Competition between rBPI23, a recombinant fragment of bactericidal/permeability-increasing protein, and lipopolysaccharide (LPS)-binding protein for binding to LPS and gram-negative bacteria.

@article{GAZZANOSANTORO1994CompetitionBR,
  title={Competition between rBPI23, a recombinant fragment of bactericidal/permeability-increasing protein, and lipopolysaccharide (LPS)-binding protein for binding to LPS and gram-negative bacteria.},
  author={HELENE GAZZANO-SANTORO and K. M{\'e}sz{\'a}ros and Cynthia Birr and Stephen F. Carroll and Georgia Theofan and Arnold H. Horwitz and Ed Wyn Lim and Silke Aberle and Herbert G Kasler and J. Brian Parent},
  journal={Infection and immunity},
  year={1994},
  volume={62 4},
  pages={1185-91}
}
Lipopolysaccharide (LPS)-binding protein (LBP) and bactericidal/permeability-increasing protein (BPI) are two structurally related lipid A-binding proteins with divergent functional activities. LBP mediates activation of macrophage and other proinflammatory cells. In contrast, BPI has potent bactericidal and LPS-neutralizing activities. A recombinant fragment of BPI (rBPI23) retains the potent biological activities of the holo protein and may represent a novel therapeutic agent for the… CONTINUE READING

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