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4. Recombinant Viruses as Vectors for Mucosal Immunity

Author

Morrow, C. D., Novak, M. J., Ansardi, D. C., Porter, D. C., Moldoveanu, Z., Compans, R. W., editor, Cooper, M., editor, Hogle, J. M., editor, Ito, Y., editor, Koprowski, H., editor, Melchers, F., editor, Oldstone, M., editor, Olsnes, S., editor, Potter, M., editor, Saedler, H., editor, Vogt, P. K., editor, Wagner, H., editor, Kraehenbuhl, Jean-Pierre, editor, and Neutra, Marian R., editor

Published
1999
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13. Systemic Immunization for the Induction of IgA Responses

Author

Tarkowski, A., Lue, C., Moldoveanu, Z., Kiyono, H., McGhee, J. R., Prchal, J. T., Halpern, N. B., Mestecky, J., Compans, R. W., editor, Cooper, M., editor, Koprowski, H., editor, McConell, I., editor, Melchers, F., editor, Oldstone, M., editor, Olsnes, S., editor, Saedler, H., editor, Vogt, P. K., editor, Wagner, H., editor, Wilson, I., editor, Mestecky, Jiri, editor, and McGhee, Jerry R., editor

Published
1989
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14. Immune Responses to Influenza Virus in Orally and Systemically Immunized Mice

Author

Moldoveanu, Z., Staas, J. K., Gilley, R. M., Ray, R., Compans, R. W., Eldridge, J. H., Tice, T. R., Mestecky, J., Compans, R. W., editor, Cooper, M., editor, Koprowski, H., editor, McConell, I., editor, Melchers, F., editor, Oldstone, M., editor, Olsnes, S., editor, Saedler, H., editor, Vogt, P. K., editor, Wagner, H., editor, Wilson, I., editor, Mestecky, Jiri, editor, and McGhee, Jerry R., editor

Published
1989
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15. Biodegradable Microspheres: Vaccine Delivery System for Oral Immunization

Author

Eldridge, J. H., Gilley, R. M., Staas, J. K., Moldoveanu, Z., Meulbroek, J. A., Tice, T. R., Compans, R. W., editor, Cooper, M., editor, Koprowski, H., editor, McConell, I., editor, Melchers, F., editor, Oldstone, M., editor, Olsnes, S., editor, Saedler, H., editor, Vogt, P. K., editor, Wagner, H., editor, Wilson, I., editor, Mestecky, Jiri, editor, and McGhee, Jerry R., editor

Published
1989
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16. Reactivities of N-acetylgalactosamine-specific lectins with human IgA1 proteins

Author

Moore, J.S., Kulhavy, R., Tomana, M., Moldoveanu, Z., Suzuki, H., Brown, R., Hall, S., Kilian, Mogens, Poulsen, Knud, Mestecky, J., Julian, B.A., and Novak, J.

Subjects
carbohydrates (lipids)
Abstract

Lectins are proteins with specificity of binding to certain monosaccharides or oligosaccharides. They can detect abnormal glycosylation patterns on immunoglobulins in patients with various chronic inflammatory diseases, including rheumatoid arthritis and IgA nephropathy (IgAN). However, lectins exhibit binding heterogeneity, depending on their source and methods of isolation. To characterize potential differences in recognition of terminal N-acetylgalactosamine (GalNAc) on IgA1, we evaluated the binding characteristics of several commercial preparations of GalNAc-specific lectins using a panel of IgA1 and, as controls, IgA2 and IgG myeloma proteins. These lectins originated from snails Helix aspersa (HAA) and Helix pomatia (HPA), and the plant Vicia villosa (VV). Only HAA and HPA bound exclusively to IgA1, with its O-linked glycans composed of GalNAc, galactose, and sialic acid. In contrast, VV reacted with sugars of both IgA subclasses and IgG, indicating that it also recognized N-linked glycans without GalNAc. Furthermore, HAA and HPA from several manufacturers differed in their ability to bind various IgA1 myeloma proteins and other GalNAc-containing glycoproteins in ELISA and Western blot. For serum samples from IgAN patients, HAA was the optimal lectin to study IgA1 glycosylation in ELISA and Western blot assays, including identification of the sites of attachment of the aberrant glycans. The galactose-deficient glycans were site-specific, localized mostly at Thr228 and/or Ser230. Because of the heterogeneity of GalNAc-specific lectins, they should be carefully characterized with appropriate substrates before undertaking any study.

Published
2007

17. IgA Nephropathy and Henoch-Schoenlein Purpura Nephritis: Aberrant Glycosylation of IgA1, Formation of IgA1-Containing Immune Complexes, and Activation of Mesangial Cells

Author

Novak, J., Moldoveanu, Z., Renfrow, M.B., Yanagihara, T., Suzuki, H., Raska, M., Hall, S., Brown, R., Huang, W-Q, Goepfert, A., Kilian, Mogens, Poulsen, Knud, Tomana, M., Wyatt, R.J., Julian, B.A., and Mestecky, J.

Subjects
fluids and secretions, stomatognathic system, chemical and pharmacologic phenomena
Abstract

IgA1 in the circulation and glomerular deposits of patients with IgA nephropathy (IgAN) is aberrantly glycosylated; the hinge-region O-linked glycans are galactose-deficient. The circulating IgA1 of patients with Henoch-Schoenlein purpura nephritis (HSPN) has a similar defect. This aberrancy exposes N-acetylgalactosamine-containing neoepitopes recognized by naturally occurring IgG or IgA1 antibodies resulting in formation of immune complexes. IgA1 contains up to six O-glycosylation sites per heavy chain; it is not known whether the glycosylation defect occurs randomly or preferentially at specific sites. We sought to define the aberrant glycosylation of a galactose-deficient IgA1 myeloma protein and analyze the formation of the immune complexes and their biological activities. Supplementation of serum or cord-blood serum with this IgA1 protein resulted in formation of new IgA1 complexes. These complexes stimulated proliferation of cultured human mesangial cells, as did the naturally-occurring IgA1-containing complexes from sera of patients with IgAN and HSPN. Uncomplexed IgA1 did not affect cellular proliferation. Using specific proteases, lectin Western blots, and mass spectrometry, we determined the O-glycosylation sites in the hinge region of the IgA1 myeloma protein and IgA1 proteins from sera of IgAN patients. The IgA1 myeloma protein had galactose-deficient sites at residues 228 and/or 230 and 232. These sites reacted with IgG specific to galactose-deficient IgA1. IgA1 from the IgAN patients had galactose-deficient O-glycans at the same residues. In summary, we identified the neoepitopes on IgA1 responsible for formation of the pathogenic immune complexes. These studies may lead to development of noninvasive diagnostic assays and future disease-specific therapy.

Published
2007

22. Immune and inflammatory mechanisms

Author

Mangieri, D., primary, Palmisano, A., additional, Libri, I., additional, Corradi, D., additional, Carnevali, M. L., additional, Buzio, C., additional, Vaglio, A., additional, Zikou, X., additional, Rousouli, K., additional, Tellis, C., additional, Tselepis, A., additional, Siamopoulos, K., additional, Zawada, A. M., additional, Rogacev, K. S., additional, Rotter, B., additional, Winter, P., additional, Marell, R. R., additional, Fliser, D., additional, Heine, G. H., additional, Fligny, C., additional, Milon, M., additional, Huang, J., additional, Schordan, S., additional, Mesnard, L., additional, Endlich, N., additional, Tharaux, P.-L., additional, Yurkevich, M., additional, Komissarov, K., additional, Pilotovich, V., additional, Zafranskaya, M., additional, Smykal-Jankowiak, K., additional, Niemir, Z., additional, Polcyn-Adamczak, M., additional, Szramka-Pawlak, B., additional, Zaba, R., additional, Wornle, M., additional, Ribeiro, A., additional, Merkle, M., additional, Hiemstra, T. F., additional, Charles, P. D., additional, Hester, S. S., additional, Al-Lamki, R., additional, Su, Y., additional, Robinson, C., additional, Floto, R. A., additional, Lilley, K. S., additional, Karet, F. E., additional, Wu, C.-C., additional, Lu, K.-C., additional, Chen, J.-S., additional, Lin, Y.-F., additional, Sytwu, H.-K., additional, Esposito, P., additional, Gabanti, E., additional, Bianzina, S., additional, Rampino, T., additional, Dal Canton, A., additional, Hung, K.-Y., additional, Lang, C.-L., additional, Liu, S.-Y., additional, Rakityanskaya, I., additional, Ryabova, T., additional, Novak, J., additional, Suzuki, H., additional, Yamada, K., additional, Moldoveanu, Z., additional, Takahashi, K., additional, Horynova, M., additional, Novakova, J., additional, Julian, B. A., additional, Novak, L., additional, Poulsen, K., additional, Kilian, M., additional, Gharavi, A. G., additional, Renfrow, M. B., additional, Mestecky, J., additional, Raska, M., additional, Camilla, R., additional, Loiacono, E., additional, Dapra, V., additional, Morando, L., additional, Peruzzi, L., additional, Conrieri, M., additional, Bianciotto, M., additional, Bosetti, F. M., additional, Gallo, R., additional, Amore, A., additional, Coppo, R., additional, Ito, S., additional, Higuchi, Y., additional, Nishijima, F., additional, Yamato, H., additional, Ishii, H., additional, Yoshida, M., additional, Na, K. Y., additional, Oh, S.-W., additional, Chin, H. J., additional, Chae, D.-W., additional, Oh, Y. K., additional, Joo, K. W., additional, Han, J. S., additional, Mazanowska, O., additional, Kaminska, D., additional, Krajewska, M., additional, Zabinska, M., additional, Kopec, W., additional, Boratynska, M., additional, Klinger, M., additional, Cohen, G., additional, Raupachova, J., additional, Borchhardt, K., additional, Horl, W. H., additional, Pletinck, A., additional, Glorieux, G., additional, Schepers, E., additional, Van Landschoot, M., additional, Van De Voorde, J., additional, Van Biesen, W., additional, Vanholder, R., additional, Bansal, V., additional, Davis, R., additional, Litinas, E., additional, Hoppensteadt, D., additional, Fareed, J., additional, Abdgawad, M., additional, Gunnarsson, L., additional, Segelmark, M., additional, Hellmark, T., additional, Izuka, I., additional, Quinto, B., additional, Goes, M., additional, Monte, J., additional, Pavao, O., additional, Santos, B., additional, Pereira, V., additional, Dalboni, M., additional, Cendoroglo, M., additional, Batista, M., additional, Durao, M., additional, Lai, C.-F., additional, Lin, S.-L., additional, Chen, Y.-M., additional, Chiang, W.-C., additional, Wu, K.-D., additional, Kuo, M.-L., additional, and Tsai, T.-J., additional

Published
2011
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23. Oral tolerance in humans. T cell but not B cell tolerance after antigen feeding

Author

Steffen Husby, Mestecky J, Moldoveanu Z, Holland S, and Co, Elson

Subjects
Adult, Male, B-Lymphocytes, Injections, Subcutaneous, T-Lymphocytes, Immunology, Administration, Oral, In Vitro Techniques, Lymphocyte Activation, Antibody Formation, Hemocyanins, Immune Tolerance, Immunology and Allergy, Humans, Female, Hypersensitivity, Delayed, Immunization, Antigens, Intestinal Mucosa, Saliva
Abstract

The purpose of this study was to investigate whether oral tolerance, defined as Ag-specific immunologic unresponsiveness after Ag feeding, could be induced in humans after prolonged Ag ingestion. Eight adult volunteers ingested a total dose of 0.5 g of keyhole limpet hemocyanin (KLH) followed by subcutaneous immunization with KLH. Eight controls received only the subcutaneous immunization. In the group fed KLH, there was a significant reduction in KLH-specific T cell proliferation (p = 0.04) and delayed skin test responses (p = 0.07) to KLH. KLH ingestion alone did not induce significant levels of Abs in either serum or secretions. However, after the subsequent subcutaneous immunization, the number of circulating IgG and IgM anti-KLH-producing cells, the titers of serum IgG, IgA, and IgM anti-KLH Abs, and the titers of IgA anti-KLH Abs in saliva and intestinal secretions were significantly greater in the KLH-fed group than in the nonfed group. We conclude that KLH feeding induced systemic T cell tolerance, but B cell priming, at both systemic and mucosal sites. These studies support the concept of using Ag feeding as a treatment for certain immune-mediated diseases.

Published
1994

25. P19-46. Co-delivery of mucosal chemokine plasmids in a systemically delivered DNA vaccine elicits systemic and mucosal immune responses in mice and macaques

Author

Kraynyak, KA, primary, Kutzler, MA, additional, Pahar, B, additional, Sylvester, A, additional, Yan, J, additional, Carnathan, D, additional, Khan, AS, additional, Sardesai, N, additional, Moldoveanu, Z, additional, Mestecky, J, additional, Betts, MR, additional, Marx, P, additional, and Weiner, DB, additional

Published
2009
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40. Aberrant glycosylation of IgA1 is inherited in both pediatric IgA nephropathy and Henoch-Schönlein purpura nephritis.

Author

Kiryluk K, Moldoveanu Z, Sanders JT, Eison TM, Suzuki H, Julian BA, Novak J, Gharavi AG, Wyatt RJ, Kiryluk, Krzysztof, Moldoveanu, Zina, Sanders, John T, Eison, T Matthew, Suzuki, Hitoshi, Julian, Bruce A, Novak, Jan, Gharavi, Ali G, and Wyatt, Robert J

Subjects
*AGING, *BIOMARKERS, *BIOLOGICAL models, *GLOMERULONEPHRITIS, *GLYCOSYLATION, *IMMUNOGLOBULINS, *LONGITUDINAL method, *NEPHRITIS, *RESEARCH funding, *CASE-control method, *SCHOENLEIN-Henoch purpura
Abstract

Serum galactose-deficient immunoglobulin A1 (Gd-IgA1) is an inherited risk factor for adult IgA nephropathy (IgAN). In this paper, we determined the heritability of serum Gd-IgA1 levels in children with IgAN and Henoch-Schönlein purpura nephritis (HSPN), two disorders with clinical phenotypes sharing common pathogenic mechanisms. Serum Gd-IgA1 concentrations were quantified using a Helix aspersa-lectin-based enzyme-linked immunosorbent assay. As a group, 34 children with either disorder (20 with HSPN and 14 with IgAN) had significantly higher Gd-IgA1 levels compared with 51 age- and ethnicity-matched pediatric controls. Serum levels of Gd-IgA1 were also elevated in a large fraction of 54 first-degree relatives of pediatric IgAN and HSPN patients compared with 141 unrelated healthy adult controls. A unilineal transmission of the trait was found in 17, bilineal transmission in 1, and sporadic occurrence in 5 of 23 families when both parents and the patient were analyzed. There was a significant age-, gender-, and household-adjusted heritability of serum galactose-deficient IgA1 estimated at 76% in pediatric IgAN and at 64% in HSPN patients. Thus, serum galactose-deficient IgA1 levels are highly inherited in pediatric patients with IgAN and HSPN, providing support for another shared pathogenic link between these disorders. [ABSTRACT FROM AUTHOR]

Published
2011
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48. High-level dietary vitamin A enhances T-helper type 2 cytokine production and secretory immunoglobulin A response to influenza A virus infection in BALB/c mice.

Author

Cui, Donming, Moldoveanu, Zina, Cui, D, Moldoveanu, Z, and Stephensen, C B

Subjects
VITAMIN A, INFLUENZA, VIRAL pneumonia, PHYSIOLOGY
Abstract

Vitamin A supplementation during acute pneumonia has not improved recovery in most human clinical trials. We hypothesize that high vitamin A intake may decrease the production of T-helper type-1 (Th1) cytokines and thereby inhibit antiviral responses. Such decreases might impair recovery from viral respiratory infections. We thus examined the effect of three interventions on viral pneumonia: 1) a high level vitamin A [250,000 IU/kg diet or 75,000 retinol equivalents (RE)/kg], or 2) control diet (4000 IU/kg diet or 1200 RE/kg) given before and during infection, and 3) initiating the high level diet upon infection to simulate the adjuvant therapy used in clinical trials. No difference was seen among the interventions in severity of disease (weight loss, lung virus titers and survival). However, both the high level diet group and the group in which vitamin A was increased at the time of infection had greater salivary immunoglobulin (Ig)A responses (geometric means, 166 and 105 microg/L, respectively) than did the control group (59 microg/L) (P = 0.0019). In contrast, the serum IgG response was higher in the control group (324+/-158 mg/L) than in the high level group (225+/-95 mg/L) (P = 0.028), although it did not differ from the group in which the diet was changed upon infection (230+/-163 mg/L) (P = 0.084). The production of interferon-gamma (IFN-gamma), a Th1 cytokine, was lower in the high level diet group (median, 0.153 microg/L) compared with the control group (median, 0.839 microg/L) (P = 0.014), whereas the production of interleukin-10 (IL-10), a Th2 cytokine, was higher with the high level diet (median, 0.304 microg/L) than with the control (median, 0.126 microg/L) (P = 0.022). This change in the Th1/Th2 pattern was not sufficient to affect recovery from viral pneumonia but may account for the increased IgA and decreased IgG responses seen with high level dietary vitamin A in this study. These data reinforce the lack of utility of vitamin A in treating acute pneumonia in children and suggest that high dose vitamin A supplements may enhance Th2-mediated immune responses, which are particularly beneficial in the case of extracellular bacterial and parasitic infections and IgA-mediated responses to mucosal infections. [ABSTRACT FROM AUTHOR]

Published
2000
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49. Role of nuclear factor-κ B in the expression by tumor necrosis factor-α of the human polymeric immunoglobulin receptor (pIgR ) gene.

Author

Takenouchi-Ohkubo, N., Takahashi, T., Tsuchiya, M., Mestecky, J., Moldoveanu, Z., and Moro, I.

Subjects
NF-kappa B, TUMOR necrosis factors, IMMUNOGLOBULINS, RNA polymerases, PROTEIN synthesis, GENETIC regulation
Abstract

We analyzed the mechanism of human polymeric immunoglobulin receptor (pIgR) gene upregulation by tumor necrosis factor (TNF)-α. Northern blot analysis showed that the expression of pIgR mRNA was enhanced by TNF-α stimulation. This activation was completely inhibited by RNA polymerase or protein synthesis inhibitors, suggesting that the regulation of pIgR gene expression depends on de novo RNA and protein synthesis. Furthermore, the stimulation of pIgR mRNA by TNF-α was decreased by pyrrolidinedithiocarbamate and l-1-4′-tosylamino-phenylethyl-chloromethyl ketone, which are known nuclear factor (NF)-κB inhibitors. For further analysis of gene regulation, we cloned and sequenced the 1.5-kb 5′-flanking region of the pIgR gene. In the upstream region, we found two NF-κB-binding motifs (named κB1 and κB2 from the 5′ region). An electrophoretic mobility shift assay indicated that two components of the NF-κB/Rel family, p50 and p65, bound with higher affinity to the κB2 element than to the κB1 element. We also analyzed pIgR gene expression using reporter plasmids expressing the firefly luciferase gene. Stimulation by TNF-α significantly activated the pIgR gene promoter, as a 775-bp upstream region of the pIgR gene increased luciferase gene expression in cells treated with TNF-α. The activation of promoter activity by TNF-α was abolished when a mutation was inserted into κB1 or κB2. These data indicated that pIgR gene expression induced by TNF-α is transcriptionally regulated via activation of NF-κB. In addition, there is a possibility that another factor may act in concert with NF-κB. [ABSTRACT FROM AUTHOR]

Published
2000
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