Special Issue "Recombinant Immunotoxins"

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

Deadline for manuscript submissions: closed (30 November 2012)

Special Issue Editors

Guest Editor
Prof. Dr. Itai Benhar
Department of Molecular Microbiology and Biotechnology, The George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv 69978, Israel
Website: http://www.tau.ac.il/lifesci/departments/biotech/members/benhar/benhar.html
E-Mail: benhar@post.tau.ac.il
Interests: monoclonal antibodies; recombinant antibodies; bispecific antibodies; antibody selection strategies; phage display; antibody humanization; targeted phage nanomedicines; antibody based biosensors; analysis of antibody repertoires by next-generation sequencing and proteomic approaches; protease-activated toxins; cytotoxic enzymes

Guest Editor
Prof. Dr. Stefan Barth
Fraunhofer IME-MB, Forckenbeckstr. 6, 52074 Aachen, Germany
Website: http://www.ime.fraunhofer.de
E-Mail: stefan.barth@ime.fraunhofer.de
Interests: monoclonal antibodies; recombinant antibody formats; phage display; immunization strategies; EBV transformation; antibody selection strategies; humanization strategies; cell surface antigens: CD7, CD25, CD30, CD33, CD38, CD64, C123, c-kit receptor; EGF receptor; cytotoxic enzymes

Special Issue Information

Dear Colleagues,

Immunotoxins comprise a field in targeted cancer therapeutics. These chimeric proteins are a form of biological guided missiles that combine a disease-specific targeting moiety with a potent effector molecule. The targeting moiety is mostly a monoclonal antibody or a recombinant antibody based fragment that confers target specificity to the immunotoxin. The effector domain is in most cases a potent protein toxin of bacterial or plant origin. Notwithstanding, immunotoxins targeted by non-antibody molecules do exist as well as immunotoxins where the effector domain is derived from a human enzyme including RNAses, proteases or kinases. Following binding to the target cells, the immunotoxin undergoes internalization, intracellular processing and trafficking and eventually causes cell death by either catalytically inhibiting a vital process and/or by activating a cell-death cascade. Over the 25 some years of their evolution, immunotoxins have been engineered to better fit to their purpose, improving on specificity and reducing undesirable properties such as untoward toxicities and immunogenicity. Many immunotoxins have undergone clinical evaluation, some showing promise and progressing to advanced clinical trials. This special issue of “Antibodies” will review recent developments as reported by experts in this exciting field. Covered topics will include target selection, toxin selection, targeting moiety selection and engineering, disease models and preclinical studies, clinical studies as well as adverse effects.

Prof. Dr. Itai Benhar
Prof. Dr. Dr. Stefan Barth
Guest Editors

Keywords

  • pseudomonas exotoxin
  • diphtheria toxin
  • ricin
  • Saporin
  • other RIPs
  • human enzymes
  • RNAses
  • immunotoxin targets
  • IgGs
  • antibody fragments
  • non-antibody-based disease models and preclinical studies
  • clinical studies
  • adverse effects

Published Papers (9 papers)

Antibodies 2014, 3(1), 92-115; doi:10.3390/antib3010092
Received: 19 November 2013; in revised form: 23 January 2014 / Accepted: 28 January 2014 / Published: 19 February 2014
Show/Hide Abstract | PDF Full-text (430 KB) | HTML Full-text | XML Full-text

Antibodies 2013, 2(3), 517-534; doi:10.3390/antib2030517
Received: 15 August 2013; in revised form: 22 August 2013 / Accepted: 22 August 2013 / Published: 17 September 2013
Show/Hide Abstract | PDF Full-text (215 KB) | HTML Full-text | XML Full-text

Antibodies 2013, 2(2), 236-269; doi:10.3390/antib2020236
Received: 27 December 2012; in revised form: 8 April 2013 / Accepted: 11 April 2013 / Published: 19 April 2013
Show/Hide Abstract | Cited by 2 | PDF Full-text (337 KB) | HTML Full-text | XML Full-text

Antibodies 2013, 2(2), 209-235; doi:10.3390/antib2020209
Received: 4 March 2013; in revised form: 27 March 2013 / Accepted: 5 April 2013 / Published: 17 April 2013
Show/Hide Abstract | Cited by 3 | PDF Full-text (809 KB) | HTML Full-text | XML Full-text
abstract graphic

Antibodies 2013, 2(1), 130-151; doi:10.3390/antib2010130
Received: 24 December 2012; in revised form: 18 February 2013 / Accepted: 20 February 2013 / Published: 27 February 2013
Show/Hide Abstract | Cited by 2 | PDF Full-text (759 KB) | HTML Full-text | XML Full-text

Antibodies 2013, 2(1), 82-92; doi:10.3390/antib2010082
Received: 6 December 2012; in revised form: 19 January 2013 / Accepted: 22 January 2013 / Published: 28 January 2013
Show/Hide Abstract | PDF Full-text (169 KB) | HTML Full-text | XML Full-text | Supplementary Files

Antibodies 2013, 2(1), 50-65; doi:10.3390/antib2010050
Received: 26 November 2012; in revised form: 31 December 2012 / Accepted: 7 January 2013 / Published: 16 January 2013
Show/Hide Abstract | PDF Full-text (457 KB) | HTML Full-text | XML Full-text | Supplementary Files
abstract graphic

Antibodies 2013, 2(1), 19-49; doi:10.3390/antib2010019
Received: 13 December 2012; in revised form: 4 January 2013 / Accepted: 8 January 2013 / Published: 16 January 2013
Show/Hide Abstract | Cited by 2 | PDF Full-text (359 KB) | HTML Full-text | XML Full-text

Antibodies 2013, 2(1), 9-18; doi:10.3390/antib2010009
Received: 5 December 2012; in revised form: 4 January 2013 / Accepted: 8 January 2013 / Published: 11 January 2013
Show/Hide Abstract | Cited by 2 | PDF Full-text (1742 KB) | HTML Full-text | XML Full-text

Last update: 20 February 2014

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