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Identification of human plasma C1 inhibitor as a target protein for staphylococcal superantigen-like protein 5 (SSL5).
Biochem Biophys Res Commun 2019; 508(4):1162-1167BB

Abstract

The family of staphylococcal superantigen-like proteins (SSLs) have a structure similar to bacterial superantigens but exhibit no superantigenic activity. These exoproteins have recently been shown to disturb the host immune defense system. One family member, SSL5, was reported to bind to human leukocyte P-selectin glycoprotein ligand-1 (PSGL-1) and matrix metalloproteinase-9 (MMP-9) and to interfere with leukocyte trafficking. In the present study, we explored human plasma proteins bound by glutathione S-transferase (GST)-tagged recombinant SSL5 (GST-SSL5) and identified plasma protease C1 inhibitor (C1Inh) as a major SSL5-binding protein based on the results of peptide mass fingerprinting analysis with MALDI-TOFMS. GST-SSL5 was found to attenuate the inhibitory activity of recombinant histidine-tagged C1Inh (C1Inh-His) toward complement C1s. We also observed that the treatment of C1Inh-His with neuraminidase markedly decreased its binding to GST-SSL5. Moreover, C1Inh-His produced by Lec2 mutant cells (deficient in sialic acid biosynthesis) showed much lower binding affinity for SSL5 than that produced by the wild-type CHO-K1 cells, as assessed by pull-down assay. These results suggest that SSL5 binds to C1Inh in a sialic acid-dependent fashion and modulates the host immune defense through perturbation of the complement system in association with S. aureus infection.

Authors+Show Affiliations

Department of Microbiology, Hoshi University School of Pharmacy and Pharmaceutical Sciences, Tokyo, Japan. Electronic address: oku@hoshi.ac.jp.Department of Microbiology, Hoshi University School of Pharmacy and Pharmaceutical Sciences, Tokyo, Japan.Department of Microbiology, Hoshi University School of Pharmacy and Pharmaceutical Sciences, Tokyo, Japan.Department of Microbiology, Hoshi University School of Pharmacy and Pharmaceutical Sciences, Tokyo, Japan. Electronic address: tsuji@hoshi.ac.jp.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

30554660

Citation

Oku, Teruaki, et al. "Identification of Human Plasma C1 Inhibitor as a Target Protein for Staphylococcal Superantigen-like Protein 5 (SSL5)." Biochemical and Biophysical Research Communications, vol. 508, no. 4, 2019, pp. 1162-1167.
Oku T, Kurisaka C, Ando Y, et al. Identification of human plasma C1 inhibitor as a target protein for staphylococcal superantigen-like protein 5 (SSL5). Biochem Biophys Res Commun. 2019;508(4):1162-1167.
Oku, T., Kurisaka, C., Ando, Y., & Tsuji, T. (2019). Identification of human plasma C1 inhibitor as a target protein for staphylococcal superantigen-like protein 5 (SSL5). Biochemical and Biophysical Research Communications, 508(4), pp. 1162-1167. doi:10.1016/j.bbrc.2018.12.026.
Oku T, et al. Identification of Human Plasma C1 Inhibitor as a Target Protein for Staphylococcal Superantigen-like Protein 5 (SSL5). Biochem Biophys Res Commun. 2019 Jan 22;508(4):1162-1167. PubMed PMID: 30554660.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Identification of human plasma C1 inhibitor as a target protein for staphylococcal superantigen-like protein 5 (SSL5). AU - Oku,Teruaki, AU - Kurisaka,Chisato, AU - Ando,Yusuke, AU - Tsuji,Tsutomu, Y1 - 2018/12/13/ PY - 2018/11/27/received PY - 2018/12/05/accepted PY - 2018/12/18/pubmed PY - 2018/12/18/medline PY - 2018/12/18/entrez KW - C1 inhibitor KW - Complement KW - Immune perturbation KW - SSL5 KW - Sialic acid KW - Staphylococcus aureus SP - 1162 EP - 1167 JF - Biochemical and biophysical research communications JO - Biochem. Biophys. Res. Commun. VL - 508 IS - 4 N2 - The family of staphylococcal superantigen-like proteins (SSLs) have a structure similar to bacterial superantigens but exhibit no superantigenic activity. These exoproteins have recently been shown to disturb the host immune defense system. One family member, SSL5, was reported to bind to human leukocyte P-selectin glycoprotein ligand-1 (PSGL-1) and matrix metalloproteinase-9 (MMP-9) and to interfere with leukocyte trafficking. In the present study, we explored human plasma proteins bound by glutathione S-transferase (GST)-tagged recombinant SSL5 (GST-SSL5) and identified plasma protease C1 inhibitor (C1Inh) as a major SSL5-binding protein based on the results of peptide mass fingerprinting analysis with MALDI-TOFMS. GST-SSL5 was found to attenuate the inhibitory activity of recombinant histidine-tagged C1Inh (C1Inh-His) toward complement C1s. We also observed that the treatment of C1Inh-His with neuraminidase markedly decreased its binding to GST-SSL5. Moreover, C1Inh-His produced by Lec2 mutant cells (deficient in sialic acid biosynthesis) showed much lower binding affinity for SSL5 than that produced by the wild-type CHO-K1 cells, as assessed by pull-down assay. These results suggest that SSL5 binds to C1Inh in a sialic acid-dependent fashion and modulates the host immune defense through perturbation of the complement system in association with S. aureus infection. SN - 1090-2104 UR - https://www.unboundmedicine.com/medline/citation/30554660/Identification_of_human_plasma_C1_inhibitor_as_a_target_protein_for_staphylococcal_superantigen-like_protein_5_(SSL5) L2 - https://linkinghub.elsevier.com/retrieve/pii/S0006-291X(18)32669-X DB - PRIME DP - Unbound Medicine ER -