dc.contributor.author | Bucaite, G | |
dc.contributor.author | Kang-Pettinger, T | |
dc.contributor.author | Moreira, J | |
dc.contributor.author | Gould, HJ | |
dc.contributor.author | James, LK | |
dc.contributor.author | Sutton, BJ | |
dc.contributor.author | McDonnell, JM | |
dc.date.accessioned | 2020-06-30T12:28:19Z | |
dc.date.available | 2019-07-19 | |
dc.date.available | 2020-06-30T12:28:19Z | |
dc.date.issued | 2019-08-28 | |
dc.identifier.citation | Bucaite et al. 2019. Interplay between Affinity and Valency in Effector Cell Degranulation: A Model System with Polcalcin Allergens and Human Patient–Derived IgE Antibodies. Journal of Immunology August 28, ji1900509; DOI: 10.4049/jimmunol.1900509 | en_US |
dc.identifier.issn | 0022-1767 | |
dc.identifier.uri | https://qmro.qmul.ac.uk/xmlui/handle/123456789/65333 | |
dc.description | This is the accepted, uncopyedited version of the manuscript. The definitive version was published in The Journal of Immunology August 28, 2019, ji1900509; DOI: https://doi.org/10.4049/jimmunol.1900509 | en_US |
dc.description | Originally published in The Journal of Immunology. Bucaite G, Kang-Pettinger T, Moreira J, et al. Interplay between Affinity and Valency in Effector Cell Degranulation: A Model System with Polcalcin Allergens and Human Patient-Derived IgE Antibodies. J Immunol. 2019;203(7):1693-1700. doi:10.4049/jimmunol.1900509 The American Association of Immunologists, Inc. | |
dc.description.abstract | An allergic reaction is rapidly generated when allergens bind and cross-link IgE bound to its receptor FcεRI on effector cells, resulting in cell degranulation and release of proinflammatory mediators. The extent of effector cell activation is linked to allergen affinity, oligomeric state, valency, and spacing of IgE-binding epitopes on the allergen. Whereas most of these observations come from studies using synthetic allergens, in this study we have used Timothy grass pollen allergen Phl p 7 and birch pollen allergen Bet v 4 to study these effects. Despite the high homology of these polcalcin family allergens, Phl p 7 and Bet v 4 display different binding characteristics toward two human patient-derived polcalcin-specific IgE Abs. We have used native polcalcin dimers and engineered multimeric allergens to test the effects of affinity and oligomeric state on IgE binding and effector cell activation. Our results indicate that polcalcin multimers are required to stimulate high levels of effector cell degranulation when using the humanized RBL-SX38 cell model and that multivalency can overcome the need for high-affinity interactions. | en_US |
dc.description.sponsorship | This work was supported by Medical Research Council Grant G1100090. G.B. was supported by a studentship from the King’s Bioscience Institute and by the Guy’s and St. Thomas’ Charity Prize Ph.D. Program in Biomedical and Translational Science. We acknowledge the support of the Centre for Biomolecular Spectroscopy, King’s College London, established with a Capital Award from the Wellcome Trust (Grant 085944). | en_US |
dc.format.extent | 1693 - 1700 | |
dc.language | eng | |
dc.language.iso | en | en_US |
dc.publisher | American Association of Immunologists | en_US |
dc.relation.ispartof | J Immunol | |
dc.title | Interplay between Affinity and Valency in Effector Cell Degranulation: A Model System with Polcalcin Allergens and Human Patient-Derived IgE Antibodies. | en_US |
dc.type | Article | en_US |
dc.rights.holder | 2019 by The American Association of Immunologists, Inc | |
dc.identifier.doi | 10.4049/jimmunol.1900509 | |
pubs.author-url | https://www.ncbi.nlm.nih.gov/pubmed/31462504 | en_US |
pubs.issue | 7 | en_US |
pubs.notes | Not known | en_US |
pubs.publication-status | Published | en_US |
pubs.volume | 203 | en_US |
dcterms.dateAccepted | 2019-07-19 | |
rioxxterms.funder | Default funder | en_US |
rioxxterms.identifier.project | Default project | en_US |