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4. Poster

Author

Spielmann, H., Heuer, J., Grune-Wolff, B., Liebsch, M., Dörendahl, A., Skolik, S., Traue, D., Scheuber, H.-P., Brill, T., Gruber, K., Weichselbaum, J., Maderbacher, R., Stockinger, L., Hlinak, A., Marx, U., Leibiger, H., Kruse, D., Koch, S., Schade, R., Schniering, A., Salén, J. C. W., Himmler, G., Öppling, V., Peter, M., Giess, S., Cußler, K., Gyra, H., Hacker, A., Vogel, I., Gerstl, F., Korencan, A., Kukral, U., Pöhland, R., Schneider, F., Kanitz, W., Schober-Bendixen, S., Kalweit, S., Döring, B., Haupt, R., Gerner, I., Wirnsperger, T., L’Eplattenier, H., Meister, L., Pfannkuch, F., Graepel, P., Bentley, P., Giessler, J., Hirschelmann, R., Rickinger, O., Hintze-Podufal, Ch., Vetter, R., Graeve, T., Noll, M., Schneider, A., Wissler, J. H., Johann, S., Mikorey, S., Lederer, T., Krauss, W., Blümel, G., Reinitzer, D., Chen, T. S., Koutsilieri, E., Kanaya, K., Rausch, W.-D., Siegl, H., Schima, H., Huber, L., Melvin, D., Müller, M. R., Prodinger, A., Losert, U., Wolner, E., Grau, M., Bienert, H., Richter, H. A., Kaden, P., Mittermayer, C., Bremer, S., Pohl, I., Pöting, A., Klein, G., Vogel, R., Pelzmann, B., Koidl, B., Renhardt, M., Wach, P., Tilg, B., Fleischmann, P., Killmann, R., Dienstl, F., Heistracher, T., Krause, E., Kästner, R., Mertz, B., Novakovic, L., Spähni, M., Knapp, W., Brücker, R., Mülhauser, P., Steiger, J., Oetliker, H., Dalitz, H., Zürich, V., Mädler, H.-J., Beyer, A., Krämer, K., Lehnert, V., Walz, O. P., Pallauf, J., Rudas, P., Muray, T., Schöffl, Harald, editor, Spielmann, H., editor, Tritthart, Helmut A., editor, Koidl, B., editor, Gruber, F.-P., editor, and Reinhardt, A., editor

Published
1993
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9. Abstracts of presentations on plant protection issues at the xth international congress of virology: August 11–16, 1996 Binyanei haOoma, Jerusalem Iarael part 3(final part)

Author

Liu, Sijun, Bedford, Ian D., Markham, Peter G., Ghanim, Morad, Zeidan, Muhamad, Czosnek, Henryk, Bruyère, A., Herrbach, E., Brault, V., Ziegler-Graff, V., Guilley, H., van den Heuvel, J. F. J. M., Taiwo, M. A., Dijkstra, J., Martinez, B., López-Moya, J. J., Llave, C., Díaz-Ruíz, J. R., López-Abella, D., Mikoshiba, Y., Honda, K., Kanematsu, S., Fujisawa, I., Salomon, Raffi, Bernardi, Francoise, Raccah, B., Singer, S., Gal-On, A., Huet, H., López-Moya, J. J., Pirone, T. P., Visser, Peter B., Bol, John F., Hernández, Carmen, Brown, Derek J. F., Pappu, H. R., Culbreath, A. K., Todd, J. W., McPherson, R. M., Sherwood, J. L., Bertrand, P. F., Robbins, M. A., Reade, R. D., Rochon, D. M., Schönfelder, M., Körbler, M., Barg, E., Lesemann, D. -E., Vetten, H. J., Manqussopoulos, I. N., Tsagris, M., Maiss, E., Marczewski, W., Syller, J., Romero, Javier, Molina-Garcia, Antonio, Babin, Mar, Bujarski, Jozef J., Pogany, Judy, Zhang, L., Palukaitis, P., Kaplan, I. B., Qu, Feng, Morris, T. Jack, Steinkellner, H., Puehringer, H., Machado, A. M. Laimer da Câmara, Hammond, J., Brandt, S., Katinger, H., Himmler, G., Carrier, K., Hans, F., Wang, A., Sanfacon, H., Palkovics, László, Balázs, Ervin, Petrzik, K., Mráz, I., Fránová-Honetšlegrová, J., Kusiak, C., Berthome, R., Dinant, S., Astier, S., Albouy, J., Renou, J. P., Bó, E. Dal, Torre, M. E. Sánchez de la, Djelouah, K., García, M. L., Grau, O., Benvenisti, Luna, Gelman, Boris, Hai, Dalia, Yadin, Hagai, Stram, Yehuda, Becker, Yechiel, Čeřovská, N., Filigarová, M., Dědič, P., Nemchinov, L., Hadidi, A., Choi, Y. G., Randles, J. W., Samson, A. C. R., Wilford, J. N., Chapman, S., Santa Cruz, S., Wilson, T. M. A., Wilkinson, Nicola, Wilson, Louise, Marlow, Susan, King, Linda, Possee, Robert, Zhu, Fanxiu, Qi, Yipeng, Huang, Yongxiu, Hu, Jianhong, Oker-Blom, Christian, Keinänen, Kari, Chauhan, B. K., Possee, R. D., French, T. J., Finkelstein, Y., Levi, B. Z., Faktor, O., Toister-Achituv, Mira, Wang, Fushan, Qi, Yipeng, Huang, Yongxiu, Lu, Liquan, Du, Quansheng, Watson, S. K., Kalmakoff, J., Broer, R., Liu, Y., Zuidema, D., Strien, E. A. van, Vlak, J. M., Heldens, J. G. M., Chejanovsky, N., Gershburg, E., Toister-Achituv, Mira, Faruchi, S., Kamensky, B., Faktor, O., Faktor, O., Nahum, O., Stockholm, D., Rivkin, H., Gurevitz, M., Chejanovsky, N., Zilberberg, N., Gershburg, E., Stockholm, D., Rivkin, H., Chejanovsky, N., Gurevitz, M., Zilberberg, N., Gershburg, E., Smith, P., King, L. A., Bamett, A., Windass, J. D., Possee, R. D., Jacobs, C., Fielding, B., Davison, S., Kunjeku, E., Guarino, L. A., Jarvis, D. L., Reilly, L., Hoover, K., Schultz, C. M., Hammock, B. D., Gordon, K. H. J., Bawden, A. L., Brooks, E. M., Lincoln, M. R., Hanzlik, T. N., Larkin, P. J., Gordon, K. H. J., Bawden, A. L., van Hulten, M. C. W., Hanzlik, T. N., Hendry, D. A., Stephens, Rachel, Barnett, Anna, Thomas, Carole, Possee, Robert, King, Linda, Phanis, Constantinos, O’Reilly, David R., Clarke, E., Tristem, Michael, Cory, Jennifer, O’Reilly, David R., Mayo, M. A., Duncan, G. H., Reavy, B., Gildow, F. E., Lamb, J. W., Hay, R. T., Li, Shoudong, Qi, Bing, Wang, Jiawang, Qi, Yipeng, O’Reilly, David R., Kang, WonKyung, Crook, Norman E., Winstanley, Doreen, Alaoui-Ismaili, M. H., Richardson, C. D., Lundsgaard, T., Kobayashi, J., Kayama, T., Ikeda, N., Miyajima, S., Inouye, K., Kimura, T., Suzuki, N., Sugawara, M., Nuss, D. L., Matsuura, Y., Simón, Laureano, Guo, Huishan, García, Juan Antonio, Wang, S., Miller, W. A., Browning, K., Fütterer, Johannes, Potrykus, Ingo, Bao, Yiming, Li, Liu, Burns, Thomas M., Hull, Roger, Hohn, Thomas, Hefferon, K. L., AbouHaider, M. G., Hulanicka, D., Juszczuk, M., Iskakov, B. K., Shmanov, M. A., Polimbetova, N. S., Zhanybekova, S. Sh., Lee, A. V., Galiakparov, N. N., Dale, J. L., Beetham, P. R., Hafner, G. J., Harding, R. M., and Dale, J. L.

Published
1998
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11. Correction

Author

Liu, Sijun, Bedford, Ian, Markham, Peter, Ghanim, Morad, Zeidan, Muhamad, Czosnek, Henryk, Bruyère, A., Herrbach, E., Brault, V., Ziegler-Graff, V., Guilley, H., van den Heuvel, J., Taiwo, M., Dijkstra, J., Martinez, B., López-Moya, J., Llave, C., Díaz-Ruíz, J., López-Abella, D., Mikoshiba, Y., Honda, K., Kanematsu, S., Fujisawa, I., Salomon, Raffi, Bernardi, Francoise, Raccah, B., Singer, S., Gal-On, A., Huet, H., Pirone, T., Visser, Peter, Bol, John, Hernández, Carmen, Brown, Derek, Pappu, H., Culbreath, A., Todd, J., McPherson, R., Sherwood, J., Bertrand, P., Robbins, M., Reade, R., Rochon, D., Schönfelder, M., Körbler, M., Barg, E., Lesemann, D., Vetten, H., Manqussopoulos, I., Tsagris, M., Maiss, E., Marczewski, W., Syller, J., Romero, Javier, Molina-Garcia, Antonio, Babin, Mar, Bujarski, Jozef, Pogany, Judy, Zhang, L., Palukaitis, P., Kaplan, I., Qu, Feng, Morris, T., Steinkellner, H., Puehringer, H., Machado, A., Hammond, J., Brandt, S., Katinger, H., Himmler, G., Carrier, K., Hans, F., Wang, A., Sanfacon, H., Palkovics, László, Balázs, Ervin, Petrzik, K., Mráz, I., Fránová-Honetšlegrová, J., Kusiak, C., Berthome, R., Dinant, S., Astier, S., Albouy, J., Renou, J., Bó, E., Torre, M., Djelouah, K., García, M., Grau, O., Benvenisti, Luna, Gelman, Boris, Hai, Dalia, Yadin, Hagai, Stram, Yehuda, Becker, Yechiel, Čeřovská, N., Filigarová, M., Dědič, P., Nemchinov, L., Hadidi, A., Choi, Y., Randles, J., Samson, A., Wilford, J., Chapman, S., Santa Cruz, S., Wilson, T., Wilkinson, Nicola, Wilson, Louise, Marlow, Susan, King, Linda, Possee, Robert, Zhu, Fanxiu, Qi, Yipeng, Huang, Yongxiu, Hu, Jianhong, Oker-Blom, Christian, Keinänen, Kari, Chauhan, B., Possee, R., French, T., Finkelstein, Y., Levi, B., Faktor, O., Toister-Achituv, Mira, Wang, Fushan, Lu, Liquan, Du, Quansheng, Watson, S., Kalmakoff, J., Broer, R., Liu, Y., Zuidema, D., Strien, E., Vlak, J., Heldens, J., Chejanovsky, N., Gershburg, E., Faruchi, S., Kamensky, B., Nahum, O., Stockholm, D., Rivkin, H., Gurevitz, M., Zilberberg, N., Smith, P., King, L., Bamett, A., Windass, J., Jacobs, C., Fielding, B., Davison, S., Kunjeku, E., Guarino, L., Jarvis, D., Reilly, L., Hoover, K., Schultz, C., Hammock, B., Gordon, K., Bawden, A., Brooks, E., Lincoln, M., Hanzlik, T., Larkin, P., van Hulten, M., Hendry, D., Stephens, Rachel, Barnett, Anna, Thomas, Carole, Phanis, Constantinos, O'Reilly, David, Clarke, E., Tristem, Michael, Cory, Jennifer, Mayo, M., Duncan, G., Reavy, B., Gildow, F., Lamb, J., Hay, R., Li, Shoudong, Qi, Bing, Wang, Jiawang, Kang, WonKyung, Crook, Norman, Winstanley, Doreen, Alaoui-Ismaili, M., Richardson, C., Lundsgaard, T., Kobayashi, J., Kayama, T., Ikeda, N., Miyajima, S., Inouye, K., Kimura, T., Suzuki, N., Sugawara, M., Nuss, D., Matsuura, Y., Simón, Laureano, Guo, Huishan, García, Juan, Wang, S., Miller, W., Browning, K., Fütterer, Johannes, Potrykus, Ingo, Bao, Yiming, Li, Liu, Burns, Thomas, Hull, Roger, Hohn, Thomas, Hefferon, K., AbouHaider, M., Hulanicka, D., Juszczuk, M., Iskakov, B., Shmanov, M., Polimbetova, N., Zhanybekova, S., Lee, A., Galiakparov, N., Dale, J., Beetham, P., Hafner, G., and Harding, R.

Published
2018

16. Correction

Author

Liu, Sijun, Bedford, Ian D., Markham, Peter G., Ghanim, Morad, Zeidan, Muhamad, Czosnek, Henryk, Bruyère, A., Herrbach, E., Brault, V., Ziegler-Graff, V., Guilley, H., van den Heuvel, J. F. J. M., Taiwo, M. A., Dijkstra, J., Martinez, B., López-Moya, J. J., Llave, C., Díaz-Ruíz, J. R., López-Abella, D., Mikoshiba, Y., Honda, K., Kanematsu, S., Fujisawa, I., Salomon, Raffi, Bernardi, Francoise, Raccah, B., Singer, S., Gal-On, A., Huet, H., López-Moya, J. J., Pirone, T. P., Visser, Peter B., Bol, John F., Hernández, Carmen, Brown, Derek J. F., Pappu, H. R., Culbreath, A. K., Todd, J. W., McPherson, R. M., Sherwood, J. L., Bertrand, P. F., Robbins, M. A., Reade, R. D., Rochon, D. M., Schönfelder, M., Körbler, M., Barg, E., Lesemann, D. -E., Vetten, H. J., Manqussopoulos, I. N., Tsagris, M., Maiss, E., Marczewski, W., Syller, J., Romero, Javier, Molina-Garcia, Antonio, Babin, Mar, Bujarski, Jozef J., Pogany, Judy, Zhang, L., Palukaitis, P., Kaplan, I. B., Qu, Feng, Morris, T. Jack, Steinkellner, H., Puehringer, H., Machado, A. M. Laimer da Câmara, Hammond, J., Brandt, S., Katinger, H., Himmler, G., Carrier, K., Hans, F., Wang, A., Sanfacon, H., Palkovics, László, Balázs, Ervin, Petrzik, K., Mráz, I., Fránová-Honetšlegrová, J., Kusiak, C., Berthome, R., Dinant, S., Astier, S., Albouy, J., Renou, J. P., Bó, E. Dal, Torre, M. E. Sánchez de la, Djelouah, K., García, M. L., Grau, O., Benvenisti, Luna, Gelman, Boris, Hai, Dalia, Yadin, Hagai, Stram, Yehuda, Becker, Yechiel, Čeřovská, N., Filigarová, M., Dědič, P., Nemchinov, L., Hadidi, A., Choi, Y. G., Randles, J. W., Samson, A. C. R., Wilford, J. N., Chapman, S., Santa Cruz, S., Wilson, T. M. A., Wilkinson, Nicola, Wilson, Louise, Marlow, Susan, King, Linda, Possee, Robert, Zhu, Fanxiu, Qi, Yipeng, Huang, Yongxiu, Hu, Jianhong, Oker-Blom, Christian, Keinänen, Kari, Chauhan, B. K., Possee, R. D., French, T. J., Finkelstein, Y., Levi, B. Z., Faktor, O., Toister-Achituv, Mira, Wang, Fushan, Qi, Yipeng, Huang, Yongxiu, Lu, Liquan, Du, Quansheng, Watson, S. K., Kalmakoff, J., Broer, R., Liu, Y., Zuidema, D., Strien, E. A. van, Vlak, J. M., Heldens, J. G. M., Chejanovsky, N., Gershburg, E., Toister-Achituv, Mira, Faruchi, S., Kamensky, B., Faktor, O., Faktor, O., Nahum, O., Stockholm, D., Rivkin, H., Gurevitz, M., Chejanovsky, N., Zilberberg, N., Gershburg, E., Stockholm, D., Rivkin, H., Chejanovsky, N., Gurevitz, M., Zilberberg, N., Gershburg, E., Smith, P., King, L. A., Bamett, A., Windass, J. D., Possee, R. D., Jacobs, C., Fielding, B., Davison, S., Kunjeku, E., Guarino, L. A., Jarvis, D. L., Reilly, L., Hoover, K., Schultz, C. M., Hammock, B. D., Gordon, K. H. J., Bawden, A. L., Brooks, E. M., Lincoln, M. R., Hanzlik, T. N., Larkin, P. J., Gordon, K. H. J., Bawden, A. L., van Hulten, M. C. W., Hanzlik, T. N., Hendry, D. A., Stephens, Rachel, Barnett, Anna, Thomas, Carole, Possee, Robert, King, Linda, Phanis, Constantinos, O’Reilly, David R., Clarke, E., Tristem, Michael, Cory, Jennifer, O’Reilly, David R., Mayo, M. A., Duncan, G. H., Reavy, B., Gildow, F. E., Lamb, J. W., Hay, R. T., Li, Shoudong, Qi, Bing, Wang, Jiawang, Qi, Yipeng, O’Reilly, David R., Kang, WonKyung, Crook, Norman E., Winstanley, Doreen, Alaoui-Ismaili, M. H., Richardson, C. D., Lundsgaard, T., Kobayashi, J., Kayama, T., Ikeda, N., Miyajima, S., Inouye, K., Kimura, T., Suzuki, N., Sugawara, M., Nuss, D. L., Matsuura, Y., Simón, Laureano, Guo, Huishan, García, Juan Antonio, Wang, S., Miller, W. A., Browning, K., Fütterer, Johannes, Potrykus, Ingo, Bao, Yiming, Li, Liu, Burns, Thomas M., Hull, Roger, Hohn, Thomas, Hefferon, K. L., AbouHaider, M. G., Hulanicka, D., Juszczuk, M., Iskakov, B. K., Shmanov, M. A., Polimbetova, N. S., Zhanybekova, S. Sh., Lee, A. V., Galiakparov, N. N., Dale, J. L., Beetham, P. R., Hafner, G. J., Harding, R. M., and Dale, J. L.

Published
1998
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20. Two-step cloning of antibody variable domains in a phage display vector

Author

Engelhardt, O., Reingard Grabherr, Himmler, G., and Ruker, F.

Subjects
Base Sequence, Genetic Vectors, Molecular Sequence Data, Immunoglobulin Variable Region, Bacteriophages, Amino Acid Sequence, Cloning, Molecular, Polymerase Chain Reaction, HIV Envelope Protein gp41
Published
1994

33. SialylTn-mAb17-1A Carbohydrate−Protein Conjugate Vaccine:  Effect of Coupling Density and Presentation of SialylTn

Author

Kircheis, R., Vondru, P., Nechansky, A., Ohler, R., Loibner, H., Himmler, G., and Mudde, G. C.

Abstract

Carbohydrate antigens resulting from aberrant glycosylation of tumor cells, such as SialylTn, represent attractive targets for cancer vaccination. However, T-cell-independent carbohydrate antigens are poorly immunogenic and fail to induce memory and IgG class switch. Clustered expression patterns of some carbohydrates on the cell surface add further complexity to the design of carbohydrate-based vaccines. We describe here a vaccine consisting of SialylTn carbohydrate epitopes coupled to a highly immunogenic carrier molecule, mAb17-1A, adsorbed on alhydrogel and coformulated with a strong adjuvant, QS-21. The SialylTn−mAb17-1A conjugate vaccine was administered in Rhesus monkeys, and the immune responses against mAb17-1A, SialylTn, ovine submaxillary mucin, and tumor cells were analyzed. The data demonstrate that the density of carbohydrate epitopes on the carrier is an essential parameter for induction of anti-carbohydrate specific memory IgG immune responses. Furthermore, the influence of different types of presentation of SialylTn (monomeric vs trimers vs clustered via a branched polyethylenimine linker) on antibody titers and specificity was studied. High-density coupling of SialylTn epitopes to mAb17-1A induced the strongest immune response against synthetic SialylTn and showed also the highest reactivity against natural targets, such as OSM and tumor cells.

Published
2005

35. Screening for monoclonal antibodies with covalently linked antigen

Author

Wagner, K., Steindl, F., Wenisch, E., Himmler, G., Rüker, F., Alois Jungbauer, and Katinger, H.

Subjects
Carbodiimides, Mice, Solubility, Glutaral, Animals, Antibodies, Monoclonal, Enzyme-Linked Immunosorbent Assay, Antigens, Urokinase-Type Plasminogen Activator
Abstract

Microtitre plates prepared for ELISA are treated for the maximum adsorption of gamma-globulins (at pH 9). The adsorption of other soluble proteins (e.g. antigens) is sometimes less effective and therefore requires a higher amount of protein for the primary coat of wells. In order to reduce the amount of pure antigen required for the screening of mAb-producing hybridomas, we improved the sensitivity of our screening ELISA technique by coupling the antigen covalently to the surface of the microtiter wells. The antigen (urokinase) was coupled by the glutaraldehyde or carbodiimide procedures respectively using "aminoplates" (Nissho Iwai, Japan). The glutaraldehyde method led to at least a five fold increase of the sensitivity compared to coventional adsorption. Reduced requirement of antigen for the assay is thus achieved by a simple procedure.

36. Cross flow diafiltration of serum with basal medium suitable for growth of hybridomas, sterilization and protein reduction

Author

Alois Jungbauer, Wenisch, E., Steindl, F., Himmler, G., Reiter, S., Rüker, F., Wagner, K., and Katinger, H.

Subjects
Mice, Hybridomas, Animals, Antibodies, Monoclonal, Dialysis, Filtration, Biotechnology, Culture Media
Abstract

Fetal Calf Serum (FCS) was extensively extracted by cross flow diafiltration (Pellicon, Millipore) and sterilized using the basal growth medium (DMEM) for the extraction. Ultrafiltration membranes of 10(5) and 3 X 10(5) Dalton cut off were used respectively. The diafiltrates were used for hybridoma cultivation and the results of growth and mAb-production were compared with standard medium (DMEM + 5% FCS). Slightly reduced mAb-titers were achieved. These were, however, compensated by decreased concentration of contaminating protein and higher specific mAb/protein ratio as examined by SDS-PAGE and enzyme linked immuno electro transfer blot (EITB).

37. A laboratory fermentor for agarose immobilized hybridomas to produce monoclonal antibodies

Author

Himmler G, Palfi G, Rüker F, Katinger H, and Scheirer W

Subjects
Mice, Hybridomas, Sepharose, Cytological Techniques, Fermentation, Animals, Antibodies, Monoclonal, Humans, Cell Division, Microspheres
Abstract

Mass culture of immobilized cells in airlift-fermenters usually ends up with the beads accumulating in the foamy layer on the surface of the reactor fluid or, in stirred tankreactors, with partial destruction of the beads. We tried to use an airlift fermenter vessel for growing cells, immobilized in agarose beads. Instead of using the gas for driving, we mounted a slowly turning marine type impeller within the drought tube. Oxygen was supplied on occasional demands by the original sparger. This set up leads to sufficient operational characteristics of the reactor without accumulation of the beads in the foamy layer and without mechanical destruction. Different productivities of either immobilized cells or cells in free suspension culture are reported.

46. Immunization of Rhesus monkeys with a conjugate vaccine IGN402 induces immune responses against carbohydrate and protein antigens, and cancer cells.

Author

Waxenecker, G., Kircheis, R., Vondru, P., Zinöcker, I., Häring, D., Krey, D., Nechansky, A., Mudde, G. C., Himmler, G., and Loibner, H.

Subjects
VACCINATION, IMMUNE response, CANCER treatment, IMMUNOGLOBULINS, CANCER cells, IMMUNOLOGICAL adjuvants
Abstract

The article shows that the immunization of Rhesus monkeys with a conjugate vaccine IGN402 induces immune responses against carbohydrate and protein antigens, and cancer cells. It reveals that immunization in the presence of additional adjuvants, such as QS-21, strongly enhanced the immune response against the carbohydrate antigen, and has resulted in the production of carbohydrate-specific IgG antibodies.

Published
2004
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47. Inhibition of signaling via erbB-receptors by antibodies that target the Lewis Y-antigen.

Author

Waxenecker, G., Klinger, M., Farhan, H., Freissmuth, M., Himmler, G., Janzek, E., Mudde, G. C., and Loibner, H.

Subjects
CANCER cells, MONOCLONAL antibodies, IMMUNOGLOBULINS, TUMORS, CYTOKINES
Abstract

The article determines whether the anti-LeY antibodies IGN311 and its murine parent version ABL 364 influence the signaling in tumor cells via inhibition of growth factor receptor functions. IGN311 is a humanized monoclonal IgG1 antibody that binds to the Lewis Y (LeY) carbohydrate overexpressed on epithelial cancers. The article shows that antibodies against carbohydrate determinants of erbB-familiy members are capable of blocking signaling.

Published
2004
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48. Increased effector functions of a monoclonal antibody by glycoform engineering.

Author

Waxenecker, G., Schuster, M., Umana, P., Brünker, P., Froihofer, I., Wiederkum, S., Schwager, C., Klug, H., Mudde, G. C., Himmler, G., and Loibner, H.

Subjects
MONOCLONAL antibodies, IMMUNOGLOBULINS, CELL lines, ENZYMES, GLYCOSYLATION, CELL culture
Abstract

The article enhances the effector function of the humanized monoclonal antibody specific for Lewis Y (IGN311) by genetically modifying the antibody producing cell line to express the glycosyl transferase GnTIII. It shows that the presence of this enzyme leads to glycosylation of the antibody with a bi-secting N-acetyl-glucosamine group and the absence of core fucosylation.

Published
2004
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49. Neutralising Effects of Different Antibodies on Clostridioides difficile Toxins TcdA and TcdB in a Translational Approach.

Author

Csukovich G, Kramer N, Pratscher B, Gotic I, Freund P, Hahn R, Himmler G, Brandt S, and Burgener IA

Subjects
Humans, Animals, Dogs, Enterotoxins toxicity, Bacterial Proteins toxicity, Antibodies, Bacterial, Bacterial Toxins toxicity, Clostridioides difficile
Abstract

Given the high prevalence of intestinal disease in humans and animals, there is a strong need for clinically relevant models recapitulating gastrointestinal systems, ideally replacing in vivo models in accordance with the principles of the 3R. We established a canine organoid system and analysed the neutralising effects of recombinant versus natural antibodies on Clostridioides difficile toxins A and B in this in vitro system. Sulforhodamine B cytotoxicity assays in 2D and FITC-dextran barrier integrity assays on basal-out and apical-out organoids revealed that recombinant, but not natural antibodies, effectively neutralised C. difficile toxins. Our findings emphasise that canine intestinal organoids can be used to test different components and suggest that they can be further refined to also mirror complex interactions between the intestinal epithelium and other cells.

Published
2023
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50. Efficient production of recombinant secretory IgA against Clostridium difficile toxins in CHO-K1 cells.

Author

Bhaskara V, Leal MT, Seigner J, Friedrich T, Kreidl E, Gadermaier E, Tesarz M, Rogalli A, Stangl L, Wallwitz J, Hammel K, Rothbauer M, Moll H, Ertl P, Hahn R, Himmler G, Bauer A, and Casanova E

Subjects
Animals, Bacterial Proteins, Cricetinae, Enterotoxins genetics, Immunoglobulin A, Secretory, Bacterial Toxins genetics, Clostridioides difficile genetics
Abstract

Despite the essential role secretory IgAs play in the defense against pathogenic invasion and the proposed value of recombinant secretory IgAs as novel therapeutics, currently there are no IgA-based therapies in clinics. Secretory IgAs are complex molecules and the major bottleneck limiting their therapeutic potential is a reliable recombinant production system. In this report, we addressed this issue and established a fast and robust production method for secretory IgAs in CHO-K1 cells using BAC-based expression vectors. As a proof of principle, we produced IgAs against Clostridium difficile toxins TcdA and TcdB. Recombinant secretory IgAs produced using our expression system showed comparable titers to IgGs, widely used as therapeutic biologicals. Importantly, secretory IgAs produced using our method were functional and could efficiently neutralize Clostridium difficile toxins TcdA and TcdB. These results show that recombinant secretory IgAs can be efficiently produced, thus opening the possibility to use them as therapeutic agents in clinics., (Copyright © 2021 The Author(s). Published by Elsevier B.V. All rights reserved.)

Published
2021
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