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  1. Article ; Online: Proteome Wide Profiling of

    Marakasova, Ekaterina / Ii, Alexandra / Nelson, Kristina T / van Hoek, Monique L

    Journal of proteome research

    2020  Volume 19, Issue 4, Page(s) 1409–1422

    Abstract: Francisella ... ...

    Abstract Francisella tularensis
    MeSH term(s) Acetylation ; Chitinases ; Francisella ; Lysine ; Protein Processing, Post-Translational ; Proteome/genetics ; Proteome/metabolism
    Chemical Substances Proteome ; Chitinases (EC 3.2.1.14) ; Lysine (K3Z4F929H6)
    Language English
    Publishing date 2020-03-04
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2078618-9
    ISSN 1535-3907 ; 1535-3893
    ISSN (online) 1535-3907
    ISSN 1535-3893
    DOI 10.1021/acs.jproteome.9b00512
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 6189: Show issues Location:
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  2. Article ; Online: Immune recognition of salivary proteins from the cattle tick Rhipicephalus microplus differs according to the genotype of the bovine host.

    Garcia, Gustavo Rocha / Maruyama, Sandra Regina / Nelson, Kristina T / Ribeiro, José Marcos Chaves / Gardinassi, Luiz Gustavo / Maia, Antonio Augusto Mendes / Ferreira, Beatriz Rossetti / Kooyman, Frans N J / de Miranda Santos, Isabel K F

    Parasites & vectors

    2017  Volume 10, Issue 1, Page(s) 144

    Abstract: Background: Males of the cattle tick Rhipicephalus microplus produce salivary immunoglobulin-binding proteins and allotypic variations in IgG are associated with tick loads in bovines. These findings indicate that antibody responses may be essential to ... ...

    Abstract Background: Males of the cattle tick Rhipicephalus microplus produce salivary immunoglobulin-binding proteins and allotypic variations in IgG are associated with tick loads in bovines. These findings indicate that antibody responses may be essential to control tick infestations. Infestation loads with cattle ticks are heritable: some breeds carry high loads of reproductively successful ticks, in others, few ticks feed and they reproduce inefficiently. Different patterns of humoral immunity against tick salivary proteins may explain these phenotypes.
    Methods: We describe the profiles of humoral responses against tick salivary proteins elicited during repeated artificial infestations of bovines of a tick-resistant (Nelore) and a tick-susceptible (Holstein) breed. We measured serum levels of total IgG1, IgG2 and IgE immunoglobulins and of IgG1 and IgG2 antibodies specific for tick salivary proteins. With liquid chromatography followed by mass spectrometry we identified tick salivary proteins that were differentially recognized by serum antibodies from tick-resistant and tick-susceptible bovines in immunoblots of tick salivary proteins separated by two-dimensional electrophoresis.
    Results: Baseline levels of total IgG1 and IgG2 were significantly higher in tick-susceptible Holsteins compared with resistant Nelores. Significant increases in levels of total IgG1, but not of IgG2 accompanied successive infestations in both breeds. Resistant Nelores presented with significantly higher levels of salivary-specific antibodies before and at the first challenge with tick larvae; however, by the third challenge, tick-susceptible Holsteins presented with significantly higher levels of IgG1 and IgG2 tick salivary protein-specific antibodies. Importantly, sera from tick-resistant Nelores reacted with 39 tick salivary proteins in immunoblots of salivary proteins separated in two dimensions by electrophoresis versus only 21 spots reacting with sera from tick-susceptible Holsteins.
    Conclusions: Levels of tick saliva-specific antibodies were not directly correlated with infestation phenotypes. However, in spite of receiving apparently lower amounts of tick saliva, tick-resistant bovines recognized more tick salivary proteins. These reactive salivary proteins are putatively involved in several functions of parasitism and blood-feeding. Our results indicate that neutralization by host antibodies of tick salivary proteins involved in parasitism is essential to control tick infestations.
    MeSH term(s) Animals ; Arthropod Proteins/immunology ; Cattle ; Cattle Diseases/blood ; Cattle Diseases/genetics ; Cattle Diseases/immunology ; Female ; Genotype ; Male ; Rhipicephalus/genetics ; Rhipicephalus/immunology ; Salivary Proteins and Peptides/immunology ; Tick Infestations/genetics ; Tick Infestations/immunology ; Tick Infestations/parasitology ; Tick Infestations/veterinary
    Chemical Substances Arthropod Proteins ; Salivary Proteins and Peptides
    Language English
    Publishing date 2017-03-14
    Publishing country England
    Document type Journal Article
    ZDB-ID 2409480-8
    ISSN 1756-3305 ; 1756-3305
    ISSN (online) 1756-3305
    ISSN 1756-3305
    DOI 10.1186/s13071-017-2077-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Mechanism of endogenous regulation of the type I interferon response by suppressor of IκB kinase epsilon (SIKE), a novel substrate of TANK-binding kinase 1 (TBK1).

    Marion, James D / Roberts, Charlotte F / Call, R Jason / Forbes, Jonathan L / Nelson, Kristina T / Bell, J Ellis / Bell, Jessica K

    The Journal of biological chemistry

    2013  Volume 288, Issue 25, Page(s) 18612–18623

    Abstract: TANK-binding kinase 1 (TBK1) serves as a key convergence point in multiple innate immune signaling pathways. In response to receptor-mediated pathogen detection, TBK1 phosphorylation promotes production of pro-inflammatory cytokines and type I ... ...

    Abstract TANK-binding kinase 1 (TBK1) serves as a key convergence point in multiple innate immune signaling pathways. In response to receptor-mediated pathogen detection, TBK1 phosphorylation promotes production of pro-inflammatory cytokines and type I interferons. Increasingly, TBK1 dysregulation has been linked to autoimmune disorders and cancers, heightening the need to understand the regulatory controls of TBK1 activity. Here, we describe the mechanism by which suppressor of IKKε (SIKE) inhibits TBK1-mediated phosphorylation of interferon regulatory factor 3 (IRF3), which is essential to type I interferon production. Kinetic analyses showed that SIKE not only inhibits IRF3 phosphorylation but is also a high affinity TBK1 substrate. With respect to IRF3 phosphorylation, SIKE functioned as a mixed-type inhibitor (K(i, app) = 350 nM) rather than, given its status as a TBK1 substrate, as a competitive inhibitor. TBK1 phosphorylation of IRF3 and SIKE displayed negative cooperativity. Both substrates shared a similar Km value at low substrate concentrations (∼50 nM) but deviated >8-fold at higher substrate concentrations (IRF3 = 3.5 μM; SIKE = 0.4 μM). TBK1-SIKE interactions were modulated by SIKE phosphorylation, clustered in the C-terminal portion of SIKE (Ser-133, -185, -187, -188, -190, and -198). These sites exhibited striking homology to the phosphorylation motif of IRF3. Mutagenic probing revealed that phosphorylation of Ser-185 controlled TBK1-SIKE interactions. Taken together, our studies demonstrate for the first time that SIKE functions as a TBK1 substrate and inhibits TBK1-mediated IRF3 phosphorylation by forming a high affinity TBK1-SIKE complex. These findings provide key insights into the endogenous control of a critical catalytic hub that is achieved not by direct repression of activity but by redirection of catalysis through substrate affinity.
    MeSH term(s) Algorithms ; Amino Acid Sequence ; Binding Sites/genetics ; Cell Line, Tumor ; HEK293 Cells ; Humans ; Immunoblotting ; Interferon Regulatory Factor-3/genetics ; Interferon Regulatory Factor-3/metabolism ; Interferon Type I/metabolism ; Interferon-alpha/metabolism ; Interferon-beta/metabolism ; Intracellular Signaling Peptides and Proteins/genetics ; Intracellular Signaling Peptides and Proteins/metabolism ; Kinetics ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Serine/genetics ; Serine/metabolism ; Signal Transduction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Substrate Specificity ; Transfection
    Chemical Substances Interferon Regulatory Factor-3 ; Interferon Type I ; Interferon-alpha ; Intracellular Signaling Peptides and Proteins ; SIKE1 protein, human ; Serine (452VLY9402) ; Interferon-beta (77238-31-4) ; Protein-Serine-Threonine Kinases (EC 2.7.11.1) ; TBK1 protein, human (EC 2.7.11.1)
    Language English
    Publishing date 2013-05-06
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 2997-x
    ISSN 1083-351X ; 0021-9258
    ISSN (online) 1083-351X
    ISSN 0021-9258
    DOI 10.1074/jbc.M112.440859
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Proteomic analysis of Anaplasma phagocytophilum during infection of human myeloid cells identifies a protein that is pronouncedly upregulated on the infectious dense-cored cell.

    Troese, Matthew J / Kahlon, Amandeep / Ragland, Stephanie A / Ottens, Andrew K / Ojogun, Nore / Nelson, Kristina T / Walker, Naomi J / Borjesson, Dori L / Carlyon, Jason A

    Infection and immunity

    2011  Volume 79, Issue 11, Page(s) 4696–4707

    Abstract: Anaplasma phagocytophilum is an obligate intracellular bacterium that invades neutrophils to cause the emerging infectious disease human granulocytic anaplasmosis. A. phagocytophilum undergoes a biphasic developmental cycle, transitioning between an ... ...

    Abstract Anaplasma phagocytophilum is an obligate intracellular bacterium that invades neutrophils to cause the emerging infectious disease human granulocytic anaplasmosis. A. phagocytophilum undergoes a biphasic developmental cycle, transitioning between an infectious dense-cored cell (DC) and a noninfectious reticulate cell (RC). To gain insights into the organism's biology and pathogenesis during human myeloid cell infection, we conducted proteomic analyses on A. phagocytophilum organisms purified from HL-60 cells. A total of 324 proteins were unambiguously identified, thereby verifying 23.7% of the predicted A. phagocytophilum proteome. Fifty-three identified proteins had been previously annotated as hypothetical or conserved hypothetical. The second most abundant gene product, after the well-studied major surface protein 2 (P44), was the hitherto hypothetical protein APH_1235. APH_1235 homologs are found in other Anaplasma and Ehrlichia species but not in other bacteria. The aph_1235 RNA level is increased 70-fold in the DC form relative to that in the RC form. Transcriptional upregulation of and our ability to detect APH_1235 correlate with RC to DC transition, DC exit from host cells, and subsequent DC binding and entry during the next round of infection. Immunoelectron microscopy pronouncedly detects APH_1235 on DC organisms, while detection on RC bacteria minimally, at best, exceeds background. This work represents an extensive study of the A. phagocytophilum proteome, discerns the complement of proteins that is generated during survival within human myeloid cells, and identifies APH_1235 as the first known protein that is pronouncedly upregulated on the infectious DC form.
    MeSH term(s) Amino Acid Sequence ; Anaplasma phagocytophilum/genetics ; Anaplasma phagocytophilum/metabolism ; Bacterial Proteins/chemistry ; Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Centrifugation, Density Gradient ; Chromatography, Liquid ; Ehrlichia/genetics ; Ehrlichia/metabolism ; Gene Expression Profiling ; Gene Expression Regulation, Bacterial/physiology ; HL-60 Cells ; Humans ; Molecular Sequence Annotation ; Myeloid Cells/microbiology ; Myeloid Cells/ultrastructure ; Proteomics ; Species Specificity ; Tandem Mass Spectrometry ; Up-Regulation
    Chemical Substances Bacterial Proteins
    Language English
    Publishing date 2011-08-15
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural
    ZDB-ID 218698-6
    ISSN 1098-5522 ; 0019-9567
    ISSN (online) 1098-5522
    ISSN 0019-9567
    DOI 10.1128/IAI.05658-11
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Zs.A 684: Show issues Location:
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