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  • 1.
    Bokarewa, Maria
    et al.
    Sahlgrenska University Hospital, Göteborg, Sweden.
    Tarkowski, Andrej
    Lind, Magnus
    Sahlgrenska University Hospital, Göteborg, Sweden.
    Dahlberg, Leif
    Lund University, Sweden .
    Magnusson, Mattias
    Sahlgrenska University Hospital, Göteborg, Sweden.
    Arthritogenic dsRNA is present in synovial fluid from rheumatoid arthritis patients with an erosive disease course2008In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 38, no 11, p. 3237-3244Article in journal (Refereed)
    Abstract [en]

    Viruses may be part of the pathogenesis of rheumatoid arthritis (RA). Double stranded RNA (dsRNA) is a prototypic viral conformation of nucleic acid that is highly arthritogenic in mice. Therefore, we developed an ELISA to detect dsRNA in sera and synovial fluids (SF) in RA patients and in osteoarthritic controls. The developed ELISA recognizes picogram levels of viral or synthetic dsRNA but shows no reactivity against DNA, synthetic ssRNA, or total RNA prepared from mammalian cells. Before analysis by ELISA, each sample was subjected to RNA precipitation. The RA patients had significantly higher levels of dsRNA than the osteoarthritis patients in SF and in sera. In 7 of 17 RA patients, EBV was present in SF and in all but one of these this was accompanied by the presence of dsRNA. No parvovirus, cytomegalovirus, or polyomavirus was detected. The anti-viral cytokine IFN-alpha was detected in SF in 10 of 21 RA patients, but in none of the osteoarthritis patients. Notably, RA patients with erosive disease course had significantly higher levels of dsRNA in SF than non-erosive patients, but no correlation between dsRNA levels and the presence of RF or levels of C-reactive protein, IL-6, or IFN-alpha was observed.

  • 2.
    Che, Karlhans F
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Molecular Virology. Linköping University, Faculty of Health Sciences.
    Sabado, RL
    New York University School of Medicine, New York, NY, USA.
    Shankar, Esaki M
    Linköping University, Department of Clinical and Experimental Medicine, Molecular Virology. Linköping University, Faculty of Health Sciences.
    Tjomsland, Veronica
    Linköping University, Department of Clinical and Experimental Medicine, Molecular Virology. Linköping University, Faculty of Health Sciences.
    Messmer, D
    Moores Cancer Center, La Jolla, CA, USA.
    Bhardwa, N
    New York University School of Medicine, New York, NY, USA.
    Lifson, JF
    National Cancer Institute at Frederick, Maryland, MD, USA.
    Larsson, Marie
    Linköping University, Department of Clinical and Experimental Medicine, Molecular Virology. Linköping University, Faculty of Health Sciences.
    HIV-1 impairs in vitro priming of naïve T cells and gives rise to contact-dependent suppressor T cells2010In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 40, no 8, p. 2248-2258Article in journal (Refereed)
    Abstract [en]

    Priming of T cells in lymphoid tissues of HIV-infected individuals occurs in the presence of HIV-1. DC in this milieu activate T cells and disseminate HIV-1 to newly activated T cells, the outcome of which may have serious implications in the development of optimal antiviral responses. We investigated the effects of HIV-1 on DC-naïve T-cell interactions using an allogeneic in vitro system. Our data demonstrate a dramatic decrease in the primary expansion of naïve T cells when cultured with HIV-1-exposed DC. CD4(+) and CD8(+) T cells showed enhanced expression of PD-1 and TRAIL, whereas CTLA-4 expression was observed on CD4(+) T cells. It is worth noting that T cells primed in the presence of HIV-1 suppressed priming of other naïve T cells in a contact-dependent manner. We identified PD-1, CTLA-4, and TRAIL pathways as responsible for this suppresion, as blocking these negative molecules restored T-cell proliferation to a higher degree. In conclusion, the presence of HIV-1 during DC priming produced cells with inhibitory effects on T-cell activation and proliferation, i.e. suppressor T cells, a mechanism that could contribute to the enhancement of HIV-1 pathogenesis.

  • 3.
    Cossarizza, Andrea
    et al.
    University of Modena, Italy; Reggio Emilia School Med, Italy.
    Chang, Hyun-Dong
    Institute Leibniz Assoc, Germany.
    Radbruch, Andreas
    Institute Leibniz Assoc, Germany.
    Andrae, Immanuel
    Technical University of Munich, Germany.
    Annunziato, Francesco
    University of Florence, Italy.
    Bacher, Petra
    Charite University of Medical Berlin, Germany.
    Barnaba, Vincenzo
    Sapienza University of Roma, Italy; Fdn Cenci Bolognetti, Italy.
    Battistini, Luca
    Santa Lucia Fdn, Italy.
    Bauer, Wolfgang M.
    Medical University of Vienna, Austria.
    Baumgart, Sabine
    Institute Leibniz Assoc, Germany.
    Becher, Burkhard
    University of Zurich, Switzerland.
    Beisker, Wolfgang
    German Research Centre Environm Heatlh, Germany.
    Berek, Claudia
    Institute Leibniz Assoc, Germany.
    Blanco, Alfonso
    University of Coll Dublin, Ireland.
    Borsellino, Giovanna
    Santa Lucia Fdn, Italy.
    Boulais, Philip E.
    Albert Einstein Coll Med, NY 10467 USA; Ruth L and David S Gottesman Institute Stem Cell and Regen, NY USA.
    Brinkman, Ryan R.
    BC Cancer Agency, Canada; University of British Columbia, Canada.
    Buescher, Martin
    Miltenyi Biotec GmbH, Germany.
    Busch, Dirk H.
    Technical University of Munich, Germany; National Centre Infect Research, Germany; Technical University of Munich, Germany.
    Bushnell, Timothy P.
    University of Rochester, NY 14642 USA; University of Rochester, NY 14642 USA.
    Cao, Xuetao
    Zhejiang University, Peoples R China; Second Mil Medical University, Peoples R China; Second Mil Medical University, Peoples R China; Chinese Academic Medical Science, Peoples R China; Chinese Academic Medical Science, Peoples R China.
    Cavani, Andrea
    NIHMP, Italy.
    Chattopadhyay, Pratip K.
    Vaccine Research Centre, MD USA.
    Cheng, Qingyu
    Charite University of Medical Berlin, Germany.
    Chow, Sue
    Princess Margaret Hospital, Canada.
    Clerici, Mario
    University of Milan, Italy; Fdn Don C Gnocchi, Italy.
    Cooke, Anne
    University of Cambridge, England.
    Cosma, Antonio
    University of Paris Sud, France.
    Cosmi, Lorenzo
    University of Firenze, Italy.
    Cumano, Ana
    Pasteur Institute, France.
    Duc Dang, Van
    Institute Leibniz Assoc, Germany.
    Davies, Derek
    Francis Crick Institute, England.
    De Biasi, Sara
    University of Modena and Reggio Emilia, Italy.
    Del Zotto, Genny
    Ist Giannina Gaslini, Italy.
    Della Bella, Silvia
    University of Milan, Italy; Lab Clin and Expt Immunol, Italy.
    Dellabona, Paolo
    Ist Science San Raffaele, Italy.
    Deniz, Gunnur
    Istanbul University, Turkey.
    Dessing, Mark
    Sony Europe Ltd, England.
    Diefenbach, Andreas
    Charite University of Medical Berlin, Germany.
    Di Santo, James
    Institute Pasteur, France.
    Dieli, Francesco
    University of Palermo, Italy.
    Dolf, Andreas
    University of Bonn, Germany.
    Donnenberg, Vera S.
    University of Pittsburgh, PA USA.
    Doerner, Thomas
    Charite University of Medical Berlin, Germany.
    Ehrhardt, Gotz R. A.
    University of Toronto, Canada.
    Endl, Elmar
    University of Bonn, Germany.
    Engel, Pablo
    University of Barcelona, Spain.
    Engelhardt, Britta
    University of Bern, Switzerland.
    Esser, Charlotte
    Leibniz Research Institute Environm Med, Germany.
    Everts, Bart
    Leiden University, Netherlands.
    Falk, Christine S.
    MHH Hannover Medical Sch, Germany; TTU IICH, Germany.
    Fehniger, Todd A.
    Washington University, MO USA.
    Filby, Andrew
    Newcastle University, England.
    Fillatreau, Simon
    INSERM, France; University of Paris 05, France; Hop Necker Enfants Malad, France.
    Follo, Marie
    University of Freiburg, Germany.
    Foerster, Irmgard
    University of Bonn, Germany.
    Foster, John
    Owl Biomed Inc, CA USA.
    Foulds, Gemma A.
    Nottingham Trent University, England.
    Frenette, Paul S.
    Albert Einstein Coll Med, NY 10467 USA.
    Galbraith, David
    University of Arizona, AZ USA.
    Garbi, Natalio
    University of Bonn, Germany; Arizona Cancer Centre, AZ USA; Institute Expt Immunol, Germany.
    Dolores Garcia-Godoy, Maria
    Josep Carreras Leukemia Research Institute, Spain.
    Geginat, Jens
    Ist Nazl Genet Molecolare Romeo Enrica Invernizzi, Italy.
    Ghoreschi, Kamran
    Eberhard Karls University of Tubingen, Germany.
    Gibellini, Lara
    University of Modena and Reggio Emilia, Italy.
    Goettlinger, Christoph
    University of Cologne, Germany.
    Goodyear, Carl S.
    University of Glasgow, Scotland.
    Gori, Andrea
    University of Milano Bicocca, Italy.
    Grogan, Jane
    Genentech Inc, CA USA.
    Gross, Mor
    Weizmann Institute Science, Israel.
    Gruetzkau, Andreas
    Institute Leibniz Assoc, Germany.
    Grummitt, Daryl
    Owl Biomed Inc, CA USA.
    Hahn, Jonas
    University of Klinikum Erlangen, Germany.
    Hammer, Quirin
    Institute Leibniz Assoc, Germany.
    Hauser, Anja E.
    Institute Leibniz Assoc, Germany; Charite University of Medical Berlin, Germany.
    Haviland, David L.
    Houston Methodist Hospital, TX USA.
    Hedley, David
    Princess Margaret Hospital, Canada.
    Herrera, Guadalupe
    University of Valencia, Spain; University of Valencia, Spain.
    Herrmann, Martin
    University of Klinikum Erlangen, Germany.
    Hiepe, Falk
    Charite University of Medical Berlin, Germany.
    Holland, Tristan
    Arizona Cancer Centre, AZ USA; Institute Expt Immunol, Germany.
    Hombrink, Pleun
    Sanquin Research and Landsteiner Lab, Netherlands.
    Houston, Jessica P.
    New Mexico State University, NM 88003 USA.
    Hoyer, Bimba F.
    Charite University of Medical Berlin, Germany.
    Huang, Bo
    Huazhong University of Science and Technology, Peoples R China; Chinese Academic Medical Science, Peoples R China; Chinese Academic Medical Science, Peoples R China; Peking Union Medical Coll, Peoples R China; Chinese Academic Medical Science, Peoples R China.
    Hunter, Christopher A.
    University of Penn, PA 19104 USA.
    Iannone, Anna
    University of Modena and Reggio Emilia, Italy.
    Jaeck, Hans-Martin
    University Hospital Erlangen, Germany.
    Javega, Beatriz
    University of Valencia, Spain.
    Jonjic, Stipan
    University of Rijeka, Croatia; University of Rijeka, Croatia.
    Juelke, Kerstin
    Institute Leibniz Assoc, Germany.
    Jung, Steffen
    Weizmann Institute Science, Israel.
    Kaiser, Toralf
    Institute Leibniz Assoc, Germany.
    Kalina, Tomas
    Charles University of Prague, Czech Republic; University Hospital Motol, Czech Republic.
    Keller, Baerbel
    University of Freiburg, Germany.
    Khan, Srijit
    University of Toronto, Canada.
    Kienhoefer, Deborah
    University of Klinikum Erlangen, Germany.
    Kroneis, Thomas
    Medical University of Graz, Austria.
    Kunkel, Desiree
    Charite University of Medical Berlin, Germany.
    Kurts, Christian
    University of Bonn, Germany.
    Kvistborg, Pia
    Netherlands Cancer Institute, Netherlands.
    Lannigan, Joanne
    University of Virginia, VA 22908 USA.
    Lantz, Olivier
    Institute Curie, France; Institute Curie, France; Institute Curie, France.
    Larbi, Anis
    Biol Aging Program, Singapore; ASTAR, Singapore; University of Sherbrooke, Canada; ElManar University, Tunisia.
    LeibundGut-Landmann, Salome
    University of Zurich, Switzerland.
    Leipold, Michael D.
    Stanford University, CA USA.
    Levings, Megan K.
    University of British Columbia, Canada; British Columbia Childrens Hospital, Canada.
    Litwin, Virginia
    Covance, IN USA.
    Liu, Yanling
    University of Toronto, Canada.
    Lohoff, Michael
    University of Marburg, Germany; University of Marburg, Germany.
    Lombardi, Giovanna
    Guys Hospital, England.
    Lopez, Lilly
    Beckman Coulter Inc, FL USA.
    Lovett-Racke, Amy
    Ohio State University, OH 43210 USA.
    Lubberts, Erik
    University of Medical Centre, Netherlands.
    Ludewig, Burkhard
    Kantonsspital St Gallen, Switzerland.
    Lugli, Enrico
    Humanitas Clin and Research Centre, Italy; Humanitas Clin and Research Centre, Italy.
    Maecker, Holden T.
    Stanford University, CA USA.
    Martrus, Gloria
    Leibniz Institute Expt Virol, Germany.
    Matarese, Giuseppe
    University of Napoli Federico II, Italy; IEOS, Italy.
    Maueroeder, Christian
    University of Klinikum Erlangen, Germany.
    McGrath, Mairi
    Institute Leibniz Assoc, Germany.
    McInnes, Iain
    University of Glasgow, Scotland.
    Mei, Henrik E.
    Institute Leibniz Assoc, Germany.
    Melchers, Fritz
    Max Planck Institute Infect Biol, Germany.
    Melzer, Susanne
    University of Leipzig, Germany.
    Mielenz, Dirk
    University of Erlangen Nurnberg, Germany.
    Mills, Kingston
    University of Dublin, Ireland.
    Mjösberg, Jenny
    Linköping University, Department of Clinical and Experimental Medicine, Division of Surgery, Orthopedics and Oncology. Linköping University, Faculty of Medicine and Health Sciences. Karolinska Institute Stockholm, Sweden.
    Moore, Jonni
    University of Penn, PA USA.
    Moran, Barry
    University of Dublin, Ireland.
    Moretta, Alessandro
    University of Genoa, Italy; Centre Eccellenza Ric Biomed CEBR, Italy.
    Moretta, Lorenzo
    Bambino Gesu Pediat Hospital, Italy.
    Mosmann, Tim R.
    University of Rochester, NY 14642 USA.
    Mueller, Susann
    UFZ Helmholtz Centre Environm Research, Germany.
    Muller, Werner
    University of Manchester, England.
    Munz, Christian
    University of Zurich, Switzerland.
    Multhoff, Gabriele
    Technical University of Munchen TUM, Germany; Helmholtz Zentrum Munchen, Germany.
    Enrique Munoz, Luis
    University of Klinikum Erlangen, Germany.
    Murphy, Kenneth M.
    Washington University of St Louis, MO USA; Washington University of St Louis, MO USA.
    Nakayama, Toshinori
    Chiba University, Japan.
    Nasi, Milena
    University of Modena and Reggio Emilia, Italy.
    Neudoerfl, Christine
    MHH Hannover Medical Sch, Germany.
    Nolan, John
    Scintillon Institute, CA USA.
    Nourshargh, Sussan
    William Harvey Research Institute, England; Queen Mary University of London, England.
    OConnor, Jose-Enrique
    University of Valencia, Spain.
    Ouyang, Wenjun
    Amgen Inc, CA USA.
    Oxenius, Annette
    Swiss Federal Institute Technology, Switzerland.
    Palankar, Raghav
    University of Medical Greifswald, Germany.
    Panse, Isabel
    University of Oxford, England.
    Peterson, Part
    University of Tartu, Estonia.
    Peth, Christian
    Miltenyi Biotec GmbH, Germany.
    Petriz, Jordi
    Josep Carreras Leukemia Research Institute, Spain.
    Philips, Daisy
    Netherlands Cancer Institute, Netherlands.
    Pickl, Winfried
    Medical University of Vienna, Austria.
    Piconese, Silvia
    Sapienza University of Roma, Italy; Fdn Cenci Bolognetti, Italy.
    Pinti, Marcello
    University of Modena and Reggio Emilia, Italy.
    Graham Pockley, A.
    Nottingham Trent University, England; Chromocyte Ltd, England.
    Justyna Podolska, Malgorzata
    University of Klinikum Erlangen, Germany.
    Pucillo, Carlo
    University of Udine, Italy.
    Quataert, Sally A.
    University of Rochester, NY 14642 USA.
    Radstake, Timothy R. D. J.
    University of Medical Centre Utrecht, Netherlands; University of Medical Centre Utrecht, Netherlands.
    Rajwa, Bartek
    Purdue University, IN 47907 USA.
    Rebhahn, Jonathan A.
    University of Rochester, NY 14642 USA.
    Recktenwald, Diether
    Desatoya LLC, NV USA.
    Remmerswaal, Ester B. M.
    Academic Medical Centre, Netherlands; Academic Medical Centre, Netherlands.
    Rezvani, Katy
    University of Texas MD Anderson Cancer Centre, TX 77030 USA.
    Rico, Laura G.
    Josep Carreras Leukemia Research Institute, Spain.
    Paul Robinson, J.
    Purdue University, IN 47907 USA.
    Romagnani, Chiara
    Institute Leibniz Assoc, Germany.
    Rubartelli, Anna
    IRCCS, Italy.
    Ruland, Juergen
    Technical University of Munich, Germany; German Cancer Research Centre, Germany.
    Sakaguchi, Shimon
    Osaka University, Japan; Kyoto University, Japan.
    Sala-de-Oyanguren, Francisco
    University of Valencia, Spain.
    Samstag, Yvonne
    Ruprecht Karls University of Heidelberg, Germany.
    Sanderson, Sharon
    University of Oxford, England.
    Sawitzki, Birgit
    Free University of Berlin, Germany; Institute Medical Immunol, Germany.
    Scheffold, Alexander
    Institute Leibniz Assoc, Germany; Charite University of Medical Berlin, Germany.
    Schiemann, Matthias
    Technical University of Munich, Germany.
    Schildberg, Frank
    Harvard Medical Sch, MA USA.
    Schimisky, Esther
    Miltenyi Biotec GmbH, Germany.
    Schmid, Stephan A.
    University of Klinikum Regensburg, Germany.
    Schmitt, Steffen
    German Cancer Research Centre, Germany.
    Schober, Kilian
    Technical University of Munich, Germany.
    Schueler, Thomas
    Otto Von Guericke University, Germany.
    Ronald Schulz, Axel
    Institute Leibniz Assoc, Germany.
    Schumacher, Ton
    Netherlands Cancer Institute, Netherlands.
    Scotta, Cristiano
    Guys Hospital, England.
    Vincent Shankey, T.
    AsedaSciences, IN USA.
    Shemer, Anat
    Weizmann Institute Science, Israel.
    Simon, Anna-Katharina
    University of Oxford, England.
    Spidlen, Josef
    BC Cancer Agency, Canada.
    Stall, Alan M.
    BD Life Science, CA USA.
    Stark, Regina
    Sanquin Research and Landsteiner Lab, Netherlands.
    Stehle, Christina
    Institute Leibniz Assoc, Germany.
    Stein, Merle
    University of Erlangen Nurnberg, Germany.
    Steinmetz, Tobit
    University of Erlangen Nurnberg, Germany.
    Stockinger, Hannes
    Medical University of Vienna, Austria.
    Takahama, Yousuke
    University of Tokushima, Japan.
    Tarnok, Attila
    Fraunhofer Institute Cell Therapy and Immunol IZI, Germany; IMISE, Germany.
    Tian, ZhiGang
    University of Science and Technology China, Peoples R China; University of Science and Technology China, Peoples R China; Zhejiang University, Peoples R China.
    Tornack, Julia
    Max Planck Institute Infect Biol, Germany.
    Traggiai, Elisabetta
    NIBR, Switzerland.
    Trotter, Joe
    BD Life Science, CA USA.
    Ulrich, Henning
    University of Sao Paulo, Brazil.
    van der Braber, Marlous
    Netherlands Cancer Institute, Netherlands.
    van Lier, Rene A. W.
    Sanquin Research and Landsteiner Lab, Netherlands.
    Veldhoen, Marc
    Institute Molecular Med, Portugal.
    Vento-Asturias, Salvador
    Arizona Cancer Centre, AZ USA.
    Vieira, Paulo
    Institute Pasteur, France.
    Voehringer, David
    University Hospital Erlangen, Germany.
    Volk, Hans-Dieter
    Labor Berlin, Germany.
    von Volkmann, Konrad
    APE Appl Phys and Elect, Germany.
    Waisman, Ari
    Johannes Gutenberg University of Mainz, Germany.
    Walker, Rachael
    Babraham Institute, England.
    Ward, Michael D.
    Thermo Fisher Science, OR USA.
    Warnatz, Klaus
    University of Freiburg, Germany.
    Warth, Sarah
    Charite University of Medical Berlin, Germany.
    Watson, James V.
    Medinfomat Ltd, England.
    Watzl, Carsten
    TU Dortmund, Germany.
    Wegener, Leonie
    Miltenyi Biotec GmbH, Germany.
    Wiedemann, Annika
    Charite University of Medical Berlin, Germany.
    Wienands, Juergen
    University of Medical Gottingen, Germany.
    Wing, James
    Osaka University, Japan; Kyoto University, Japan.
    Wurst, Peter
    University of Bonn, Germany.
    Yu, Liping
    BD Bioscience, CA USA.
    Yue, Alice
    Simon Fraser University, Canada.
    Zhang, Qianjun
    Emerald Biotech Co Ltd, Peoples R China.
    Zhao, Yi
    Sichuan University, Peoples R China.
    Ziegler, Susanne
    Leibniz Institute Expt Virol, Germany.
    Zimmermann, Jakob
    University of Bern, Switzerland.
    Guidelines for the use of flow cytometry and cell sorting in immunological studies2017In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 47, no 10, p. 1584-1797Article in journal (Refereed)
    Abstract [en]

    n/a

  • 4.
    Forkel, Marianne
    et al.
    Karolinska Institute, Sweden.
    Berglin, Lena
    Karolinska Institute, Sweden.
    Kekalainen, Eliisa
    Karolinska Institute, Sweden.
    Carlsson, Adrian
    Karolinska Institute, Sweden.
    Svedin, Emma
    Karolinska Institute, Sweden.
    Michaelsson, Jakob
    Karolinska Institute, Sweden.
    Nagasawa, Maho
    University of Amsterdam, Netherlands.
    Erjefalt, Jonas S.
    Lund University, Sweden.
    Mori, Michiko
    Lund University, Sweden.
    Flodstrom-Tullberg, Malin
    Karolinska Institute, Sweden.
    Bergquist, Annika
    Karolinska Institute, Sweden; Karolinska University Hospital, Sweden.
    Ljunggren, Hans-Gustaf
    Karolinska Institute, Sweden.
    Westgren, Magnus
    Karolinska Institute, Sweden.
    Lindforss, Ulrik
    Karolinska Institute, Sweden; Karolinska University Hospital, Sweden.
    Friberg, Danielle
    KI, Sweden.
    Jorns, Carl
    Karolinska Institute, Sweden.
    Ellis, Ewa
    Karolinska Institute, Sweden.
    Bjorkstrom, Niklas K.
    Karolinska Institute, Sweden.
    Mjösberg, Jenny
    Linköping University, Department of Clinical and Experimental Medicine, Division of Surgery, Orthopedics and Oncology. Linköping University, Faculty of Medicine and Health Sciences. Karolinska Institute, Sweden.
    Composition and functionality of the intrahepatic innate lymphoid cell-compartment in human nonfibrotic and fibrotic livers2017In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 47, no 8, p. 1280-1294Article in journal (Refereed)
    Abstract [en]

    Human innate lymphoid cells have been described to exist in different organs, with functional deregulation of these cells contributing to several disease states. Here, we performed the first detailed characterization of the phenotype, tissue-residency properties, and functionality of ILC1s, ILC2s, and ILC3s in the human adult and fetal liver. In addition, we investigated changes in the ILC compartment in liver fibrosis. A unique composition of tissue-resident ILCs was observed in nonfibrotic livers as compared with that in mucosal tissues, with NKp44(-) ILC3s accounting for the majority of total intrahepatic ILCs. The frequency of ILC2s, representing a small fraction of ILCs in nonfibrotic livers, increased in liver fibrosis and correlated directly with the severity of the disease. Notably, intrahepatic ILC2s secreted the profibrotic cytokine IL-13 when exposed to IL-33 and thymic stromal lymphopoetin (TSLP); these cytokines were produced by hepatocytes, hepatic stellate cells (HSCs), and Kupffer cells in response to TLR-3 stimulation. In summary, the present results provide the first detailed characterization of intrahepatic ILCs in human adult and fetal liver. The results indicate a role for ILC2s in human liver fibrosis, implying that targeting ILC2s might be a novel therapeutic strategy for its treatment.

  • 5.
    Grage-Griebenow, E.
    et al.
    Forschungszentrum Borstel, Department of Immunology and Cell Biology, Borstel, Germany.
    Baran, J.
    Jagiellonian University, Institute of Molecular Biology, Cracow, Poland.
    Loppnow, H.
    Forschungszentrum Borstel, Department of Immunology and Cell Biology, Borstel, Germany.
    Los, Marek Jan
    Deutsches Krebsforschungs-zentrum, Heidelberg, Germany.
    Ernst, M.
    Forschungszentrum Borstel, Department of Immunology and Cell Biology, Borstel, Germany.
    Flad, H. D.
    Forschungszentrum Borstel, Department of Immunology and Cell Biology, Borstel, Germany.
    Pryjma, J.
    Jagiellonian University, Institute of Molecular Biology, Cracow, Poland.
    An Fcγ receptor I (CD64)-negative subpopulation of human peripheral blood monocytes is resistant to killing by antigen-activated CD4-positive cytotoxic T cells1997In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 27, no 9, p. 2358-2365Article in journal (Refereed)
    Abstract [en]

    It has been demonstrated that in monocyte/T cell co-cultures activated with recall antigens, cytotoxic T cells were generated which are able to reduce the number of antigen-presenting monocytes. In previous studies we could show that a minor subset of monocytes, the Fc gamma receptor I-negative (CD64(-)) monocytes, exhibits significantly higher antigen-presenting capacity than the main population of monocytes (> 90%) which are Fc gamma receptor I-positive (CD64(+)). Therefore, we addressed the question whether they are also differentially susceptible to T cell-mediated killing. In the present study we demonstrate that the CD64(-) monocyte subset is more resistant to killing by antigen-activated T cells than CD64(+) monocytes, as indicated by a higher viability and recovery of CD64(-) monocytes. This mechanism involves CD95 (Fas) antigen, since monocyte death in co-cultures with antigen-activated T cells could be partially reduced by blocking anti-Fas monoclonal antibodies (mAb). In agreement with this finding, although CD95 antigen was expressed on CD64(+) and CD64(-) monocytes at comparable levels, killing of CD64(-) monocytes by activating anti-Fas mAb was lower than of CD64(+) monocytes.

  • 6.
    Johansson, Maria E.
    et al.
    Karolinska Institute, Sweden; University of Gothenburg, Sweden.
    Zhang, Xiao-Ying
    Karolinska Institute, Sweden; Peking University, Peoples R China.
    Edfeldt, Kristina
    Karolinska Institute, Sweden; Karolinska Institute, Sweden.
    Lundberg, Anna M.
    Karolinska Institute, Sweden.
    Levin, Malin C.
    University of Gothenburg, Sweden.
    Boren, Jan
    University of Gothenburg, Sweden.
    Li, Wei
    Linköping University, Department of Clinical and Experimental Medicine, Division of Clinical Sciences. Linköping University, Faculty of Health Sciences.
    Yuan, Ximing
    Linköping University, Department of Clinical and Experimental Medicine, Division of Cell Biology. Linköping University, Faculty of Health Sciences.
    Folkersen, Lasse
    Karolinska Institute, Sweden; Novo Nordisk, Denmark.
    Eriksson, Per
    Karolinska Institute, Sweden.
    Hedin, Ulf
    Karolinska Institute, Sweden.
    Low, Hann
    Baker IDI Heart and Diabet Institute, Australia.
    Sviridov, Dmitri
    Baker IDI Heart and Diabet Institute, Australia.
    Rios, Francisco J.
    Karolinska Institute, Sweden; University of Glasgow, Scotland.
    Hansson, Goran K.
    Karolinska Institute, Sweden.
    Yan, Zhong-Qun
    Karolinska Institute, Sweden.
    Innate immune receptor NOD2 promotes vascular inflammation and formation of lipid-rich necrotic cores in hypercholesterolemic mice2014In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 44, no 10, p. 3081-3092Article in journal (Refereed)
    Abstract [en]

    Atherosclerosis is an inflammatory disease associated with the activation of innate immune TLRs and nucleotide-binding oligomerization domain-containing protein (NOD)like receptor pathways. However, the function of most innate immune receptors in atherosclerosis remains unclear. Here, we show that NOD2 is a crucial innate immune receptor influencing vascular inflammation and atherosclerosis severity. 10-week stimulation with muramyl dipeptide (MDP), the NOD2 cognate ligand, aggravated atherosclerosis, as indicated by the augmented lesion burden, increased vascular inflammation and enlarged lipid-rich necrotic cores in Ldlr(-/-) mice. Myeloid-specific ablation of NOD2, but not its downstream kinase, receptor-interacting serine/threonine-protein kinase 2, restrained the expansion of the lipid-rich necrotic core in Ldlr(-/-) chimeric mice. In vitro stimulation of macrophages with MDP enhanced the uptake of oxidized low-density lipoprotein and impaired cholesterol efflux in concordance with upregulation of scavenger receptor A1/2 and downregulation of ATP-binding cassette transporter A1. Ex vivo stimulation of human carotid plaques with MDP led to increased activation of inflammatory signaling pathways p38 MAPK and NF-kappa B-mediated release of proinflammatory cytokines. Altogether, this study suggests that NOD2 contributes to the expansion of the lipid-rich necrotic core and promotes vascular inflammation in atherosclerosis.

  • 7.
    Los, Marek Jan
    et al.
    Division of Immunochemistry, University of Freiburg, Freiburg; Division of Immunogenetics, University of Freiburg, Freiburg.
    Droge, W.
    Division of Immunochemistry, University of Freiburg, Freiburg.
    Stricker, K.
    Deutsches Krebsforschungszentrum, Heidelberg and Institute of Biochemistry, University of Freiburg, Freiburg.
    Baeuerle, Pa
    Division of Immunogenetics, University of Freiburg, Freiburg.
    Schulze-Osthoff, Klaus
    Division of Immunochemistry, University of Freiburg, Freiburg ; Division of Immunogenetics, University of Freiburg, Freiburg; Deutsches Krebsforschungszentrum, Heidelberg and Institute of Biochemistry, University of Freiburg, Freiburg.
    Hydrogen-Peroxide as a Potent Activator of T-Lymphocyte Functions1995In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 25, no 1, p. 159-165Article in journal (Refereed)
    Abstract [en]

    During inflammatory processes infiltrating cells produce large amounts of reactive oxygen intermediates (ROI). Increasing evidence suggests that ROI besides being cytotoxic may act as important mediators influencing various cellular and immunological processes. In this study, we have investigated the effects of hydrogen peroxide on several aspects of lymphocyte activation. In ESb-L T lymphoma cells, micromolar concentrations of hydrogen peroxide rapidly induced activation of the transcription factor NF-kappa B, whereas DNA-binding activity of the transcription factor AP-1 was virtually not affected. In addition, hydrogen peroxide induced early gene expression of interleukin-2 (IL-2) and the IL-2 receptor alpha chain. The stimulation of IL-2 expression was found to be conferred by a kappa B-like cis-regulatory region within the IL-2 gene promoter. In contrast to these activating effects, addition of hydrogen peroxide was largely inhibitory on cell proliferation which is consistent with a general requirement of thiol compounds for lymphocyte proliferation. However, hydrogen peroxide significantly increased T cell proliferation when applied for a short period under reducing conditions. These data indicate that ROI may act as an important competence signal in T lymphocytes inducing early gene expression as well as cell proliferation.

  • 8.
    Lukin, Kara
    et al.
    National Jewish Health.
    Fields, Scott
    National Jewish Health.
    Guerrettaz, Lisa
    National Jewish Health.
    Straign, Desiree
    National Jewish Health.
    Rodriguez, Valerie
    National Jewish Health.
    Zandi, Sasan
    Linköping University, Department of Clinical and Experimental Medicine, Experimental Hematology. Linköping University, Faculty of Health Sciences.
    Mansson, Robert
    Lund Strategic Centre for Stem Cell Biology.
    Cambier, John C.
    National Jewish Health.
    Sigvardsson, Mikael
    Linköping University, Department of Clinical and Experimental Medicine, Experimental Hematology. Linköping University, Faculty of Health Sciences.
    Hagman, James
    National Jewish Health.
    A dose-dependent role for EBF1 in repressing non-B-cell-specific genes2011In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 41, no 6, p. 1787-1793Article in journal (Refereed)
    Abstract [en]

    In the absence of early B-cell factor 1 (EBF1), B-cell development is arrested at an uncommitted progenitor stage that exhibits increased lineage potentials. Previously, we investigated the roles of EBF1 and its DNA-binding partner Runx1 by evaluating B lymphopoiesis in single (EBF1(het) and Runx1(het)) and compound haploinsufficent (Ebf1(+/-) Runx1(+/-), ER(het)) mice. Here, we demonstrate that decreased Ebf1 gene dosage results in the inappropriate expression of NK-cell lineage-specific genes in B-cell progenitors. Moreover, prolonged expression of Ly6a/Sca-1 suggested the maintenance of a relatively undifferentiated phenotype. These effects were exacerbated by reduced expression of Runx1 and occurred despite expression of Pax5. Repression of inappropriately expressed genes was restored in most pre-B and all immature B cells of ER(het) mice. Enforced EBF1 expression repressed promiscuous transcription in pro-B cells of ER(het) mice and in Ebf1(-/-) Pax5(-/-) fetal liver cells. Together, our studies suggest that normal levels of EBF1 are critical for maintaining B-cell identity by directing repression of non-B-cell-specific genes.

  • 9.
    Mansson, R.
    et al.
    Månsson, R., Department for Hematopoetic Stem Cell Biology, Lund Stemcell Center, Lund University, S-221 84 Lund, Sweden.
    Lagergren, A.
    Department for Hematopoetic Stem Cell Biology, Lund Stemcell Center, Lund University, S-221 84 Lund, Sweden.
    Hansson, F.
    Department for Hematopoetic Stem Cell Biology, Lund Stemcell Center, Lund University, S-221 84 Lund, Sweden.
    Smith, E.
    Department for Hematopoetic Stem Cell Biology, Lund Stemcell Center, Lund University, S-221 84 Lund, Sweden.
    Sigvardsson, Mikael
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Clinical and Experimental Medicine, Experimental Hematology .
    The CD53 and CEACAM-1 genes are genetic targets for early B cell factor2007In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 37, no 5, p. 1365-1376Article in journal (Refereed)
    Abstract [en]

    Early B cell factor (EBF)-1 is a transcription factor known to be of critical importance for early B lymphocyte development. EBF-1 has been shown to directly interact with and regulate expression of a set of genes involved in the functional formation of the pre-B cell receptor, but the dramatic phenotype observed in the EBF-1-deficient mice suggests that several additional genes are activated by this protein. In order to identify additional target genes for EBF-1, we transduced a hematopoietic progenitor cell line, BaF/3, with an EBF-1-encoding retrovirus and investigated the induced gene expression pattern by micro-arrays. This analysis suggested that among others, the CD53 and the carcinoembryonic antigen-related cell adhesion molecule (CEAACAM)-1 genes both were induced by ectopic expression of EBF-1. Identification of the 5' end of the cDNA enabled the identification of promoter elements with functional binding sites for EBF-1 and ability to respond to EBF-1 expression in transient transfection assays. These data suggest that CD53 and CEACAM-1 are direct genetic targets for EBF-1, providing additional information concerning the activity of this crucial transcription factor in hematopoiesis. © 2007 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.

  • 10.
    Påhlsson, Peter
    et al.
    Linköping University, Department of Biomedicine and Surgery, Clinical Chemistry. Linköping University, Faculty of Health Sciences.
    Strindhall, Jan
    Linköping University, Department of Biomedicine and Surgery, Clinical Chemistry. Linköping University, Faculty of Health Sciences.
    Srinivas, Uppugunduri
    Hospital Pharmacy, University Hospital, Linköping, Sweden.
    Lundblad, Arne
    Linköping University, Department of Biomedicine and Surgery, Clinical Chemistry. Linköping University, Faculty of Health Sciences.
    Role of N-linked glycosylation in expression of E-selectin on human endothelial cells1995In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 25, no 9, p. 2452-2459Article in journal (Refereed)
    Abstract [en]

    E-selectin is a cytokine-inducible membrane glycoprotein capable of mediating adhesion of leukocytes to endothelial cells. It is highly glycosylated, containing 11 sites for N-linked glycosylation. N-Glycosylation of E-selectin was analyzed by endoglycosidase treatment. Analysis of immunoprecipitated E-selectin from human umbilical vein endothelial cells (HUVEC) by polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate showed that E-selectin was completely resistant to endoglycosidase H, but sensitive to peptide N-glycanase F digestion. This suggested that all N-linked oligosaccharide chains were of the complex type. The role of N-linked glycosylation in surface expression and secretion of E-selectin was studied using interleukin-1-stimulated HUVEC, cultured in the presence of the soluble glycosylation inhibitors tunicamycin or castanospermine. Cell surface expression was analyzed by indirect flow cytometry. N-Glycosylation was blocked by tunicamycin, and resulted in a significantly reduced surface expression of E-selectin, whereas castanospermine only marginally reduced E-selectin expression. The deglycosylated forms of E-selectin were also found to be fully capable of mediating adhesion of HT-29 cells in vitro. In conclusion, these studies show that E-selectin is heavily glycosylated with complex type N-linked oligosaccharides and that N-glycosylation is important for expression of E-selectin on human endothelial cells.

  • 11.
    Sabado, Rachel L.
    et al.
    Department of Medicine and Pathology, School of Medicine, New York University, New York, NY, United States.
    Babcock, Ethan
    Department of Medicine and Pathology, School of Medicine, New York University, New York, NY, United States.
    Kavanagh, Daniel G.
    Department of Medicine and Pathology, School of Medicine, New York University, New York, NY, United States, Partner AIDS Research Center, Massachusetts General Hospital, Charlestown, MA, United States.
    Tjomsland, Veronica
    Linköping University, Department of Clinical and Experimental Medicine, Molecular Virology. Linköping University, Faculty of Health Sciences.
    Walker, Bruce D.
    Partner AIDS Research Center, Massachusetts General Hospital, Charlestown, MA, United States, Howard Hughes Medical Institute, Chevy Chase, MD, United States.
    Lifson, Jeffrey D.
    AIDS Vaccine Program, SAIC-Frederick Inc., National Cancer Institute at Frederick, Frederick, MD, United States.
    Bhardwaj, Nina
    Department of Medicine and Pathology, School of Medicine, New York University, New York, NY, United States.
    Larsson, Marie
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Clinical and Experimental Medicine, Molecular Virology.
    Pathways utilized by dendritic cells for binding, uptake, processing and presentation of antigens derived from HIV-12007In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 37, no 7, p. 1752-1763Article in journal (Refereed)
    Abstract [en]

    The outcome following HIV infection depends on the nature and durability of the HIV-specific T cell response induced initially. The activation of protective T cell responses depends upon dendritic cells (DC), antigen-presenting cells which have the capacity to process and present viral antigens. DC pulsed with aldrithiol-2-inactivated HIV and delivered in vivo were reported to induce immune responses and promote virologic control in chronically HIV-1-infected subjects. To gain an understanding of this phenomenon, we characterized the steps involved in the presentation of antigens derived from aldrithiol-2-treated vs. infectious HIV-1 by DC. Antigen presentation, on both MHC class I and II, was independent of DC-specific ICAM-3-grabbing integrin, DEC-205 and macrophage mannose receptor, C-type lectins expressed by the DC. Inhibitor studies showed that presentation on MHC class I was dependent on viral fusion in a CD4/coreceptor-dependent manner, both at the cell surface and within endosomes, and access to the classical endosomal processing pathway. MHC class II presentation of HIV-associated antigens was dependent on active endocytosis, probably receptor-mediated, and subsequent degradation of virions in acidified endosomes in the DC. Our study brings forth new facts regarding the binding, uptake, and processing of chemically inactivated virions leading to efficient antigen presentation and should aid in the design of more effective HIV vaccines. © 2007 Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim.

  • 12.
    Tjomsland, Veronica
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Molecular Virology. Linköping University, Faculty of Health Sciences.
    Ellegård, Rada
    Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Health Sciences.
    Burgener, Adam
    University of Manitoba, Canada.
    Mogk, Kenzie
    University of Manitoba, Canada.
    Fru Che, Karlhans
    Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Health Sciences.
    Westmacott, Garrett
    National Microbiol Lab, Canada.
    Hinkula, Jorma
    Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Health Sciences.
    Lifson, Jeffrey D.
    SAIC Frederick Inc, MD USA.
    Larsson, Marie
    Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Health Sciences.
    Complement opsonization of HIV-1 results in a different intracellular processing pattern and enhanced MHC class I presentation by dendritic cells2013In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 43, no 6, p. 1470-1483Article in journal (Refereed)
    Abstract [en]

    Induction of optimal HIV-1-specific T-cell responses, which can contribute to controlling viral infection in vivo, depends on antigen processing and presentation processes occurring in DCs. Opsonization can influence the routing of antigen processing and pathways used for presentation. We studied antigen proteolysis and the role of endocytic receptors in MHC class I (MHCI) and II (MHCII) presentation of antigens derived from HIV-1 in human monocyte-derived immature DCs (IDCs) and mature DCs, comparing free and complement opsonized HIV-1 particles. Opsonization of virions promoted MHCI presentation by DCs, indicating that complement opsonization routes more virions toward the MHCI presentation pathway. Blockade of macrophage mannose receptor (MMR) and β7-integrin enhanced MHCI and MHCII presentation by IDCs and mature DCs, whereas the block of complement receptor 3 decreased MHCI and MHCII presentation. In addition, we found that IDC and MDC proteolytic activities were modulated by HIV-1 exposure; complement-opsonized HIV-1 induced an increased proteasome activity in IDCs. Taken together, these findings indicate that endocytic receptors such as MMR, complement receptor 3, and β7-integrin can promote or disfavor antigen presentation probably by routing HIV-1 into different endosomal compartments with distinct efficiencies for degradation of viral antigens and MHCI and MHCII presentation, and that HIV-1 affects the antigen-processing machinery.

  • 13.
    Tjomsland, Veronica
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Molecular Virology. Linköping University, Faculty of Health Sciences.
    Ellegård, Rada
    Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Health Sciences.
    Kjölhede, Preben
    Linköping University, Department of Clinical and Experimental Medicine, Division of Clinical Sciences. Linköping University, Faculty of Health Sciences. Östergötlands Läns Landsting, Center of Paediatrics and Gynaecology and Obstetrics, Department of Gynaecology and Obstetrics in Linköping.
    Borendal Wodlin, Ninni
    Linköping University, Department of Clinical and Experimental Medicine. Linköping University, Faculty of Health Sciences.
    Hinkula, Jorma
    Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Health Sciences.
    Lifson, Jeffrey
    SAIC/Fredrick, National Cancer Institute at Fredrick, Frederick, Maryland, USA.
    Larsson, Marie
    Linköping University, Department of Clinical and Experimental Medicine, Division of Microbiology and Molecular Medicine. Linköping University, Faculty of Health Sciences.
    Blocking of integrins inhibits HIV-1 infection of human cervical mucosa immune cells with free and complement-opsonized virions2013In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 43, no 9, p. 2361-2372Article in journal (Refereed)
    Abstract [en]

    The initial interaction between HIV-1 and the host occurs at the mucosa during sexual intercourse. In cervical mucosa, HIV-1 exists both as free and opsonized virions and this might influence initial infection. We used cervical explants to study HIV-1 transmission, the effects of opsonization on infectivity, and how infection can be prevented. Complement opsonization enhanced HIV-1 infection of dendritic cells (DCs) compared with that by free HIV-1, but this increased infection was not observed with CD4+ T cells. Blockage of the α4-, β7-, and β1-integrins significantly inhibited HIV-1 infection of both DCs and CD4+ T cells. We found a greater impairment of HIV-1 infection in DCs for complement-opsonized virions compared with that of free virions when αM/β2- and α4-integrins were blocked. Blocking the C-type lectin receptor macrophage mannose receptor (MMR) inhibited infection of emigrating DCs but had no effect on CD4+ T-cell infection. We show that blocking of integrins decreases the HIV-1 infection of both mucosal DCs and CD4+ T cells emigrating from the cervical tissues. These findings may provide the basis of novel microbicidal strategies that may help limit or prevent initial infection of the cervical mucosa, thereby reducing or averting systemic HIV-1 infection.

  • 14.
    Ying, Fei
    et al.
    Affiliated Hospital, Guiyang Medical College.
    Chalise, Jaya Prakash
    Linköping University, Department of Clinical and Experimental Medicine, Rheumatology. Linköping University, Faculty of Health Sciences.
    Chenna Narendra, Sudeep
    Linköping University, Department of Clinical and Experimental Medicine, Rheumatology. Linköping University, Faculty of Health Sciences.
    Magnusson, Mattias
    Linköping University, Department of Clinical and Experimental Medicine, Rheumatology. Linköping University, Faculty of Health Sciences.
    Type I IFN protects against antigen-induced arthritis2011In: European Journal of Immunology, ISSN 0014-2980, E-ISSN 1521-4141, Vol. 41, no 6, p. 1687-1695Article in journal (Refereed)
    Abstract [en]

    Autoimmune diseases including rheumatoid arthritis (RA) involve immune reactions against specific antigens. The type I IFN system is suspected to promote autoimmunity in systemic lupus erythematosus, but may also dampen immune reactions in e. g. inflammatory bowel disease. This prompted us to investigate the role of type I IFN in antigen-induced arthritis (AIA). The importance of type I IFN in methylated (m) BSA-induced arthritis was studied by using mice deficient for the type I IFN receptor (IFNAR) and by administration of the IFN-alpha activator viral double-stranded (ds) RNA or recombinant IFN-alpha at antigen sensitization. In IFNAR knock-out mice, arthritis severity was significantly higher than in WT mice. Administration of dsRNA at antigen sensitization protected WT but not IFNAR KO mice from arthritis. Also, addition of recombinant IFN-alpha during the immunization, but not the induction phase of arthritis, almost abolished arthritis. Protection mediated by IFN-alpha was accompanied by delayed and decreased antigen-specific proliferative responses, including impaired lymph node recall responses after intra-articular antigenic challenge. In conclusion, we demonstrate that type I IFN can prevent joint inflammation by downregulating antigen-specific cellular immunity.

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