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Escherichia coli Bound to the Primate Erythrocyte Complement Receptor via Bispecific Monoclonal Antibodies Are Transferred to and Phagocytosed by Human Monocytes in an In Vitro Model¹

Susan E. Kuhn^*, Alessandra Nardin^*, Philip E. Klebba and Ronald P. Taylor^2,*

^* Department of Biochemistry, University of Virginia School of Medicine, Charlottesville, VA 22908; and Department of Chemistry and Biochemistry, University of Oklahoma, Norman, OK 73019

We have prepared cross-linked, bispecific mAb complexes (heteropolymers) that facilitate rapid and quantitative binding of a prototype pathogen, Escherichia coli, to the complement receptor (CR1) on primate erythrocytes. Incubation of the erythrocyte-heteropolymer-E. coli complexes with freshly isolated human mononuclear cells leads to rapid removal of the E. coli from the erythrocytes, and phagocytosis and killing of the bacteria. The erythrocytes are not lysed or phagocytosed during this transfer reaction, but both heteropolymer and CR1 are removed from the erythrocytes along with the E. coli. These findings parallel observations made in previous in vivo experiments in which heteropolymers were used to facilitate clearance of innocuous prototype pathogens in a monkey model. It should now be possible to extend the heteropolymer paradigm to a live pathogen in a primate model.

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