Lectins inhibit the Aujeszky's disease virus-induced interferon-alpha production of porcine peripheral blood mononuclear cells.

The interaction between virus and peripheral blood mononuclear cells (PBMC) required to elicit the production of interferon-alpha (IFN-alpha) by the so-called natural interferon-producing cell is unknown. However, results from inhibition experiments suggest that viral glycoproteins are essential in this IFN induction process. We demonstrate here that cellular glycoproteins also appear to be involved in the initiation of IFN-alpha production. Lectins, that is, sugar binding glycoproteins, inhibited the Aujeszky's disease virus-induced IFN-alpha production of porcine PBMC by up to 99%. The level of inhibition varied with lectin used (concanavalin A, Galanthus nivalis lectin, Helix pomatia lectin, and lentil lectin). Preincubation experiments with porcine cells and concanavalin A (ConA) revealed that the lectin exerted its major effect directly on the PBMC. Although the IFN-alpha production in some cases was reduced by more than 90%, the PBMC were still able to proliferate in response to mitogenic lectins. The ConA-mediated inhibition of the IFN-alpha production was reduced if the lectin was added later than 6-8 h after the start of induction and was not mediated by soluble factors. Both orthovanadate and staurosporine inhibited the IFN-alpha production and did not relieve the ConA-mediated inhibition. Thus, ConA seems to interfere with the early events during IFN-alpha induction, but the mechanisms behind this interference could not be clarified.

[1]  A. Scheynius,et al.  Interferon‐α Production and Tissue Localization of Interferon‐α/β Producing Cells after Intradermal Administration of Aujeszky's Disease Virus–Infected Cells in Pigs , 1995, Scandinavian journal of immunology.

[2]  B. Charley,et al.  Enrichment of coronavirus-induced interferon-producing blood leukocytes increases the interferon yield per cell: A study with pig leukocytes , 1993, Research in Immunology.

[3]  P. Fitzgerald-Bocarsly Human natural interferon-α producing cells , 1993, Pharmacology & Therapeutics.

[4]  P. Erb,et al.  Effects of a new protein kinase C inhibitor CGP 41251 on T cell functions: inhibition of activation, growth, and target cell killing. , 1993, Cellular Immunology.

[5]  G. Schieven,et al.  Ionizing radiation stimulates unidentified tyrosine-specific protein kinases in human B-lymphocyte precursors, triggering apoptosis and clonogenic cell death. , 1992, Proceedings of the National Academy of Sciences of the United States of America.

[6]  P. Maher Stimulation of endothelial cell proliferation by vanadate is specific for microvascular endothelial cells , 1992, Journal of cellular physiology.

[7]  D. Golan,et al.  Differential activation of phosphotyrosine protein phosphatase activity in a murine T cell hybridoma by monoclonal antibodies to CD45. , 1992, The Journal of biological chemistry.

[8]  H. Laude,et al.  Single amino acid changes in the viral glycoprotein M affect induction of alpha interferon by the coronavirus transmissible gastroenteritis virus , 1992, Journal of virology.

[9]  K. Artursson,et al.  A sensitive immunoassay for porcine interferon-α , 1992 .

[10]  V. Everts,et al.  Phagocytosis of collagen fibrils by periosteal fibroblasts in long bone explants. Effect of concanavalin A. , 1992, Tissue & cell.

[11]  A. Gobl,et al.  Phorbol ester-mediated inhibition of IFN-alpha/beta gene transcription in blood mononuclear leukocytes. , 1991, Journal of immunology.

[12]  B. Fredholm,et al.  Translocation of the α‐ and β‐isoforms of protein kinase C following activation of human T‐lymphocytes , 1991 .

[13]  B. Delmas,et al.  Glycosylation is Required for Coronavirus TGEV to Induce an Efficient Production of IFNα by Blood Mononuclear Cells , 1991, Scandinavian journal of immunology.

[14]  F. Lefèvre,et al.  Production of an hybridoma library to recombinant porcine alpha I interferon: a very sensitive assay (ISBBA) allows the detection of a large number of clones. , 1991, Hybridoma.

[15]  T. Mustelin,et al.  Phosphotyrosine phosphatases are involved in reversion of T lymphoblastic proliferation , 1990, European journal of immunology.

[16]  M. Courreges,et al.  Meliacine, an antiviral compound from Melia azedarach L., inhibits interferon production. , 1990, Journal of interferon research.

[17]  P. Matsson,et al.  A distinct population of nonphagocytic and low level CD4+ null lymphocytes produce IFN-alpha after stimulation by herpes simplex virus-infected cells. , 1990, Journal of immunology.

[18]  F. Lefèvre,et al.  Production, purification and biological properties of an Escherichia coli-derived recombinant porcine alpha interferon. , 1990, The Journal of general virology.

[19]  P. Wallgren,et al.  Appearance of interferon-alpha in serum and signs of reduced immune function in pigs after transport and installation in a fattening farm. , 1989, Veterinary immunology and immunopathology.

[20]  E. Dodson,et al.  The structure of the saccharide‐binding site of concanavalin A. , 1989, The EMBO journal.

[21]  P. Kiener,et al.  CD45-protein tyrosine phosphatase cross-linking inhibits T cell receptor CD3-mediated activation in human T cells. , 1989, Journal of immunology.

[22]  K. Funa,et al.  Characterization of the Blood Mononuclear Leucocytes Producing Alpha Interferon after Stimulation with Herpes Simplex Virus in Vitro, by Means of Combined Immunohistochemical Staining and in Situ RNA‐RNA Hybridization , 1989, Scandinavian journal of immunology.

[23]  N. Tonks,et al.  CD45 regulates signal transduction and lymphocyte activation by specific association with receptor molecules on T or B cells. , 1988, Proceedings of the National Academy of Sciences of the United States of America.

[24]  E. Damonte,et al.  Induction of a refractory state to viral infection in mammalian cells by a plant inhibitor isolated from leaves of Melia azedarach L. , 1988, Antiviral research.

[25]  T. Maniatis,et al.  2-Aminopurine selectively inhibits the induction of beta-interferon, c-fos, and c-myc gene expression. , 1988, Science.

[26]  P. Fitzgerald-Bocarsly,et al.  Human Mononuclear Cells Which Produce Interferon‐Alpha During NK(HSV‐FS) Assays Are HLA‐DR Positive Cells Distinct From Cytolytic Natural Killer Effectors , 1988, Journal of leukocyte biology.

[27]  H. Laude,et al.  Induction of alpha interferon by transmissible gastroenteritis coronavirus: role of transmembrane glycoprotein E1 , 1988, Journal of virology.

[28]  G. Trinchieri,et al.  Requirement for HLA-DR+ accessory cells in natural killing of cytomegalovirus-infected fibroblasts , 1986, The Journal of experimental medicine.

[29]  P. Lebon Inhibition of herpes simplex virus type 1-induced interferon synthesis by monoclonal antibodies against viral glycoprotein D and by lysosomotropic drugs. , 1985, The Journal of general virology.

[30]  J. Lunney,et al.  Preparation and characterization of monoclonal antibodies reactive with porcine PBL. , 1984, Journal of immunology.

[31]  E. Tokunaga,et al.  Treatment of human peripheral blood leukocytes with proteases does not affect Sendai virus-induced interferon production , 1984, Infection and immunity.

[32]  H. Eisen,et al.  Isolation and partial characterization of concanavalin A receptors on cloned cytotoxic T lymphocytes. , 1984, Proceedings of the National Academy of Sciences of the United States of America.

[33]  F. Deinhardt,et al.  Phenotype of human alpha-interferon producing leucocytes identified by monoclonal antibodies. , 1983, Clinical and experimental immunology.

[34]  J. Parker,et al.  Lymphocyte receptors for polyclonal T mitogens. II. High-molecular-weight glycoproteins are the best candidate sites for mitogenic action by concanavalin A and galactose oxidase. , 1982, Cellular immunology.

[35]  I. Goldstein,et al.  What should be called a lectin? , 1980, Nature.

[36]  P. Edelson,et al.  EFFECTS OF CONCANAVALIN A ON MOUSE PERITONEAL MACROPHAGES , 1974, The Journal of experimental medicine.

[37]  I. Goldstein,et al.  Protein-carbohydrate interaction. XX. On the number of combining sites on concanavalin A, the phytohemagglutinin of the jack bean. , 1968, Biochimica et biophysica acta.