Mutation of amino acids 39-44 of human CD14 abrogates binding of lipopolysaccharide and Escherichia coli.

@article{Stelter1997MutationOA,
  title={Mutation of amino acids 39-44 of human CD14 abrogates binding of lipopolysaccharide and Escherichia coli.},
  author={Felix Stelter and Martin Bernheiden and Ren{\'e} Menzel and Robert Smail Jack and Stephanie L Witt and Xiaohong Fan and Martin Pfister and Christine Schuett},
  journal={European journal of biochemistry},
  year={1997},
  volume={243 1-2},
  pages={100-9}
}
As a key receptor for lipopolysaccharide (LPS) on the surface of monocytes and macrophages, the CD14 molecule is primarily involved in non-specific host defense mechanisms against gram-negative bacteria. To delineate the structural basis of LPS binding, 23 mutants in the N-terminal 152 amino acids of human CD14 were generated and stably transfected into CHO cells. In each mutant, a block of five amino acids was substituted by alanine. Reactivity of the mutants with anti-CD14 mAbs, and their… CONTINUE READING

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