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  1. Article ; Online: The U1-snRNP complex: structural properties relating to autoimmune pathogenesis in rheumatic diseases.

    Kattah, Nicole H / Kattah, Michael G / Utz, Paul J

    Immunological reviews

    2010  Volume 233, Issue 1, Page(s) 126–145

    Abstract: The U1 small nuclear ribonucleoprotein particle (snRNP) is a target of autoreactive B cells and T cells in several rheumatic diseases including systemic lupus erythematosus (SLE) and mixed connective tissue disease (MCTD). We propose that inherent ... ...

    Abstract The U1 small nuclear ribonucleoprotein particle (snRNP) is a target of autoreactive B cells and T cells in several rheumatic diseases including systemic lupus erythematosus (SLE) and mixed connective tissue disease (MCTD). We propose that inherent structural properties of this autoantigen complex, including common RNA-binding motifs, B and T-cell epitopes, and a unique stimulatory RNA molecule, underlie its susceptibility as a target of the autoimmune response. Immune mechanisms that may contribute to overall U1-snRNP immunogenicity include epitope spreading through B and T-cell interactions, apoptosis-induced modifications, and toll-like receptor (TLR) activation through stimulation by U1-snRNA. We conclude that understanding the interactions between U1-snRNP and the immune system will provide insights into why certain patients develop anti-U1-snRNP autoimmunity, and more importantly how to effectively target therapies against this autoimmune response.
    MeSH term(s) Animals ; Apoptosis/immunology ; Autoantibodies/immunology ; Autoantigens/chemistry ; Autoantigens/immunology ; Autoimmune Diseases/immunology ; Autoimmune Diseases/pathology ; Autoimmune Diseases/therapy ; Autoimmunity ; Epitopes ; Humans ; Lymphocytes/immunology ; Protein Conformation ; Rheumatic Diseases/immunology ; Rheumatic Diseases/pathology ; Rheumatic Diseases/therapy ; Ribonucleoprotein, U1 Small Nuclear/chemistry ; Ribonucleoprotein, U1 Small Nuclear/immunology ; Structure-Activity Relationship ; Toll-Like Receptors/immunology
    Chemical Substances Autoantibodies ; Autoantigens ; Epitopes ; Ribonucleoprotein, U1 Small Nuclear ; Toll-Like Receptors
    Language English
    Publishing date 2010-02-25
    Publishing country England
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 391796-4
    ISSN 1600-065X ; 0105-2896
    ISSN (online) 1600-065X
    ISSN 0105-2896
    DOI 10.1111/j.0105-2896.2009.00863.x
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  2. Article: The U1-snRNP complex: structural properties relating to autoimmune pathogenesis in rheumatic diseases

    Kattah, Nicole H / Kattah, Michael G / Utz, Paul J

    Immunological reviews. 2010 Jan., v. 233, no. 1

    2010  

    Abstract: The U1 small nuclear ribonucleoprotein particle (snRNP) is a target of autoreactive B cells and T cells in several rheumatic diseases including systemic lupus erythematosus (SLE) and mixed connective tissue disease (MCTD). We propose that inherent ... ...

    Abstract The U1 small nuclear ribonucleoprotein particle (snRNP) is a target of autoreactive B cells and T cells in several rheumatic diseases including systemic lupus erythematosus (SLE) and mixed connective tissue disease (MCTD). We propose that inherent structural properties of this autoantigen complex, including common RNA-binding motifs, B and T-cell epitopes, and a unique stimulatory RNA molecule, underlie its susceptibility as a target of the autoimmune response. Immune mechanisms that may contribute to overall U1-snRNP immunogenicity include epitope spreading through B and T-cell interactions, apoptosis-induced modifications, and Toll-like receptor (TLR) activation through stimulation by U1-snRNA. We conclude that understanding the interactions between U1-snRNP and the immune system will provide insights into why certain patients develop anti-U1-snRNP autoimmunity, and more importantly how to effectively target therapies against this autoimmune response.
    Keywords autoimmunity
    Language English
    Dates of publication 2010-01
    Size p. 126-145.
    Publisher Blackwell Publishing Ltd
    Publishing place Oxford, UK
    Document type Article
    ZDB-ID 391796-4
    ISSN 1600-065X ; 0105-2896
    ISSN (online) 1600-065X
    ISSN 0105-2896
    DOI 10.1111/j.0105-2896.2009.00863.x
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  3. Article ; Online: Tetramers reveal IL-17-secreting CD4+ T cells that are specific for U1-70 in lupus and mixed connective tissue disease.

    Kattah, Nicole H / Newell, Evan W / Jarrell, Justin Ansel / Chu, Alvina D / Xie, Jianming / Kattah, Michael G / Goldberger, Ofir / Ye, Jessica / Chakravarty, Eliza F / Davis, Mark M / Utz, Paul J

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

    2015  Volume 112, Issue 10, Page(s) 3044–3049

    Abstract: Antigen-specific CD4(+) T cells are implicated in the autoimmune disease systemic lupus erythematosus (SLE), but little is known about the peptide antigens that they recognize and their precise function in disease. We generated a series of MHC class II ... ...

    Abstract Antigen-specific CD4(+) T cells are implicated in the autoimmune disease systemic lupus erythematosus (SLE), but little is known about the peptide antigens that they recognize and their precise function in disease. We generated a series of MHC class II tetramers of I-E(k)-containing peptides from the spliceosomal protein U1-70 that specifically stain distinct CD4(+) T-cell populations in MRL/lpr mice. The T-cell populations recognize an epitope differing only by the presence or absence of a single phosphate residue at position serine(140). The frequency of CD4(+) T cells specific for U1-70(131-150):I-E(k) (without phosphorylation) correlates with disease severity and anti-U1-70 autoantibody production. These T cells also express RORγt and produce IL-17A. Furthermore, the U1-70-specific CD4(+) T cells that produce IL-17A are detected in a subset of patients with SLE and are significantly increased in patients with mixed connective tissue disease. These studies provide tools for studying antigen-specific CD4(+) T cells in lupus, and demonstrate an antigen-specific source of IL-17A in autoimmune disease.
    MeSH term(s) Animals ; Autoantibodies/biosynthesis ; CD4-Positive T-Lymphocytes/secretion ; Enzyme-Linked Immunosorbent Assay ; Female ; Humans ; Interleukin-17/secretion ; Lupus Erythematosus, Systemic/immunology ; Male ; Mice ; Mixed Connective Tissue Disease/immunology ; Oligopeptides/immunology ; Phosphorylation
    Chemical Substances Autoantibodies ; Interleukin-17 ; Oligopeptides
    Language English
    Publishing date 2015-03-10
    Publishing country United States
    Document type Journal Article
    ZDB-ID 209104-5
    ISSN 1091-6490 ; 0027-8424
    ISSN (online) 1091-6490
    ISSN 0027-8424
    DOI 10.1073/pnas.1424796112
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  4. Article ; Online: Characterization of influenza vaccine immunogenicity using influenza antigen microarrays.

    Price, Jordan V / Jarrell, Justin A / Furman, David / Kattah, Nicole H / Newell, Evan / Dekker, Cornelia L / Davis, Mark M / Utz, Paul J

    PloS one

    2013  Volume 8, Issue 5, Page(s) e64555

    Abstract: Background: Existing methods to measure influenza vaccine immunogenicity prohibit detailed analysis of epitope determinants recognized by immunoglobulins. The development of highly multiplex proteomics platforms capable of capturing a high level of ... ...

    Abstract Background: Existing methods to measure influenza vaccine immunogenicity prohibit detailed analysis of epitope determinants recognized by immunoglobulins. The development of highly multiplex proteomics platforms capable of capturing a high level of antibody binding information will enable researchers and clinicians to generate rapid and meaningful readouts of influenza-specific antibody reactivity.
    Methods: We developed influenza hemagglutinin (HA) whole-protein and peptide microarrays and validated that the arrays allow detection of specific antibody reactivity across a broad dynamic range using commercially available antibodies targeted to linear and conformational HA epitopes. We derived serum from blood draws taken from 76 young and elderly subjects immediately before and 28±7 days post-vaccination with the 2008/2009 trivalent influenza vaccine and determined the antibody reactivity of these sera to influenza array antigens.
    Results: Using linear regression and correcting for multiple hypothesis testing by the Benjamini and Hochberg method of permutations over 1000 resamplings, we identified antibody reactivity to influenza whole-protein and peptide array features that correlated significantly with age, H1N1, and B-strain post-vaccine titer as assessed through a standard microneutralization assay (p<0.05, q <0.2). Notably, we identified several peptide epitopes that were inversely correlated with regard to age and seasonal H1N1 and B-strain neutralization titer (p<0.05, q <0.2), implicating reactivity to these epitopes in age-related defects in response to H1N1 influenza. We also employed multivariate linear regression with cross-validation to build models based on age and pre-vaccine peptide reactivity that predicted vaccine-induced neutralization of seasonal H1N1 and H3N2 influenza strains with a high level of accuracy (84.7% and 74.0%, respectively).
    Conclusion: Our methods provide powerful tools for rapid and accurate measurement of broad antibody-based immune responses to influenza, and may be useful in measuring response to other vaccines and infectious agents.
    MeSH term(s) Adolescent ; Adult ; Aged ; Aged, 80 and over ; Amino Acid Sequence ; Antibodies, Viral/immunology ; Antibodies, Viral/metabolism ; Antigens, Viral/immunology ; Antigens, Viral/metabolism ; Epitopes/immunology ; Epitopes/metabolism ; Female ; Hemagglutinin Glycoproteins, Influenza Virus/immunology ; Humans ; Influenza A Virus, H1N1 Subtype/immunology ; Influenza A Virus, H3N2 Subtype/immunology ; Influenza Vaccines/administration & dosage ; Influenza Vaccines/immunology ; Influenza, Human/immunology ; Influenza, Human/prevention & control ; Influenza, Human/virology ; Linear Models ; Male ; Middle Aged ; Molecular Sequence Data ; Peptides/immunology ; Peptides/metabolism ; Protein Array Analysis/methods ; Proteomics/methods ; Vaccination ; Young Adult
    Chemical Substances Antibodies, Viral ; Antigens, Viral ; Epitopes ; Hemagglutinin Glycoproteins, Influenza Virus ; Influenza Vaccines ; Peptides
    Language English
    Publishing date 2013-05-29
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ISSN 1932-6203
    ISSN (online) 1932-6203
    DOI 10.1371/journal.pone.0064555
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  5. Article ; Online: Self-antigen recognition by follicular lymphoma B-cell receptors.

    Sachen, Kacey L / Strohman, Michael J / Singletary, Jonathan / Alizadeh, Ash A / Kattah, Nicole H / Lossos, Chen / Mellins, Elizabeth D / Levy, Shoshana / Levy, Ronald

    Blood

    2012  Volume 120, Issue 20, Page(s) 4182–4190

    Abstract: Follicular lymphoma is a monoclonal B-cell malignancy with each patient's tumor expressing a unique cell surface immunoglobulin (Ig), or B-cell receptor (BCR), that can potentially recognize antigens and/or transduce signals into the tumor cell. Here we ... ...

    Abstract Follicular lymphoma is a monoclonal B-cell malignancy with each patient's tumor expressing a unique cell surface immunoglobulin (Ig), or B-cell receptor (BCR), that can potentially recognize antigens and/or transduce signals into the tumor cell. Here we evaluated the reactivity of tumor derived Igs for human tissue antigens. Self-reactivity was observed in 26% of tumor Igs (25 of 98). For one follicular lymphoma patient, the recognized self-antigen was identified as myoferlin. This patient's tumor cells bound recombinant myoferlin in proportion to their level of BCR expression, and the binding to myoferlin was preserved despite ongoing somatic hypermutation of Ig variable regions. Furthermore, BCR-mediated signaling was induced after culture of tumor cells with myoferlin. These results suggest that antigen stimulation may provide survival signals to tumor cells and that there is a selective pressure to preserve antigen recognition as the tumor evolves.
    MeSH term(s) Antibodies, Neoplasm/chemistry ; Antibodies, Neoplasm/genetics ; Antibodies, Neoplasm/immunology ; Autoantigens/genetics ; Autoantigens/immunology ; Autoimmunity ; Calcium-Binding Proteins/genetics ; Calcium-Binding Proteins/immunology ; Cell Line, Tumor ; Cell Survival ; DNA, Neoplasm/genetics ; Glycosylation ; Humans ; Immunoglobulin G/chemistry ; Immunoglobulin G/genetics ; Immunoglobulin G/immunology ; Immunoglobulin Heavy Chains/genetics ; Immunoglobulin Light Chains/genetics ; Interferometry ; Lymphoma, Follicular/immunology ; Membrane Proteins/genetics ; Membrane Proteins/immunology ; Muscle Proteins/genetics ; Muscle Proteins/immunology ; Neoplasm Proteins/genetics ; Neoplasm Proteins/immunology ; Protein Processing, Post-Translational ; Receptors, Antigen, B-Cell/immunology ; Recombinant Proteins/genetics ; Recombinant Proteins/immunology ; Ribosomal Protein S6 Kinases, 90-kDa/metabolism ; Tumor Microenvironment/immunology
    Chemical Substances Antibodies, Neoplasm ; Autoantigens ; Calcium-Binding Proteins ; DNA, Neoplasm ; Immunoglobulin G ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; MYOF protein, human ; Membrane Proteins ; Muscle Proteins ; Neoplasm Proteins ; Receptors, Antigen, B-Cell ; Recombinant Proteins ; RPS6KA1 protein, human (EC 2.7.11.1) ; Ribosomal Protein S6 Kinases, 90-kDa (EC 2.7.11.1)
    Language English
    Publishing date 2012-09-28
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
    ZDB-ID 80069-7
    ISSN 1528-0020 ; 0006-4971
    ISSN (online) 1528-0020
    ISSN 0006-4971
    DOI 10.1182/blood-2012-05-427534
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  6. Article ; Online: Characterization of influenza vaccine immunogenicity using influenza antigen microarrays.

    Jordan V Price / Justin A Jarrell / David Furman / Nicole H Kattah / Evan Newell / Cornelia L Dekker / Mark M Davis / Paul J Utz

    PLoS ONE, Vol 8, Iss 5, p e

    2013  Volume 64555

    Abstract: Existing methods to measure influenza vaccine immunogenicity prohibit detailed analysis of epitope determinants recognized by immunoglobulins. The development of highly multiplex proteomics platforms capable of capturing a high level of antibody binding ... ...

    Abstract Existing methods to measure influenza vaccine immunogenicity prohibit detailed analysis of epitope determinants recognized by immunoglobulins. The development of highly multiplex proteomics platforms capable of capturing a high level of antibody binding information will enable researchers and clinicians to generate rapid and meaningful readouts of influenza-specific antibody reactivity.We developed influenza hemagglutinin (HA) whole-protein and peptide microarrays and validated that the arrays allow detection of specific antibody reactivity across a broad dynamic range using commercially available antibodies targeted to linear and conformational HA epitopes. We derived serum from blood draws taken from 76 young and elderly subjects immediately before and 28±7 days post-vaccination with the 2008/2009 trivalent influenza vaccine and determined the antibody reactivity of these sera to influenza array antigens.Using linear regression and correcting for multiple hypothesis testing by the Benjamini and Hochberg method of permutations over 1000 resamplings, we identified antibody reactivity to influenza whole-protein and peptide array features that correlated significantly with age, H1N1, and B-strain post-vaccine titer as assessed through a standard microneutralization assay (p<0.05, q <0.2). Notably, we identified several peptide epitopes that were inversely correlated with regard to age and seasonal H1N1 and B-strain neutralization titer (p<0.05, q <0.2), implicating reactivity to these epitopes in age-related defects in response to H1N1 influenza. We also employed multivariate linear regression with cross-validation to build models based on age and pre-vaccine peptide reactivity that predicted vaccine-induced neutralization of seasonal H1N1 and H3N2 influenza strains with a high level of accuracy (84.7% and 74.0%, respectively).Our methods provide powerful tools for rapid and accurate measurement of broad antibody-based immune responses to influenza, and may be useful in measuring response to other vaccines and infectious agents.
    Keywords Medicine ; R ; Science ; Q
    Subject code 570
    Language English
    Publishing date 2013-01-01T00:00:00Z
    Publisher Public Library of Science (PLoS)
    Document type Article ; Online
    Database BASE - Bielefeld Academic Search Engine (life sciences selection)

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