6 results on '"Crescioli, S."'
Search Results
2. An immunologically relevant rodent model demonstrates safety of therapy using a tumour‐specific IgE
- Author
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Josephs, D. H., Nakamura, M., Bax, H. J., Dodev, T. S., Muirhead, G., Saul, L., Karagiannis, P., Ilieva, K. M., Crescioli, S., Gazinska, P., Woodman, N., Lombardelli, C., Kareemaghay, S., Selkirk, C., Lentfer, H., Barton, C., Canevari, S., Figini, M., Downes, N., Dombrowicz, D., Corrigan, C. J., Nestle, F. O., Jones, P. S., Gould, H. J., Blower, P. J., Tsoka, S., Spicer, J. F., and Karagiannis, S. N.
- Subjects
AllergoOncology ,Receptors, IgE ,Tumor Necrosis Factor-alpha ,Immunoglobulin E ,Statistics, Nonparametric ,Rats ,Antibodies, Monoclonal, Murine-Derived ,Mice ,Treatment Outcome ,Experimental Allergy and Immunology ,Cell Line, Tumor ,Immunoglobulin G ,Neoplasms ,Models, Animal ,cancer ,Animals ,Humans ,Original Article ,rat ,Folate Receptor 1 ,IgE ,Immunotherapy ,ORIGINAL ARTICLES ,Protein Binding - Abstract
Background Designing biologically informative models for assessing the safety of novel agents, especially for cancer immunotherapy, carries substantial challenges. The choice of an in vivo system for studies on IgE antibodies represents a major impediment to their clinical translation, especially with respect to class‐specific immunological functions and safety. Fcε receptor expression and structure are different in humans and mice, so that the murine system is not informative when studying human IgE biology. By contrast, FcεRI expression and cellular distribution in rats mirror that of humans. Methods We are developing MOv18 IgE, a human chimeric antibody recognizing the tumour‐associated antigen folate receptor alpha. We created an immunologically congruent surrogate rat model likely to recapitulate human IgE‐FcεR interactions and engineered a surrogate rat IgE equivalent to MOv18. Employing this model, we examined in vivo safety and efficacy of antitumour IgE antibodies. Results In immunocompetent rats, rodent IgE restricted growth of syngeneic tumours in the absence of clinical, histopathological or metabolic signs associated with obvious toxicity. No physiological or immunological evidence of a “cytokine storm” or allergic response was seen, even at 50 mg/kg weekly doses. IgE treatment was associated with elevated serum concentrations of TNFα, a mediator previously linked with IgE‐mediated antitumour and antiparasitic functions, alongside evidence of substantially elevated tumoural immune cell infiltration and immunological pathway activation in tumour‐bearing lungs. Conclusion Our findings indicate safety of MOv18 IgE, in conjunction with efficacy and immune activation, supporting the translation of this therapeutic approach to the clinical arena.
- Published
- 2018
3. AllergoOncology: Opposite outcomes of immune tolerance in allergy and cancer
- Author
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Jensen-Jarolim, E., primary, Bax, H. J., additional, Bianchini, R., additional, Crescioli, S., additional, Daniels-Wells, T. R., additional, Dombrowicz, D., additional, Fiebiger, E., additional, Gould, H. J., additional, Irshad, S., additional, Janda, J., additional, Josephs, D. H., additional, Levi-Schaffer, F., additional, O′Mahony, L., additional, Pellizzari, G., additional, Penichet, M. L., additional, Redegeld, F., additional, Roth-Walter, F., additional, Singer, J., additional, Untersmayr, E., additional, Vangelista, L., additional, and Karagiannis, S. N., additional
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- 2017
- Full Text
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4. IgE glycosylation and impact on structure and function: A systematic review.
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McCraw AJ, Palhares LCGF, Hendel JL, Gardner RA, Santaolalla A, Crescioli S, McDonnell J, Van Hemelrijck M, Chenoweth A, Spencer DIR, Wagner GK, and Karagiannis SN
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- Animals, Humans, Glycosylation, Hypersensitivity immunology, Hypersensitivity metabolism, Polysaccharides metabolism, Polysaccharides chemistry, Structure-Activity Relationship, Immunoglobulin E immunology, Immunoglobulin E metabolism
- Abstract
The impact of human IgE glycosylation on structure, function and disease mechanisms is not fully elucidated, and heterogeneity in different studies renders drawing conclusions challenging. Previous reviews discussed IgE glycosylation focusing on specific topics such as health versus disease, FcεR binding or impact on function. We present the first systematic review of human IgE glycosylation conducted utilizing the PRISMA guidelines. We sought to define the current consensus concerning the roles of glycosylation on structure, biology and disease. Despite diverse analytical methodologies, source, expression systems and the sparsity of data on IgE antibodies from non-allergic individuals, collectively evidence suggests differential glycosylation profiles, particularly in allergic diseases compared with healthy states, and indicates functional impact, and contributions to IgE-mediated hypersensitivities and atopic diseases. Beyond allergic diseases, dysregulated terminal glycan structures, including sialic acid, may regulate IgE metabolism. Glycan sites such as N394 may contribute to stabilizing IgE structure, with alterations in these glycans likely influencing both structure and IgE-FcεR interactions. This systematic review therefore highlights critical IgE glycosylation attributes in health and disease that may be exploitable for therapeutic intervention, and the need for novel analytics to explore pertinent research avenues., (© 2024 The Author(s). Allergy published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd.)
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- 2024
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5. AllergoOncology: Danger signals in allergology and oncology: A European Academy of Allergy and Clinical Immunology (EAACI) Position Paper.
- Author
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Bergmann C, Poli A, Agache I, Bianchini R, Bax HJ, Castells M, Crescioli S, Dombrowicz D, Ferastraoaru D, Fiebiger E, Gould HJ, Hartmann K, Izquierdo E, Jordakieva G, Josephs DH, Jutel M, Levi-Schaffer F, de Las Vecillas L, Lotze MT, Osborn G, Pascal M, Redegeld F, Rosenstreich D, Roth-Walter F, Schmidt-Weber C, Shamji M, Steveling EH, Turner MC, Untersmayr E, Jensen-Jarolim E, and Karagiannis SN
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- Humans, Immunity, Inflammation, Signal Transduction, Hypersensitivity diagnosis, Hypersensitivity etiology, Hypersensitivity therapy, Neoplasms etiology, Neoplasms therapy
- Abstract
The immune system interacts with many nominal 'danger' signals, endogenous danger-associated (DAMP), exogenous pathogen (PAMP) and allergen (AAMP)-associated molecular patterns. The immune context under which these are received can promote or prevent immune activating or inflammatory mechanisms and may orchestrate diverse immune responses in allergy and cancer. Each can act either by favouring a respective pathology or by supporting the immune response to confer protective effects, depending on acuity or chronicity. In this Position Paper under the collective term danger signals or DAMPs, PAMPs and AAMPs, we consider their diverse roles in allergy and cancer and the connection between these in AllergoOncology. We focus on their interactions with different immune cells of the innate and adaptive immune system and how these promote immune responses with juxtaposing clinical outcomes in allergy and cancer. While danger signals present potential targets to overcome inflammatory responses in allergy, these may be reconsidered in relation to a history of allergy, chronic inflammation and autoimmunity linked to the risk of developing cancer, and with regard to clinical responses to anti-cancer immune and targeted therapies. Cross-disciplinary insights in AllergoOncology derived from dissecting clinical phenotypes of common danger signal pathways may improve allergy and cancer clinical outcomes., (© 2022 The Authors. Allergy published by European Academy of Allergy and Clinical Immunology and John Wiley & Sons Ltd.)
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- 2022
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6. AllergoOncology: Expression platform development and functional profiling of an anti-HER2 IgE antibody.
- Author
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Ilieva KM, Fazekas-Singer J, Bax HJ, Crescioli S, Montero-Morales L, Mele S, Sow HS, Stavraka C, Josephs DH, Spicer JF, Steinkellner H, Jensen-Jarolim E, Tutt ANJ, and Karagiannis SN
- Subjects
- Gene Expression, Gene Expression Profiling, Humans, Transcriptome, Neoplasms immunology, Receptor, ErbB-2 genetics, Receptor, ErbB-2 immunology
- Published
- 2019
- Full Text
- View/download PDF
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