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Inhibition of antibody‐dependent stimulation of lipoteichoic acid‐treated human monocytes and macrophages by polyglycerolphosphate‐reactive peptides
Author(s) -
Gargir Ari,
Ofek Itzhak,
Hasty David,
MeronSudai Shiri,
Tsubery Hayim,
Keisari Yona,
Nissim Ahuva
Publication year - 2001
Publication title -
journal of leukocyte biology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.819
H-Index - 191
eISSN - 1938-3673
pISSN - 0741-5400
DOI - 10.1189/jlb.70.4.537
Subject(s) - lipoteichoic acid , biology , cytokine , biotinylation , macrophage , antibody , macrophage inflammatory protein , biochemistry , microbiology and biotechnology , immunology , bacteria , staphylococcus aureus , in vitro , genetics
By itself, lipoteichoic acid (LTA) obtained from S. pyogenes, S. aureus , or E. hirae poorly stimulated cytokine production by macrophages, whereas in the presence of anti‐polyglycerol phosphate (PGP), the cells secreted significant amounts of IL‐6. Two peptides constructed from the deduced sequence of the selected anti‐PGP phage‐antibody’s complementary‐determining region 3 of the variable heavy chain (V H ‐CDR3) reacted specifically with PGP. The monomeric form of the peptides markedly inhibited cytokine production by macrophages pretreated with LTA and anti‐LTA. In contrast, the polyvalent form of biotinylated peptides complex with streptavidin‐induced cytokine production by the LTA‐treated macrophages. The data taken together support the concept that cross‐linking of macrophage‐bound LTA by anti‐PGP is required for cytokine release by these cells. Importantly, these studies identified small, PGP‐reactive peptides as potential tools in reducing this proinflammatory process.