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Sialylation of immunoglobulin E is a determinant of allergic pathogenicity

Shade, Kai-Ting C., Conroy, Michelle E., Washburn, Nathaniel, Kitaoka, Maya, Huynh, Daniel J., Laprise, Emma, Patil, Sarita U., Shreffler, Wayne G., Anthony, Robert M.·2020·Nature
DOI 10.1038/s41586-020-2311-zPMC PMC7386252
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Citations

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Research works printed but not linked: 35

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  3. Bird, J. A., Crain, M. & Varshney, P. Food allergen panel testing often results in misdiagnosis of food allergy. J. Pediatr. 166, 97–100 (2015). · DOI · Paper page
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  6. Arnold, J. N., Wormald, M. R., Sim, R. B., Rudd, P. M. & Dwek, R. A. The impact of glycosylation on the biological function and structure of human immunoglobulins. Annu. Rev. Immunol. 25, 21–50 (2007). · DOI
  7. Bégin, P. et al. Phase 1 results of safety and tolerability in a rush oral immunotherapy protocol to multiple foods using omalizumab. Allergy Asthma Clin. Immunol. 10, 7 (2014). · DOI · Paper page
  8. Patil, S. U. et al. Peanut oral immunotherapy transiently expands circulating Ara h 2-specific B cells with a homologous repertoire in unrelated subjects. J. Allergy Clin. Immunol. 136, 125–134 (2015). · DOI
  9. Wang, T. T. et al. IgG antibodies to dengue enhanced for FcγRIIIA binding determine disease severity. Science 355, 395–398 (2017). · DOI
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  11. Wang, T. T. et al. Anti-HA glycoforms drive B cell affinity selection and determine influenza vaccine efficacy. Cell 162, 160–169 (2015). · DOI
  12. Parekh, R. B. et al. Association of rheumatoid arthritis and primary osteoarthritis with changes in the glycosylation pattern of total serum IgG. Nature 316, 452–457 (1985). · DOI · Paper page
  13. Espy, C. et al. Sialylation levels of anti-proteinase 3 antibodies are associated with the activity of granulomatosis with polyangiitis (Wegener’s). Arthritis Rheum. 63, 2105–2115 (2011). · DOI
  14. Wang, T. T. & Ravetch, J. V. Functional diversification of IgGs through Fc glycosylation. J. Clin. Invest. 129, 3492–3498 (2019). · DOI
  15. Arnold, J. N. et al. The glycosylation of human serum IgD and IgE and the accessibility of identified oligomannose structures for interaction with mannan-binding lectin. J. Immunol. 173, 6831–6840 (2004). · DOI
  16. Plomp, R. et al. Site-specific N-glycosylation analysis of human immunoglobulin E. J. Proteome Res. 13, 536–546 (2014). · DOI
  17. Shade, K. T. et al. A single glycan on IgE is indispensable for initiation of anaphylaxis. J. Exp. Med. 212, 457–467 (2015). · DOI
  18. Wu, G. et al. Glycoproteomic studies of IgE from a novel hyper IgE syndrome linked to PGM3 mutation. Glycoconj. J. 33, 447–456 (2016). · DOI
  19. Yamazaki, T. et al. Receptor-destroying enzyme (RDE) from Vibrio cholerae modulates IgE activity and reduces the initiation of anaphylaxis. J. Biol. Chem. 294, 6659–6669 (2019). · DOI
  20. Jabs, F. et al. Trapping IgE in a closed conformation by mimicking CD23 binding prevents and disrupts FcεRI interaction. Nat. Commun. 9, 7 (2018). · DOI
  21. Wuhrer, M. et al. Glycosylation profiling of immunoglobulin G (IgG) subclasses from human serum. Proteomics 7, 4070–4081 (2007). · DOI
  22. Nimmerjahn, F. & Ravetch, J. V. Anti-inflammatory actions of intravenous immunoglobulin. Annu. Rev. Immunol. 26, 513–533 (2008). · DOI
  23. Ding, J. X. et al. Aberrant sialylation of serum IgA1 was associated with prognosis of patients with IgA nephropathy. Clin. Immunol. 125, 268–274 (2007). · DOI
  24. Maurer, M. A. et al. Glycosylation of human IgA directly inhibits influenza A and other sialic-acid-binding viruses. Cell Rep. 23, 90–99 (2018). · DOI
  25. Colucci, M. et al. Sialylation of N-linked glycans influences the immunomodulatory effects of IgM on T cells. J. Immunol. 194, 151–157 (2015). · DOI
  26. Collins, B. E., Smith, B. A., Bengtson, P. & Paulson, J. C. Ablation of CD22 in ligand-deficient mice restores B cell receptor signaling. Nat. Immunol. 7, 199–206 (2006). · DOI
  27. Abe, K., Yamamoto, K. & Sinohara, H. Clearance of desialylated mouse alpha-macroglobulin and murinoglobulin in the mouse. J. Biochem. 108, 726–729 (1990). · DOI
  28. Fleischer, D. M. et al. Oral food challenges in children with a diagnosis of food allergy. J. Pediatr. 158, 578–583 (2011). · DOI
  29. Sampath, V. et al. Deciphering the black box of food allergy mechanisms. Ann. Allergy Asthma Immunol. 118, 21–27 (2017). · DOI
  30. Christensen, S. & Egebjerg, J. Cloning, expression and characterization of a sialidase gene from Arthrobacter ureafaciens. Biotechnol. Appl. Biochem. 41, 225–231 (2005). · DOI
  31. Dombrowicz, D. et al. Anaphylaxis mediated through a humanized high affinity IgE receptor. J. Immunol. 157, 1645–1651 (1996). · DOI
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  33. MacGlashan, D. Jr, Lavens-Phillips, S. & Katsushi, M. IgE-mediated desensitization in human basophils and mast cells. Front. Biosci. 3, d746–d756 (1998). · DOI
  34. Kirshenbaum, A. S. et al. Characterization of novel stem cell factor responsive human mast cell lines LAD 1 and 2 established from a patient with mast cell sarcoma/leukemia; activation following aggregation of FcεRI or FcγRI. Leuk. Res. 27, 677–682 (2003). · DOI
  35. Bandara, G., Metcalfe, D. D. & Kirshenbaum, A. S. Growth of human mast cells from bone marrow and peripheral blood-derived CD34+ pluripotent hematopoietic cells. Methods Mol. Biol. 1220, 155–162 (2015). · DOI

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Metadata

Authors
Shade, K.-T. C., Conroy, M. E., Washburn, N., Kitaoka, M., Huynh, D. J., Laprise, E., Patil, S. U., Shreffler, W. G., & Anthony, R. M.
ORCID
Venue
Nature
Publisher
Springer Science and Business Media LLC
Published
2020-05-20
Volume
582
Issue
7811
Pages
265-270
ISSN
  • 0028-0836
  • 1476-4687
DOI
10.1038/s41586-020-2311-z
PMC
PMC7386252
Cited by
160
References
1
Language
en
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