Recombinant chimeric OKT3/IgM antibodies for immune suppression: evaluation in a human CD3 transgenic mouse model

Choi, Ingrid; Schmitt, Wolfgang; Bähre, Alexandra; Little, Melvyn; Cochlovius, Björn

doi:10.1016/s0165-2478(01)00302-9

Cited by 3 publications

(2 citation statements)

References 24 publications

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“…In concert with previous studies showing the increased avidity and increased effect of multivalent mAbs, including those based on scFv, Fab, and IgG (13)(14)(15)(16)(17)(18)(19)(20)(21)(22)(23), the mAb forms evaluated in this study underscore the potential for enhanced therapeutic utility of multivalent mAbs. Although functionally similar with regard to clustering of target molecules, the multivalent mAb forms vary in size and half-life.…”

Section: Discussionsupporting

confidence: 77%

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Design, Construction, and In Vitro Analyses of Multivalent Antibodies

Miller¹,

Meng²,

et al. 2003

The Journal of Immunology

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Some Abs are more efficacious after being cross-linked to form dimers or multimers, presumably as a result of binding to and clustering more surface target to either amplify or diversify cellular signaling. To improve the therapeutic potency of these types of Abs, we designed and generated Abs that express tandem Fab repeats with the aim of mimicking cross-linked Abs. The versatile design of the system enables the creation of a series of multivalent human IgG Ab forms including tetravalent IgG1, tetravalent F(ab′)2, and linear Fab multimers with either three or four consecutively linked Fabs. The multimerized Abs target the cell surface receptors HER2, death receptor 5, and CD20, and are more efficacious than their parent mAbs in triggering antitumor cellular responses, indicating they could be useful both as reagents for study as well as novel therapeutics.

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Section: Discussionsupporting

confidence: 77%

“…Covalently linked full-length IgGs that form tetravalent Abs (5,7,10,11) and naturally occurring IgM and IgG Abs designed to mimic polymeric IgM and IgA via the use of their secretory tailpiece (13)(14)(15) have been evaluated. Another tetravalent form was designed by adding Fab at the C terminus of each H chain of a full-length IgG (16).…”

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confidence: 99%