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Identification of Porphyromonas gingivalis lipopolysaccharide-binding proteins in human saliva
DC Field | Value | Language |
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dc.contributor.author | Choi, Seulggie | - |
dc.contributor.author | Baik, Jung Eun | - |
dc.contributor.author | Jeon, Jun Ho | - |
dc.contributor.author | Cho, Kun | - |
dc.contributor.author | Kum, Kee-Yeon | - |
dc.contributor.author | Han, Seung Hyun | - |
dc.contributor.author | Yun, Cheol-Heui | - |
dc.contributor.author | Seo, Deog-Gyu | - |
dc.date.accessioned | 2013-01-14T07:26:04Z | - |
dc.date.available | 2013-01-14T07:26:04Z | - |
dc.date.issued | 2011-09 | - |
dc.identifier.citation | MOLECULAR IMMUNOLOGY, Vol.48, No.15-16, pp.2207-2213 | ko_KR |
dc.identifier.issn | 0161-5890 | - |
dc.identifier.uri | https://hdl.handle.net/10371/80470 | - |
dc.description.abstract | Porphyromonas gingivalis causes periodontal diseases and its lipopolysaccharide (LPS) is considered as a major virulence factor responsible for pathogenesis. Since initial recognition of P. gingivalis LPS (Pg.LPS) in the oral cavity might be crucial for the host response, we identified Pg.LPS-binding proteins (Pg.LPS-BPs) using Pg.LPS-immobilized beads and a high-resolution mass spectrometry. LPS purified from P. gingivalis was conjugated onto N-hydroxysuccinimidyl-Sepharose (R) 4 Fast Flow beads. Notably, Pg.LPS-conjugated beads could stimulate Toll-like receptor 2 (TLR2) as determined by a TLR2-depdendent reporter expression system using CHO/CD14/TLR2. In addition, the Pg.LPS-conjugated beads induced the production of inflammatory mediators such as nitric oxide and interferon-gamma-inducible protein-10 in the macrophage cell-line, RAW 264.7. These results imply that Pg.LPS retained its immunological properties during the conjugation process. Then, the Pg.LPS-conjugated beads were mixed with a pool of saliva obtained from nine human subjects to capture Pg.LPS-BPs and molecular identities were determined by LTQ-Orbitrap hybrid fourier transform mass spectrometry. Pg.LPS-BPs captured at high frequencies included alpha-amylase, cystatin, prolactin-inducible protein, lysozyme C, immunoglobulin components, serum albumin, lipocalin-1, and submaxillary gland androgen-regulated protein 3B. These proteins are known to be involved in bacterial adhesion and colonization, anti-microbial functions or modulation of immune responses. (C) 2011 Elsevier Ltd. All rights reserved. | ko_KR |
dc.description.sponsorship | This research was supported by the grants from the National Research Foundation (NRF) of Korea funded by the Ministry of Education, Science and Technology (MEST) (Nos. 2009-0086835, 2010-0029116, and 20110001030), Republic of Korea. | - |
dc.language.iso | en | ko_KR |
dc.publisher | PERGAMON-ELSEVIER SCIENCE LTD | ko_KR |
dc.subject | Porphyromonas gingivalis | ko_KR |
dc.subject | Lipopolysaccharide | ko_KR |
dc.subject | Lipopolysaccharide-binding proteins | ko_KR |
dc.subject | Mass spectrometry | ko_KR |
dc.subject | Saliva | ko_KR |
dc.title | Identification of Porphyromonas gingivalis lipopolysaccharide-binding proteins in human saliva | ko_KR |
dc.type | Article | ko_KR |
dc.contributor.AlternativeAuthor | 백정은 | - |
dc.contributor.AlternativeAuthor | 전준호 | - |
dc.contributor.AlternativeAuthor | 조건 | - |
dc.contributor.AlternativeAuthor | 금기연 | - |
dc.contributor.AlternativeAuthor | 한승현 | - |
dc.contributor.AlternativeAuthor | 윤철희 | - |
dc.contributor.AlternativeAuthor | 서덕규 | - |
dc.identifier.doi | 10.1016/j.molimm.2011.06.434 | - |
dc.citation.journaltitle | MOLECULAR IMMUNOLOGY | - |
dc.description.tc | 1 | - |
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