Special Issue "Modes of Antibody Action for Cancer Therapy"

Guest Editor
Prof. Dr. Patrick A. Baeuerle
AMGEN Research (Munich) GmbH, Staffelseestr. 2, 81477 Munich, Germany
E-Mail: baeuerle@amgen.com
Phone: +49 89 895277-601
Fax: +49 89 895277-88601
Interests: bispecific antibodies; T cells; antibody drug conjugates; Fc-engineered antibodies; cancer therapy; antibody targets

Dear Colleagues,

Antibody-based therapies have high potential to treat malignant diseases. Very different modes of action can be employed to this end. There are intrinsic properties of antibodies such as ADCC, which can be enhanced by Fc gamma engineering, CDC, or an anti-apoptotic activity induced by antibody binding to a specific target antigen. There are also ways of bolting onto antibodies toxic compounds for improving efficacy. Conjugation of antibodies with plant or bacterial toxins leads to immunotoxins, with chemotherapeutics to antibody drug conjugates (ADCs), and with radioisotopes to radioimmunoconjugates. Bispecific antibodies have the potential to inhibit at a time two receptors, neutralize two angiogenic factors, or combinations thereof. Bispecific antibodies can also be used to tether T cells to cancer target cells, which is not possible with conventional antibodies. Lastly, antibodies binding to immune regulatory receptors can significantly  support natural or antibody-mediated immune reactions against tumors. For each class, there are now drug candidates under late-stage development, or on the market. A special issues with focus on "modes of antibody action against cancer" will review recent developments and allow comparison of these different modes of action.

Prof. Dr. Patrick A. Baeuerle
Guest Editor

Submission

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• antibody-dependent cellular cytotoxicity (ADCC)
• complement-dependent cytotoxicity (CDC)
• antibody drug conjugates
• immunotoxins
• immunocytokines
• radioimmuno conjugates
• Fc gamma engineering
• bispecific antibodies
• T or NK cell engaging antibodies
• immune-stimulating antibodies

Type of Paper: Review
Title: Role and Redirection of IgE Against Cancer
Author: Luca Vangelista
Affiliation: San Raffaele Scientific Institute, Milan, Italy
Abstract: IgE is a highly elusive antibody isotype, yet a tremendously powerful elicitor of immune reactions. Despite huge efforts spent on the characterization and understanding of the IgE system many questions remain either unanswered or only marginally addressed. One above all relates to the role of IgE. A common doubt is based on whether IgE mode of action should only be relegated to anti-parasite immunity and allergic manifestations. In search for a hidden role of IgE, reports from several laboratories are described herein in which a natural IgE link to cancer or the experimental redirection of IgE against cancer have been investigated. Epidemiological and investigational studies are trying to elucidate a possible direct intervention of endogenous IgE against cancer, raising thus far no definitive evidence. Conversely, experimental approaches implementing several strategies and engineered IgE formats built up a series of convincing results indicating that cancer might be tackled by the effector functions of this immunoglobulin isotype. Because of its peculiar immune features, IgE may present a superior anti-tumor performance as compared to IgG. However, extreme care should be taken on how IgE-based anti-tumor approaches should be devised. Overall, IgE appears as a promising resource, likely destined to enrich the anti-cancer arsenal.

Type of Paper: Review
Title: IgG Effector Function Dictated by the Fc Glycan Composition
Authors: Kai-Ting Chuang and Robert M. Anthony
Affiliation: Center for Immunology and Inflammatory Diseases, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02129, USA
Abstract: IgG antibodies are the basis for some of the most effective therapeutics developed over the last 20 years. These proteins are highly specific, have long serum-half lives, and can be produced relatively routinely, making them ideal drugs. Importantly, the effector functions that are elicited by IgG antibodies can be enhanced or manipulated by the composition of the single, N-linked glycan attached to the Fc. IgG antibodies with identical protein sequences can gain 50- fold increased potency, in terms of initiating antibody-dependent cytotoxicity, by removing a single, specific sugar moiety from the Fc glycan. Conversely, the addition of sialic acid to the terminus of the Fc glycan converts IgG antibodies into anti-inflammatory mediators, capable of suppressing autoantibody driven inflammation. This review will discuss the contribution of the Fc glycan to IgG antibody effector functions, the regulation of the Fc glycan in vivo, and implications for the rationale design of IgG antibody-based therapeutics.