Fusion of the Fc part of human IgG1 to CD14 enhances its binding to gram-negative bacteria and mediates phagocytosis by Fc receptors of neutrophils.

No abstract is available for this paper.

• Publication year

  2012

• Venue

  Immunology Letters

• Publication date

  2012-08-30

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1016/j.imlet.2012.04.008PMID 22575527
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• A novel peptide-IgG conjugate, CAP18(106-138)-IgG, that binds and neutralizes endotoxin and kills gram-negative bacteria.

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

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• Image‐based cytometry reveals three distinct subsets of activated granulocytes based on phagocytosis and oxidative burst

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• Hydrophobic Amino-terminal Pocket Cd14 Reveals a Bent Solenoid with a the Crystal Structure of Human Soluble

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