Complement Fixation on Cell Surfaces by 19
            <i>S</i>
            and 7
            <i>S</i>
            Antibodies

Borsos, Tibor; Rapp, Herbert J.

doi:10.1126/science.150.3695.505

Cited by 314 publications

(126 citation statements)

References 4 publications

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“…Immunoglobulin G may act as an activator of the classical pathway. A prerequisite for classical activation by IgG is that the Clq binding region at the CHI domain is exposed [32] and that more than one Clq binding region must bind IgG [33]. According to our results, spontaneous adsorption of immunoglobulin G molecules, especially on hydrophobic surfaces, fulfill these prerequisites.…”

Section: Discussionsupporting

confidence: 64%

Complement deposition from human sera on silicon surfaces studied in situ by ellipsometry. The influence of surface wettability

1986

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Organic material deposition from human sera on silicon dioxide surfaces was studied in situ by means of ellipsometry, an optical method for quantification of thin organic films.The deposition of organic material from sera was followed continously for 2 h on hydrophobic and hydrophilic silicon surfaces. Both types of surfaces adsorbed organic material and the additional incubation with anti-C3 resulted in further deposition of organic material indicating the presence of C3 in the organic layers. Addition of EDTA in serum or heat inactivation resulted in a decrease of the amount of organic material deposited on the hydrophobic surface as well as in a lack of subsequent anti-C3 deposition on both hydrophilic and hydrophobic surfaces. Preadsorption with immunoglobulin G on the surfaces caused a pronounced increase of the deposition of material from serum as well as of subsequent anti-C3 deposition. Both effects were absent if EDTA was present in the serum. Our results indicate that complement activation and deposition occur by incubation of human sera on hydrophobic and hydrophilic silicon dioxide surfaces, which are two surfaces with very simple and well-defined chemical composition. The degree of the reversibility of the deposition of immunoglobulin G was furthermore larger on hydrophilic silicon.

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Section: Discussionsupporting

confidence: 64%

Complement deposition from human sera on silicon surfaces studied in situ by ellipsometry. The influence of surface wettability

1986

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“…Binding and activation of Clq requires the formation of doublet IgG on the cell surface (18). Since Hd-IgG intrinsically contains a doublet of Fc regions, it may allow more efficient binding of the polyvalent Clq.…”

Section: Resultsmentioning

confidence: 99%

Engineered humanized dimeric forms of IgG are more effective antibodies.

Caron

Laird

et al. 1992

The Journal of Experimental Medicine

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SummaryHumanized IgG1 M195 (HuG1-M195), a complementarity determining region-grafted recombinant monoclonal antibody, is reactive with CD33, an antigen expressed on myelogenous leukemia cells. M195 is in use in trials for the therapy of acute myelogenous leukemia. Since biological activity of IgG may depend, in part, on multimeric Fab and Fc clustering, homodimeric forms of HuG1-M195 were constructed by introducing a mutation in the 3'1 chain CH3 region gene to change a serine to a cysteine, allowing interchain disulfide bond formation at the COOH terminal of the IgG. Despite similar avidity, the homodimeric IgG showed a dramatic improvement in the ability to internalize and retain radioisotope in target leukemia cells, Moreover, homodimers were 100-fold more potent at complement-mediated leukemia cell killing and antibody-dependent cellular cytotoxicity using human effectors. Therefore, genetically engineered multimeric constructs of IgG may have advantages relative to those forms that are found naturally.

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“…The pentameric structure of IgM, in contrast to IgG, can potentially yield a high avidity for Ag despite a low Ag-specific affinity. Moreover, one molecule of IgM can activate complement, whereas two IgG molecules are required; this may lead to enhanced complement coating of selected self Ags when complexed to IgM, resulting in more efficient engagement of coreceptor signals (16,17). Consequently, BCR signaling could be reduced and MZ B cells preferentially formed in the absence of IgM, despite normal levels of serum IgG.…”

Section: Discussionmentioning

confidence: 99%

Cutting Edge: Selection of B Lymphocyte Subsets Is Regulated by Natural IgM

Baker

Ehrenstein

2002

The Journal of Immunology

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Natural IgM has a wide range of actions in the immune system. Here we demonstrate that mice lacking serum IgM have an expansion in splenic marginal zone B cells with a proportionately smaller reduction in follicular B cells. The increase in the marginal zone-follicular B cell ratio (and an expansion in peritoneal B1a cells) is fully reversed by administration of polyclonal IgM, but not by two IgM monoclonals. Mice engineered to have a secreted oligoclonal IgM repertoire with an endogenous membrane IgM also exhibited a similar expansion of marginal zone B cells. We propose that natural IgM, by virtue of its polyreactivity, enhances Ag-driven signaling through the B cell receptor and promotes the formation of follicular B cells. These results demonstrate that natural IgM regulates the selection of B lymphocyte subsets.

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Complement Fixation on Cell Surfaces by 19 S and 7 S Antibodies

Cited by 314 publications

References 4 publications

Complement deposition from human sera on silicon surfaces studied in situ by ellipsometry. The influence of surface wettability

Complement deposition from human sera on silicon surfaces studied in situ by ellipsometry. The influence of surface wettability

Engineered humanized dimeric forms of IgG are more effective antibodies.

Cutting Edge: Selection of B Lymphocyte Subsets Is Regulated by Natural IgM

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