ArticleProceedings of the National Academy of Sciences of the United States of America1995
Identification of receptor-binding domains on human interleukin 5 and design of an interleukin 5-derived receptor antagonist.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 103 citations in OpenAlex.
- Orai inhibition modulates pulmonary ILC2 metabolism and alleviates airway hyperreactivity in murine and humanized models.Nature communications · 2023Article
- CD52-targeted depletion by Alemtuzumab ameliorates allergic airway hyperreactivity and lung inflammation.Mucosal immunology · 2021Article
- CD200-CD200R immune checkpoint engagement regulates ILC2 effector function and ameliorates lung inflammation in asthma.Nature communications · 2021Article
- Article
- Glioblastoma exosomes and IGF-1R/AS-ODN are immunogenic stimuli in a translational research immunotherapy paradigm.Cancer immunology, immunotherapy : CII · 2015Article
- Structural basis of interleukin-5 dimer recognition by its α receptor.Protein science : a publication of the Protein Society · 2012Article
- Interleukin-5 and IL-5 receptor in health and diseases.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2011Review
- Two modes of beta-receptor recognition are mediated by distinct epitopes on mouse and human interleukin-3.The Journal of biological chemistry · 2010Article
- Review
- Interleukin-5 receptor subunit oligomerization and rearrangement revealed by fluorescence resonance energy transfer imaging.The Journal of biological chemistry · 2008Article
- Slow-dissociation effect of common signaling subunit beta c on IL5 and GM-CSF receptor assembly.Cytokine · 2008Article
- Asymmetric usage of antagonist charged residues drives interleukin-5 receptor recruitment but is insufficient for receptor activation.Biochemistry · 2006Article
- Structural and functional hot spots in cytokine receptors.International journal of hematology · 2001Review
- A potent dimeric peptide antagonist of interleukin-5 that binds two interleukin-5 receptor alpha chains.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- IL-3 signaling and the role of Src kinases, JAKs and STATs: a covert liaison unveiled.Oncogene · 2000Review
- Expression and in vitro properties of guinea pig IL-5: comparison to human and murine orthologs.Mediators of inflammation · 2000Article
- Interleukin-5, a therapeutic target in allergic inflammation.Transactions of the American Clinical and Climatological Association · 2000Review
- Cytokines in asthma.Thorax · 1999Review
- An interleukin 5 mutant distinguishes between two functional responses in human eosinophils.The Journal of experimental medicine · 1997Article
- Engineering of a functional interleukin-5 monomer: a paradigm for redesigning helical bundle cytokines with therapeutic potential in allergy and asthma.Journal of molecular medicine (Berlin, Germany) · 1996Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A detailed structure-function analysis of human interleukin 5 (hIL5) has been performed. The hIL5 receptor is composed of two different polypeptide chains, the alpha and beta subunits. The alpha subunit alone is sufficient for ligand binding, but association with the beta subunit leads to a 2- to 3-fold increase in binding affinity. The beta chain is shared with the receptors for IL3 and granulocyte/macrophage-colony-stimulating factor--hence the descriptor beta C (C for common). All hIL5 mutants were analyzed in a solid-phase binding assay for hIL5R alpha interaction and in a proliferation assay using IL5-dependent cell lines for receptor-complex activation. Most residues affecting binding to the receptor alpha subunit were clustered in a loop connecting beta-strand 1 and helix B (mutants H38A, K39A, and H41A), in beta-strand 2 (E89A and R91A; weaker effect for E90A) and close to the C terminus (T109A, E110A, W111S, and I112A). Mutations at one position, E13 (Glu13), caused a reduced activation of the hIL5 receptor complex. In the case of E13Q, only 0.05% bioactivity was detected on a hIL5-responsive subclone of the mouse promyelocytic cell line FDC-P1. Moreover, on hIL5-responsive TF1 cells, the same mutant was completely inactive and proved to have antagonistic properties. Interactions of this mutant with both receptor subunits were nevertheless indistinguishable from those of nonmutated hIL5 by crosslinking and Scatchard plot analysis of transfected COS-1 cells.
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