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Macrophages Expressing a Fusion Protein Derived From Bactericidal/Permeability-Increasing Protein and IgG Are Resistant to Endotoxin

Peter S. Dahlberg, MD; Robert D. Acton, MD; Marc E. Uknis, MD; Hanz G. Klaerner, MD; Jennifer W. Johnston; Christopher D. Levelle; Beulah H. Gray, PhD; David L. Dunn, MD, PhD
Arch Surg. 1996;131(11):1173-1178. doi:10.1001/archsurg.1996.01430230055010.
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Objectives:  To generate a recombinant fusion protein (FP) based on the endotoxin-binding domain of bactericidal/permeability-increasing protein (BPI) and the constant domain of IgG and to test its ability to inhibit lipopolysaccharide (LPS)-induced macrophage tumor necrosis factor α (TNF-α) secretion.

Design:  A murine macrophage cell line, RAW 264.7, was transfected with a BPI-IgG FP before incubation with LPS. The amount of LPS-induced TNF-α protein secreted was measured and compared with that secreted by cells transfected with a control construct.

Setting:  Basic science research laboratory.

Main Outcome Measure:  Secreted TNF-α protein concentration.

Results:  After transfection, RAW 264.7–cell FP expression was detected in cell lysates and supernatants. At each LPS dose tested, cells transfected with the FP gene secreted less TNF-α than did cells transfected with a control construct.

Conclusions:  The FP possesses substantial antiendotoxin activity, as delineated by inhibition of LPS-induced TNF-α secretion by murine macrophages transfected with the fusion gene construct. In the future, such FP may be used as a clinical reagent to reduce the morbidity and mortality associated with serious gram-negative bacterial infections in surgical patients.Arch Surg. 1996;131:1173-1178


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