Engineered human IgG antibodies with longer serum half-lives in primates
Paul R. Hinton,Mary G. Johlfs,Joanna M. Xiong,Kelly Hanestad,Kelly C. Ong,Chuck Bullock,Stephen Keller,Meina Tao Tang,J. Yun Tso,Max Vasquez,Naoya Tsurushita +10 more
TLDR
A pharmacokinetics study of two mutant IgG2 antibodies with increased FcRn binding affinity indicated that they had serum half-lives in rhesus monkeys ∼2-fold longer than the wild-type antibody.About:
This article is published in Journal of Biological Chemistry.The article was published on 2004-02-20 and is currently open access. It has received 454 citations till now. The article focuses on the topics: Neonatal Fc receptor & Binding site.read more
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FcRn: the neonatal Fc receptor comes of age
TL;DR: The neonatal Fc receptor for IgG (FcRn) has been well characterized in the transfer of passive humoral immunity from a mother to her fetus and throughout life, FcRm protects IgG from degradation, thereby explaining the long half-life of this class of antibody in the serum.
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Structure and function of immunoglobulins.
TL;DR: Immunoglobulins are heterodimeric proteins composed of 2 heavy and 2 light chains that can be separated functionally into variable domains that bind antigens and constant domains that specify effector functions, such as activation of complement or binding to Fc receptors.
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Potent antibody therapeutics by design
TL;DR: The generation of potent antibody therapeutics, which I review here, is an iterative design process that involves the generation and optimization of antibodies to improve their clinical potential.
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Therapeutic antibodies for autoimmunity and inflammation
Andrew C. Chan,Paul Carter +1 more
TL;DR: How key insights obtained from the development of therapeutic antibodies complemented by newer antibody engineering technologies are delivering a second generation of therapeutic antibody with promise for greater clinical efficacy and safety is reviewed.
Patent
Dual variable domain immunoglobulins and uses thereof
TL;DR: The present invention relates to engineered multivalent and multispecific binding proteins, methods of making, and specifically to their uses in the prevention, diagnosis, and/or treatment of disease.
References
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Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mp18 and pUC19 vectors
TL;DR: New Escherichia coli host strains have been constructed for the E. coli bacteriophage M13 and the high-copy-number pUC-plasmid cloning vectors and mutations introduced into these strains improve cloning of unmodified DNA and of repetitive sequences.
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Replacing the complementarity-determining regions in a human antibody with those from a mouse
TL;DR: This work substituted the CDRs from the heavy-chain variable region of mouse antibody B1–8, which binds the hapten NP-cap, for the corresponding CDRs of a human myeloma protein, to determine whether the antigen-binding site could be transplanted from one framework to another by grafting theCDRs.
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Chimeric human antibody molecules: mouse antigen-binding domains with human constant region domains
TL;DR: Chimeric genes were constructed that utilized the rearranged and expressed antigen-binding variable region exons from the myeloma cell line S107, which produces an IgA (kappa) anti-phosphocholine antibody as discussed by the authors.
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High Resolution Mapping of the Binding Site on Human IgG1 for FcγRI, FcγRII, FcγRIII, and FcRn and Design of IgG1 Variants with Improved Binding to the FcγR
Robert L. Shields,Angela K. Namenuk,Kyu Hong,Y. Gloria Meng,Julie Rae,Josephine P. Briggs,Dong Xie,Jadine Lai,Andrew Stadlen,Betty Li,Judith A. Fox,Leonard G. Presta +11 more
TL;DR: Select IgG1 variants with improved binding to FcγRIIIA exhibited up to 100% enhancement in antibody-dependent cell cytotoxicity using human effector cells; these variants included changes at residues not found at the binding interface in the IgG/Fcγ RIIIA co-crystal structure.