Special Issue "The IgE System"

A special issue of Antibodies (ISSN 2073-4468).

Deadline for manuscript submissions: closed (30 November 2013)

Special Issue Editor

Guest Editor
Dr. Luca Vangelista

Protein Engineering and Therapeutics Group, Division of Immunology, Transplantation and Infectious Diseases, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italy
Website | E-Mail
Interests: molecular biology of IgE and FcεRI; IgE versus cancer; HIV-1 inhibitors and microbicides; CCL5/RANTES engineering; commensal bacteria engineering

Special Issue Information

Dear Colleagues,

The IgE antibody, with its homeostasis, biological significance and disease implications, constitutes a system that sparks the curiosity and interest of a large number of investigators. This interest dates even long before IgE was discovered and characterized and the immune potency and intrinsic difficulty that surrounds some aspects of this antibody class is a continuous source for new discoveries and debates. This Special Issue would reach its purpose by becoming a forum for the state of the art knowledge and dissemination on this fascinating system.

With the aim to keep IgE central to all its multifaceted aspects, this issue welcomes contributions from a wide range of topics, such as: the IgE system regulation (e.g., genetic, molecular and cellular); the B cell differentiation and homeostasis behind IgE production and memory; the IgE receptor system (FcϵRI, CD23, galectins); the central role of IgE in allergy (including aspects related to the IgE-allergen interaction); the IgE system implications in physiology and pathology (including some less classic/obvious implications); the special case of IgE antibody engineering to combat allergic manifestations and beyond (e.g., cancer and IgE formats as antibody engineering tools); and antibody and drug development against IgE (e.g., therapeutic anti-IgE monoclonal antibodies and small chemical inhibitors of the IgE-FcϵRI interaction).

Dr. Luca Vangelista
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All papers will be peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Antibodies is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 350 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.


  • allergy
  • antibody engineering
  • antibody formats
  • antibody fragments
  • B cells
  • clinical studies
  • Fc engineering
  • Fcϵ receptors
  • immune complexes
  • immunoreceptors
  • inflammation
  • monoclonal antibodies
  • preclinical studies
  • signal transduction
  • small-molecule drugs

Published Papers (1 paper)

View options order results:
result details:
Displaying articles 1-1
Export citation of selected articles as:


Open AccessReview IgE and Drug Allergy: Antibody Recognition of ‘Small’ Molecules of Widely Varying Structures and Activities
Antibodies 2014, 3(1), 56-91; https://doi.org/10.3390/antib3010056
Received: 19 November 2013 / Revised: 19 December 2013 / Accepted: 18 January 2014 / Published: 22 January 2014
Cited by 2 | PDF Full-text (2929 KB) | HTML Full-text | XML Full-text
The variety of chemically diverse pharmacologically-active compounds administered to patients is large and seemingly forever growing, and, with every new drug released and administered, there is always the potential of an allergic reaction. The most commonly occurring allergic responses to drugs are the
[...] Read more.
The variety of chemically diverse pharmacologically-active compounds administered to patients is large and seemingly forever growing, and, with every new drug released and administered, there is always the potential of an allergic reaction. The most commonly occurring allergic responses to drugs are the type I, or immediate hypersensitivity reactions mediated by IgE antibodies. These reactions may affect a single organ, such as the nasopharynx (allergic rhinitis), eyes (conjunctivitis), mucosa of mouth/throat/tongue (angioedema), bronchopulmonary tissue (asthma), gastrointestinal tract (gastroenteritis) and skin (urticaria, eczema), or multiple organs (anaphylaxis), causing symptoms ranging from minor itching and inflammation to death. It seems that almost every drug is capable of causing an immediate reaction and it is unusual to find a drug that has not provoked an anaphylactic response in at least one patient. These facts alone indicate the extraordinary breadth of recognition of IgE antibodies for drugs ranging from relatively simple structures, for example, aspirin, to complex molecules, such as the macrolide antibiotics composed of a large macrocyclic ring with attached deoxy sugars. This wide recognition profile is borne out at the molecular level by results of quantitative immunochemical studies where hapten inhibition investigations have identified structural determinants complementary to IgE antibodies in the sera of allergic subjects. Allergenic determinants have been identified on a variety of drugs including neuromuscular blockers, penicillins, cephalosporins, opioids, thiopentone, sulfonamides, trimethoprim, quinolones, chlorhexidine and the non-steroidal anti-inflammatory drug aspirin. It is already clear that IgE can distinguish fine structural differences on a wide variety of molecules, determinants may be at least as small as an amino group or encompass the whole molecule, and individual drugs may demonstrate allergenic heterogeneity. Full article
(This article belongs to the Special Issue The IgE System)

Figure 1

Back to Top