| Staphylococcal superantigen-like protein 3 binds to the Toll-like receptor 2 extracellular domain and inhibits cytokine production induced by Staphylococcus aureus, cell wall component, or lipopeptides in murine macrophages. | |
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MedLine Citation:
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PMID: 22665377 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Staphylococcal superantigen-like proteins (SSLs) are a family of exoproteins sharing structural similarity with superantigens, but no superantigenic activity. Corresponding host target proteins or receptors against a portion of SSLs in the family have been identified. In this study, we show that SSL3 specifically binds to Toll-like receptor 2 (TLR2) and inhibits the stimulation of macrophages by TLR2 ligands. An approximately 100-kDa protein was recovered by using recombinant His-tagged SSL3-conjugated Sepharose from the lysate of porcine spleen, and the protein was identified as porcine TLR2 by peptide mass fingerprinting analysis. The SSL3-conjugated Sepharose recovered human and mouse TLR2 but not TLR4 from human neutrophils and mouse macrophage RAW 264.7 cells, as well as a recombinant TLR2 extracellular domain chimera protein. The production levels of interleukin 12 (IL-12) from mouse macrophages treated with heat-killed Staphylococcus aureus and of tumor necrosis factor alpha (TNF-α) from RAW 264.7 cells induced by peptidoglycan or lipopeptide TLR2 ligands were strongly suppressed in the presence of SSL3. The mutation of consensus sialic acid-containing glycan-binding residues in SSL3 did not abrogate the binding ability to TLR2 or inhibitory activity on TLR2, indicating that the interaction of SSL3 with TLR2 was independent of the sialic acid-containing glycan-binding residues. These findings demonstrate that SSL3 is able to bind the extracellular domain of TLR2 and interfere with TLR2 function. The present study provides a novel mechanism of SSL3 in immune evasion of S. aureus via interfering with its recognition by innate immune cells. |
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Authors:
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Ryosuke Yokoyama; Saotomo Itoh; Go Kamoshida; Takemasa Takii; Satoshi Fujii; Tsutomu Tsuji; Kikuo Onozaki |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2012-06-04 |
Journal Detail:
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Title: Infection and immunity Volume: 80 ISSN: 1098-5522 ISO Abbreviation: Infect. Immun. Publication Date: 2012 Aug |
Date Detail:
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Created Date: 2012-07-19 Completed Date: 2012-10-10 Revised Date: 2013-04-08 |
Medline Journal Info:
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Nlm Unique ID: 0246127 Medline TA: Infect Immun Country: United States |
Other Details:
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Languages: eng Pagination: 2816-25 Citation Subset: IM |
Affiliation:
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Department of Molecular Health Sciences, Graduate School of Pharmaceutical Sciences, Nagoya City University, Tanabe-dori, Mizuho-ku, Nagoya, Japan. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Bacterial Proteins / genetics, metabolism* Cell Wall / metabolism Cytokines / antagonists & inhibitors, metabolism* Gene Expression Regulation / physiology Lipopeptides / pharmacology Macrophages / drug effects, immunology, metabolism* Mice Peptidoglycan / metabolism, pharmacology Protein Structure, Tertiary Staphylococcus aureus / genetics, immunology, metabolism* Superantigens / metabolism Toll-Like Receptor 2 / genetics, immunology, metabolism* |
| Chemical | |
Reg. No./Substance:
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0/Bacterial Proteins; 0/Cytokines; 0/Lipopeptides; 0/Peptidoglycan; 0/Superantigens; 0/Tlr2 protein, mouse; 0/Toll-Like Receptor 2 |
| Comments/Corrections | |
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