Special Issue "Modes of Antibody Action for Cancer Therapy"
A special issue of Antibodies (ISSN 2073-4468).
Deadline for manuscript submissions: closed (31 March 2013)
Prof. Dr. Patrick A. Baeuerle
AMGEN Research (Munich) GmbH, Staffelseestr. 2, 81477 Munich, Germany
Interests: bispecific antibodies; T cells; antibody drug conjugates; Fc-engineered antibodies; cancer therapy; antibody targets
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
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. Papers will be published continuously (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as 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 refereed through a 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). English correction and/or formatting fees of 250 CHF (Swiss Francs) will be charged in certain cases for those articles accepted for publication that require extensive additional formatting and/or English corrections.
- antibody-dependent cellular cytotoxicity (ADCC)
- complement-dependent cytotoxicity (CDC)
- antibody drug conjugates
- radioimmuno conjugates
- Fc gamma engineering
- bispecific antibodies
- T or NK cell engaging antibodies
- immune-stimulating antibodies
The below list represents only planned manuscripts. Some of these manuscripts have not been received by the Editorial Office yet. Papers submitted to MDPI journals are subject to peer-review.
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.