Structural highlights
Publication Abstract from PubMed
IgE mediates hypersensitivity reactions responsible for most allergic diseases, which affect 20-40% of the population in developed countries. A 52-residue domain of membrane-bound IgE (mIgE) called CepsilonmX is currently a target for developing therapeutic antibodies; however, its structure is unknown. Here we show that two antibodies with therapeutic potential in IgE-mediated allergic diseases, which can cause cytolytic effects on mIgE-expressing B lymphocytes and downregulate IgE production, target different conformations of an intrinsically disordered region (IDR) in the extracellular CepsilonmX domain. We provide an important example of antibodies targeting an extracellular IDR of a receptor on the surface of intended target cells. We also provide fundamental structural characteristics unique to human mIgE, which may stimulate further studies to investigate whether other monoclonal antibodies (mAbs) targeting intrinsically disordered peptide segments or vaccine-like products targeting IDRs of a membrane protein can be developed.
Two potential therapeutic antibodies bind to a peptide segment of membrane-bound IgE in different conformations.,Chu HM, Wright J, Chan YH, Lin CJ, Chang TW, Lim C Nat Commun. 2014;5:3139. doi: 10.1038/ncomms4139. PMID:24457896[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Chu HM, Wright J, Chan YH, Lin CJ, Chang TW, Lim C. Two potential therapeutic antibodies bind to a peptide segment of membrane-bound IgE in different conformations. Nat Commun. 2014;5:3139. doi: 10.1038/ncomms4139. PMID:24457896 doi:http://dx.doi.org/10.1038/ncomms4139
