PMID- 23125076
OWN - NLM
STAT- MEDLINE
DCOM- 20130506
LR  - 20121205
IS  - 1860-7314 (Electronic)
IS  - 1860-6768 (Linking)
VI  - 7
IP  - 12
DP  - 2012 Dec
TI  - Current strategies in antibody engineering: Fc engineering and pH-dependent 
      antigen binding, bispecific antibodies and antibody drug conjugates.
PG  - 1444-50
LID - 10.1002/biot.201200250 [doi]
AB  - Antibody engineering technologies are constantly advancing to improve the 
      clinical effectiveness of monoclonal antibodies (mAbs). Effector functions may be 
      modified by engineering the Fc region, for example to improve or reduce binding 
      to Fc gamma receptors (FcgammaRs) or complement factors. Other examples for Fc 
      engineering include modification of the half-life of immunoglobulin G (IgG); 
      various studies have shown that half-life can be prolonged by increasing the 
      affinity of Fc for the Fc neonatal receptor (FcRn). Furthermore, engineered 
      pH-dependent antigen binding can be applied to enhance the recycling of IgG via 
      FcRn, enabling binding to additional target molecules. Since bispecific 
      approaches may elicit desired effects on disease targets, a variety of bispecific 
      formats have been developed, including variants that structurally mimic IgG. 
      Finally, antibody-drug conjugates (ADCs) create new opportunities for treatment 
      of certain diseases. Advances in antibody generation, selection of highly 
      cytotoxic molecules and production of stable linkers have paved the way to the 
      development of many ADCs that can be tested in clinical trials. This review 
      covers current antibody engineering strategies for the modification of 
      therapeutic antibodies in the areas of Fc engineering and pH-dependent antigen 
      binding, bispecific antibodies and ADCs.
CI  - Copyright (c) 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
FAU - Vincent, Karen J
AU  - Vincent KJ
AD  - Novartis Pharma AG, Novartis Institute of Biomedical Research, Basel, 
      Switzerland. karen.vincent@novartis.com
FAU - Zurini, Mauro
AU  - Zurini M
LA  - eng
PT  - Journal Article
PT  - Review
DEP - 20121101
PL  - Germany
TA  - Biotechnol J
JT  - Biotechnology journal
JID - 101265833
RN  - 0 (Antibodies, Bispecific)
RN  - 0 (Immunoconjugates)
RN  - 0 (Receptors, Fc)
RN  - 0 (Recombinant Fusion Proteins)
SB  - IM
MH  - Animals
MH  - Antibodies, Bispecific/*genetics/immunology/metabolism
MH  - Antibody Affinity
MH  - Drug Delivery Systems/*methods
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Immunoconjugates/*genetics/immunology/metabolism
MH  - Protein Binding
MH  - Protein Engineering/*methods
MH  - Receptors, Fc/*genetics/immunology/metabolism
MH  - Recombinant Fusion Proteins/genetics/immunology/metabolism
EDAT- 2012/11/06 06:00
MHDA- 2013/05/07 06:00
CRDT- 2012/11/06 06:00
PHST- 2012/07/13 00:00 [received]
PHST- 2012/09/13 00:00 [revised]
PHST- 2012/10/01 00:00 [accepted]
PHST- 2012/11/06 06:00 [entrez]
PHST- 2012/11/06 06:00 [pubmed]
PHST- 2013/05/07 06:00 [medline]
AID - 10.1002/biot.201200250 [doi]
PST - ppublish
SO  - Biotechnol J. 2012 Dec;7(12):1444-50. doi: 10.1002/biot.201200250. Epub 2012 Nov 
      1.