4.5 Article

Complexes with anti-epitope tag IgGs improve the therapeutic potential of epitope-tagged antibody fragments

Journal

MOLECULAR IMMUNOLOGY
Volume 47, Issue 7-8, Pages 1529-1534

Publisher

PERGAMON-ELSEVIER SCIENCE LTD
DOI: 10.1016/j.molimm.2010.01.016

Keywords

Epitope tag; Fab; ScFv; Recombinant antibody fragment (rAbF); Anti-epitope tag IgG; Serum persistence; Fc-mediated effector functions; Therapeutic

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The use of recombinant antibody fragments (rAbF) as therapeutic agents is compromised by shorter serum persistences than IgG therapeutics and their inability to mediate Fc-dependent effector functions. Here, we show that the strategy of complex formation between epitope-tagged rAbFs and anti-epitope IgG monoclonal antibodies (mAb) can improve the therapeutic potential of rAbFs by both enhancing their serum persistence and conferring on them the ability to recruit Fc-mediated effector functions. These two mechanistic aspects of this strategy were demonstrated using c-myc- and 6xHis-tagged Fab and scFv rAbFs, both directed against Pseudomonas aeruginosa O6ad, in combination with two different murine anti-epitope tag IgGs, anti-5xHis IgG (Penta-His) and anti-c-myc IgG (9E10). Further enhancement of this strategy for the employment of rAbFs as therapeutics is discussed. Crown Copyright (C) 2010 Published by Elsevier Ltd. All rights reserved.

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