Antibody-Dependent Cell-Mediated Cytotoxicity- and Complement-Dependent Cytotoxicity-Independent Bactericidal Activity of an IgG againstPseudomonasaeruginosaO6ad

Antibody-Dependent Cell-Mediated Cytotoxicity- and Complement-Dependent Cytotoxicity-Independent Bactericidal Activity of an IgG

In addition to Ag recognition, some Abs are capable of killing target organisms in the absence of phagocytes and complement. In this study, we report that an anti-Pseudomonas aeruginosa O6ad LPS IgG 1 , tobacco-expressed human S20 IgG 1 (te-hS20), as well as its recombinant Fab and single-chain variable fragment (scFv) fragments have cellular-and complement-independent bactericidal activity. te...

Antibody-dependent cell-mediated cytotoxicity- and complement-dependent cytotoxicity-independent bactericidal activity of an IgG against Pseudomonas aeruginosa O6ad.

In addition to Ag recognition, some Abs are capable of killing target organisms in the absence of phagocytes and complement. In this study, we report that an anti-Pseudomonas aeruginosa O6ad LPS IgG(1), tobacco-expressed human S20 IgG(1) (te-hS20), as well as its recombinant Fab and single-chain variable fragment (scFv) fragments have cellular- and complement-independent bactericidal activity. ...

Using impedance-based approaches for measuring cell-mediated cytotoxicity and antibody-dependent cell-mediated cytotoxicity (ADCC)

The most common method for measuring cell-mediated cytotoxicity is the release assay. Effector cell-mediated disruption of the target cell membrane results in leakage of its cytoplasmic contents into the culture medium. Endogenous biomolecules (such as lactate dehydrogenase) or previously added exogenous labels (such as the radioisotopes Cr or In) that leak into the media are then measured as a...

Antibody-Mediated, FcR-Dependent Enhancement of Cytotoxicity

Sialylation of IgG Fc domain impairs complement-dependent cytotoxicity.

IgG molecules exert both pro- and antiinflammatory effector functions based on the composition of the fragment crystallizable (Fc) domain glycan. Sialylated IgG Fc domains have antiinflammatory properties that are attributed to their ability to increase the activation threshold of innate effector cells to immune complexes by stimulating the upregulation of the inhibitory Fcγ receptor IIB (FcγRI...