s)	Catechol O-Methyltransferase/analysis ; Catechol O-Methyltransferase/metabolism ; DNA-Binding Proteins/analysis ; DNA-Binding Proteins/metabolism ; Fluorescence Polarization/methods ; Histone-Lysine N-Methyltransferase/analysis ; Histone-Lysine N-Methyltransferase/metabolism ; Humans ; Hydrolases/analysis ; Hydrolases/metabolism ; Nuclear Proteins/analysis ; Nuclear Proteins/metabolism ; S-Adenosylhomocysteine/metabolism ; S-Adenosylmethionine/metabolism ; Transcription Factors/analysis ; Transcription Factors/metabolism
Chemical Substances	DNA-Binding Proteins ; Nuclear Proteins ; Transcription Factors ; S-Adenosylmethionine (7LP2MPO46S) ; S-Adenosylhomocysteine (979-92-0) ; Histone-Lysine N-Methyltransferase (EC 2.1.1.43) ; PRDM2 protein, human (EC 2.1.1.43) ; COMT protein, human (EC 2.1.1.6) ; Catechol O-Methyltransferase (EC 2.1.1.6) ; Hydrolases (EC 3.-) ; adenosylmethionine hydrolase (EC 3.3.1.2)
Language	English
Publishing date	2014-08-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2014.08.013
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Article: Using S-adenosyl-l-homocysteine capture compounds to characterize S-adenosyl-l-methionine and S-adenosyl-l-homocysteine binding proteins

Brown, Lindsey J / Baranowski, Matthias / Wang, Yun / Schrey, Anna K / Lenz, Thomas / Taverna, Sean D / Cole, Philip A / Sefkow, Michael

Analytical biochemistry. 2014 Dec. 15, v. 467

2014

Abstract	S-Adenosyl-l-methionine (SAM) is recognized as an important cofactor in a variety of biochemical reactions. As more proteins and pathways that require SAM are discovered, it is important to establish a method to quickly identify and characterize SAM binding proteins. The affinity of S-adenosyl-l-homocysteine (SAH) for SAM binding proteins was used to design two SAH-derived capture compounds (CCs). We demonstrate interactions of the proteins COMT and SAHH with SAH–CC with biotin used in conjunction with streptavidin–horseradish peroxidase. After demonstrating SAH-dependent photo-crosslinking of the CC to these proteins, we used a CC labeled with a fluorescein tag to measure binding affinity via fluorescence anisotropy. We then used this approach to show and characterize binding of SAM to the PR domain of PRDM2, a lysine methyltransferase with putative tumor suppressor activity. We calculated the Kd values for COMT, SAHH, and PRDM2 (24.1±2.2μM, 6.0±2.9μM, and 10.06±2.87μM, respectively) and found them to be close to previously established Kd values of other SAM binding proteins. Here, we present new methods to discover and characterize SAM and SAH binding proteins using fluorescent CCs.
Keywords	S-adenosylmethionine ; anisotropy ; binding capacity ; binding proteins ; biotin ; chemical reactions ; fluorescein ; fluorescence ; methyltransferases ; peroxidase
Language	English
Dates of publication	2014-1215
Size	p. 14-21.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1110-1
ISSN	1096-0309 ; 0003-2697
ISSN (online)	1096-0309
ISSN	0003-2697
DOI	10.1016/j.ab.2014.08.013
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Article ; Online: Infection-derived lipids elicit an immune deficiency circuit in arthropods.

Nature communications

2017 Volume 8, Page(s) 14401

Abstract: The insect immune deficiency (IMD) pathway resembles the tumour necrosis factor receptor network in mammals and senses diaminopimelic-type peptidoglycans present in Gram-negative bacteria. Whether unidentified chemical moieties activate the IMD ... ...

Abstract	The insect immune deficiency (IMD) pathway resembles the tumour necrosis factor receptor network in mammals and senses diaminopimelic-type peptidoglycans present in Gram-negative bacteria. Whether unidentified chemical moieties activate the IMD signalling cascade remains unknown. Here, we show that infection-derived lipids 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphoglycerol (POPG) and 1-palmitoyl-2-oleoyl diacylglycerol (PODAG) stimulate the IMD pathway of ticks. The tick IMD network protects against colonization by three distinct bacteria, that is the Lyme disease spirochete Borrelia burgdorferi and the rickettsial agents Anaplasma phagocytophilum and A. marginale. Cell signalling ensues in the absence of transmembrane peptidoglycan recognition proteins and the adaptor molecules Fas-associated protein with a death domain (FADD) and IMD. Conversely, biochemical interactions occur between x-linked inhibitor of apoptosis protein (XIAP), an E3 ubiquitin ligase, and the E2 conjugating enzyme Bendless. We propose the existence of two functionally distinct IMD networks, one in insects and another in ticks.
MeSH term(s)	Adaptor Proteins, Signal Transducing/genetics ; Adaptor Proteins, Signal Transducing/metabolism ; Anaplasma marginale/immunology ; Anaplasma marginale/pathogenicity ; Anaplasma phagocytophilum/immunology ; Anaplasma phagocytophilum/pathogenicity ; Animals ; Arthropods/immunology ; Arthropods/metabolism ; Borrelia burgdorferi/immunology ; Borrelia burgdorferi/pathogenicity ; Carrier Proteins ; Disease Models, Animal ; Drosophila Proteins/genetics ; Drosophila Proteins/metabolism ; Drosophila melanogaster/metabolism ; Escherichia coli/genetics ; Fas-Associated Death Domain Protein ; Gene Silencing ; HEK293 Cells ; Humans ; Immunologic Deficiency Syndromes/immunology ; Immunologic Deficiency Syndromes/veterinary ; Ixodes/immunology ; Ixodes/metabolism ; Lipids/adverse effects ; Lipids/immunology ; Lyme Disease/immunology ; Phosphatidylglycerols/immunology ; RNA, Small Interfering/metabolism ; Recombinant Proteins ; Signal Transduction ; Transcription Factors/genetics ; Transcription Factors/metabolism ; Ubiquitin-Conjugating Enzymes/genetics ; Ubiquitin-Conjugating Enzymes/metabolism ; Ubiquitin-Protein Ligases/metabolism ; X-Linked Inhibitor of Apoptosis Protein/metabolism
Chemical Substances	Adaptor Proteins, Signal Transducing ; Carrier Proteins ; Drosophila Proteins ; Fas-Associated Death Domain Protein ; Lipids ; Phosphatidylglycerols ; RNA, Small Interfering ; Recombinant Proteins ; Rel protein, Drosophila ; Transcription Factors ; X-Linked Inhibitor of Apoptosis Protein ; casp protein, Drosophila ; peptidoglycan recognition protein ; 1-palmitoyl-2-oleoylglycero-3-phosphoglycerol (81490-05-3) ; Ubiquitin-Conjugating Enzymes (EC 2.3.2.23) ; Uev1a protein, Drosophila (EC 2.3.2.23) ; ben protein, Drosophila (EC 2.3.2.23) ; Ubiquitin-Protein Ligases (EC 2.3.2.27)
Language	English
Publishing date	2017-02-14
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	2553671-0
ISSN	2041-1723 ; 2041-1723
ISSN (online)	2041-1723
ISSN	2041-1723
DOI	10.1038/ncomms14401
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Article ; Online: The tick salivary protein sialostatin L2 inhibits caspase-1-mediated inflammation during Anaplasma phagocytophilum infection.

Chen, Gang / Wang, Xiaowei / Severo, Maiara S / Sakhon, Olivia S / Sohail, Mohammad / Brown, Lindsey J / Sircar, Mayukh / Snyder, Greg A / Sundberg, Eric J / Ulland, Tyler K / Olivier, Alicia K / Andersen, John F / Zhou, Yi / Shi, Guo-Ping / Sutterwala, Fayyaz S / Kotsyfakis, Michail / Pedra, Joao H F

Infection and immunity

2014 Volume 82, Issue 6, Page(s) 2553–2564

Abstract: Saliva from arthropod vectors facilitates blood feeding by altering host inflammation. Whether arthropod saliva counters inflammasome signaling, a protein scaffold that regulates the activity of caspase-1 and cleavage of interleukin-1β (IL-1β) and IL-18 ... ...

Abstract	Saliva from arthropod vectors facilitates blood feeding by altering host inflammation. Whether arthropod saliva counters inflammasome signaling, a protein scaffold that regulates the activity of caspase-1 and cleavage of interleukin-1β (IL-1β) and IL-18 into mature molecules, remains elusive. In this study, we provide evidence that a tick salivary protein, sialostatin L2, inhibits inflammasome formation during pathogen infection. We show that sialostatin L2 targets caspase-1 activity during host stimulation with the rickettsial agent Anaplasma phagocytophilum. A. phagocytophilum causes macrophage activation and hemophagocytic syndrome features. The effect of sialostatin L2 in macrophages was not due to direct caspase-1 enzymatic inhibition, and it did not rely on nuclear factor κB or cathepsin L signaling. Reactive oxygen species from NADPH oxidase and the Loop2 domain of sialostatin L2 were important for the regulatory process. Altogether, our data expand the knowledge of immunoregulatory pathways of tick salivary proteins and unveil an important finding in inflammasome biology.
MeSH term(s)	Analysis of Variance ; Anaplasma phagocytophilum/physiology ; Animals ; Caspase 1/metabolism ; Cells, Cultured ; Cytokines/metabolism ; Disease Models, Animal ; Ehrlichiosis/metabolism ; Ehrlichiosis/microbiology ; Ehrlichiosis/pathology ; Inflammasomes/metabolism ; Inflammation/physiopathology ; Macrophages/metabolism ; Macrophages/microbiology ; Mice ; Mice, Inbred C57BL ; Reactive Oxygen Species ; Salivary Cystatins/physiology
Chemical Substances	Cytokines ; Inflammasomes ; Reactive Oxygen Species ; Salivary Cystatins ; Caspase 1 (EC 3.4.22.36)
Language	English
Publishing date	2014-03-31
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	218698-6
ISSN	1098-5522 ; 0019-9567
ISSN (online)	1098-5522
ISSN	0019-9567
DOI	10.1128/IAI.01679-14
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Article ; Online: Epigenetic specificity of loss of imprinting of the IGF2 gene in Wilms tumors.

Bjornsson, Hans T / Brown, Lindsey J / Fallin, M Danielle / Rongione, Michael A / Bibikova, Marina / Wickham, Eliza / Fan, Jian-Bing / Feinberg, Andrew P

Journal of the National Cancer Institute

2007 Volume 99, Issue 16, Page(s) 1270–1273

Abstract: Loss of imprinting (LOI) of the IGF2 gene (which encodes insulin-like growth factor II) is the most common genetic or epigenetic alteration in Wilms tumor; LOI involves aberrant activation of the normally repressed maternally inherited allele. We found ... ...

Abstract	Loss of imprinting (LOI) of the IGF2 gene (which encodes insulin-like growth factor II) is the most common genetic or epigenetic alteration in Wilms tumor; LOI involves aberrant activation of the normally repressed maternally inherited allele. We found previously that LOI of IGF2 occurs in approximately half of all Wilms tumors (i.e., those arising from lineage-committed nephrogenic progenitor cells). We investigated whether LOI of IGF2 is associated with relaxation of imprinting at loci other than IGF2 or with widespread alterations in DNA methylation. We stratified 59 Wilms tumor samples by IGF2 LOI status by use of hot-stop reverse transcription-polymerase chain reaction and/or methylation analysis of the differentially methylated region of the H19 gene and identified 31 samples with and 28 without LOI. We used quantitative allele-specific expression analysis to determine whether six other imprinted genes (i.e., H19, KCNQ1, LIT1, TSSC5, GRB10, and MEG3) had subtle LOI. No statistically significant difference in allele-specific expression between Wilms tumor with or without LOI was found for LIT1, TSSC5, GRB10, and MEG3. For the KCNQ1 gene there was a slight difference between the groups with (37.0%, 95% confidence interval [CI] = 31.8% to 42.2%) and without (27.7%, 95% CI = 21.8% to 33.5%) LOI (P = .02 for F test of group differences in a mixed-effects model). For H19, we also found a slight difference between the groups with (7.5%, 95% CI = 2.4% to 12.7%) and without (2.2%, 95% CI = -3.2% to 7.6%) LOI of IGF2 (P = .15 for F test). In 27 tumor samples, we also used a microarray technique to analyze methylation of 378 genes, 38 of which were suspected or confirmed imprinted genes. We found that statistically significant alterations in only the differentially methylated region of the H19 gene were associated with LOI of IGF2. Thus, epigenetic alterations in Wilms tumors are not widespread, supporting the gene and lineage specificity of LOI of IGF2.
MeSH term(s)	DNA Methylation ; Gene Expression Regulation, Neoplastic ; Genomic Imprinting ; Humans ; Insulin-Like Growth Factor II/genetics ; Wilms Tumor/genetics
Chemical Substances	Insulin-Like Growth Factor II (67763-97-7)
Language	English
Publishing date	2007-08-15
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	2992-0
ISSN	1460-2105 ; 0027-8874 ; 0198-0157
ISSN (online)	1460-2105
ISSN	0027-8874 ; 0198-0157
DOI	10.1093/jnci/djm069
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Article: A histological survey of green fluorescent protein expression in 'green' mice: implications for stem cell research.

Biankin, Sandra A / Collector, Michael I / Biankin, Andrew V / Brown, Lindsey J / Kleeberger, Wolfram / Devereux, Wendy L / Zahnow, Cynthia A / Baylin, Stephen B / Watkins, D Neil / Sharkis, Saul J / Leach, Steven D

Pathology

2007 Volume 39, Issue 2, Page(s) 247–251

Abstract: Aims: The transgenic enhanced green fluorescent protein (EGFP) expressing 'green' mouse (C57BL/6-TgN(ACTbEGFP)1Osb) is a widely used tool in stem cell research, where the ubiquitous nature of EGFP expression is critical to track the fate of single or ... ...

Abstract	Aims: The transgenic enhanced green fluorescent protein (EGFP) expressing 'green' mouse (C57BL/6-TgN(ACTbEGFP)1Osb) is a widely used tool in stem cell research, where the ubiquitous nature of EGFP expression is critical to track the fate of single or small groups of transplanted haematopoietic stem cells (HSC). Our aim was to investigate this assumed ubiquitous expression by performing a detailed histological survey of EGFP expression in these mice. Methods: Fluorescent microscopy of frozen tissue sections was used to perform a detailed histological survey of the pattern of EGFP expression in these mice. Flow cytometry was also used to determine the expression pattern in blood and bone marrow. Results: Three patterns of EGFP expression were noted. In most tissues there was an apparently stochastic variegation of the transgene, with individual cell types demonstrating highly variable rates of EGFP expression. Certain specific cell types such as pancreatic ductal epithelium, cerebral cortical neurones and glial cells and glomerular mesangial cells consistently lacked EGFP expression, while others, including pancreatic islet cells, expressed EGFP only at extremely low levels, barely distinguishable from background. Lastly, in the colon and stomach the pattern of EGFP expression was suggestive of clonal inactivation. Only cardiac and skeletal muscle showed near ubiquitous expression. Conclusions: These findings raise questions regarding the 'ubiquitous' expression of EGFP in these transgenic mice and suggest caution in relying overly on EGFP alone as an infallible marker of donor cell origin.
MeSH term(s)	Animals ; Biomedical Research/methods ; Cell Lineage ; Flow Cytometry ; Fluorescent Antibody Technique ; Green Fluorescent Proteins/biosynthesis ; Green Fluorescent Proteins/genetics ; Mice ; Mice, Transgenic ; Microscopy, Fluorescence ; Models, Animal ; Stem Cells
Chemical Substances	Green Fluorescent Proteins (147336-22-9)
Language	English
Publishing date	2007-04
Publishing country	England
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	7085-3
ISSN	1465-3931 ; 0031-3025
ISSN (online)	1465-3931
ISSN	0031-3025
DOI	10.1080/00313020701230807
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