Asset Details
Do you wish to reserve the book?
The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
Hey, we have placed the reservation for you!
By the way, why not check out events that you can attend while you pick your title.
Oops! Something went wrong.
Looks like we were not able to place the reservation. Kindly try again later.
Are you sure you want to remove the book from the shelf?
The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
Do you wish to request the book?
The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
Please be aware that the book you have requested cannot be checked out. If you would like to checkout this book, you can reserve another copy
We have requested the book for you!
Your request is successful and it will be processed during the Library working hours. Please check the status of your request in My Requests.
Oops! Something went wrong.
Looks like we were not able to place your request. Kindly try again later.
Journal Article
The mechanistic and functional profile of the therapeutic anti-IgE antibody ligelizumab differs from omalizumab
2020
Overview
Targeting of immunoglobulin E (IgE) represents an interesting approach for the treatment of allergic disorders. A high-affinity monoclonal anti-IgE antibody, ligelizumab, has recently been developed to overcome some of the limitations associated with the clinical use of the therapeutic anti-IgE antibody, omalizumab. Here, we determine the molecular binding profile and functional modes-of-action of ligelizumab. We solve the crystal structure of ligelizumab bound to IgE, and report epitope differences between ligelizumab and omalizumab that contribute to their qualitatively distinct IgE-receptor inhibition profiles. While ligelizumab shows superior inhibition of IgE binding to FcεRI, basophil activation, IgE production by B cells and passive systemic anaphylaxis in an in vivo mouse model, ligelizumab is less potent in inhibiting IgE:CD23 interactions than omalizumab. Our data thus provide a structural and mechanistic foundation for understanding the efficient suppression of FcεRI-dependent allergic reactions by ligelizumab in vitro as well as in vivo.
Immunoglobulin E (IgE) plays a central role in allergic responses, yet therapeutic targeting of IgE with antibodies such as omalizumab is met with various limitations. Here the authors characterize the molecular properties and crystal structure of a new anti-IgE antibody, ligelizumab, for mechanistic insights related to its enhanced suppression activity.
Publisher
Nature Publishing Group UK,Nature Publishing Group,Nature Portfolio
Subject
/ 13/31
/ 14/1
/ 64/60
/ 82/103
/ Allergy
/ Animals
/ Anti-Allergic Agents - administration & dosage
/ Anti-Allergic Agents - chemistry
/ Antibodies, Anti-Idiotypic - administration & dosage
/ Antibodies, Anti-Idiotypic - chemistry
/ Antibodies, Monoclonal, Humanized - administration & dosage
/ B-Lymphocytes - drug effects
/ Binding
/ Epitopes
/ Humanities and Social Sciences
/ Humans
/ Hypersensitivity - drug therapy
/ Hypersensitivity - immunology
/ Immunoglobulin E - chemistry
/ Immunoglobulin E - immunology
/ Mice
/ Omalizumab - administration & dosage
/ Science
