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Reshaping human antibodies for therapy
A human IgGI antibody has been reshaped for serotherapy in humans by introducing the six hypervariable regions from the heavy- and light-chain variable domains of a rat antibody directed against
Comparison of the effector functions of human immunoglobulins using a matched set of chimeric antibodies
The results suggest that IgG1 might be the favoured IgG subclass for therapeutic applications in complement-dependent hemolysis and in antibody-dependent cell-mediated cytotoxicity using both human effector and human target cells.
Antibody humanization: a case of the 'Emperor's new clothes'?
  • M. Clark
  • Medicine
    Immunology today
  • 1 August 2000
Although there is clear evidence that chimeric antibodies are less immunogenic than murine monoclonal antibodies, little evidence exists to support claims for further improvements as a result of more elaborate humanization protocols.
Recombinant human IgG molecules lacking Fcγ receptor I binding and monocyte triggering activities
The aim is to engineer non‐destructive human IgG constant regions for therapeutic applications where depletion of cells bearing the target antigen is undesirable and a lack of killing via Fcγ receptors (R) and complement but retention of neonatal FcR binding to maintain placental transport and the prolonged half‐life of IgG.
A genetically reshaped human IgG1 monoclonal antibody (CAMPATH-1H) was used to treat two patients with non-Hodgkin lymphoma and might have an important use in the treatment of lymphoproliferative disorders and additionally as an immunosuppressive agent.
Sequences of complementary DNAs that encode the NA1 and NA2 forms of Fc receptor III on human neutrophils.
The amino acid substitutions and differences in the number of potential N-linked glycosylation sites probably account for the different forms of neutrophil FcR III observed after digestion with N-glycanase and for the antigenic heterogeneity of this receptor.
The herpes simplex virus type 1 Fc receptor discriminates between IgG1 allotypes
Using recombinant monoclonal IgG molecules of known isotype and mutants thereof, it is unexpectedly discovered that the HSV‐1 FcR discriminates between IgG1 allotypes, evidence of functional differences between Igg1 allotype that may account for their distribution in populations.
Human IgG isotypes and activating Fcγ receptors in the interaction of Salmonella enterica serovar Typhimurium with phagocytic cells
The results show that IgG binding to OmpA increases the uptake of Salmonella by human phagocytic cells and that the efficiency of this process depends both on the subclass of the IgG and the type of FcR that is available for antibody binding.
Recombinant HPA-1a antibody therapy for treatment of fetomaternal alloimmune thrombocytopenia: proof of principle in human volunteers.
It is demonstrated that HPA-1a1b autologous platelets (matching fetal phenotype) sensitized with B2G1Δnab have the same intravascular survival as unsensitized platelets, and it is shown that platelets Sensitized with a combination of B2 G1 and B2Nab survive 3 times as long in circulation compared with platelets sensitized with B1G1 alone.
Expression of human FcgammaRIIIa as a GPI-linked molecule on CHO cells to enable measurement of human IgG binding.
These robust assays should be valuable for batch-testing clinical material as well as providing tools for improving the design of therapeutic IgG, by choosing the appropriate method, weakly- or strongly-binding IgG can be efficiently compared.