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Identification of Porphyromonas gingivalis lipopolysaccharide-binding proteins in human saliva

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dc.contributor.authorChoi, Seulggie-
dc.contributor.authorBaik, Jung Eun-
dc.contributor.authorJeon, Jun Ho-
dc.contributor.authorCho, Kun-
dc.contributor.authorKum, Kee-Yeon-
dc.contributor.authorHan, Seung Hyun-
dc.contributor.authorYun, Cheol-Heui-
dc.contributor.authorSeo, Deog-Gyu-
dc.date.accessioned2013-01-14T07:26:04Z-
dc.date.available2013-01-14T07:26:04Z-
dc.date.issued2011-09-
dc.identifier.citationMOLECULAR IMMUNOLOGY, Vol.48, No.15-16, pp.2207-2213ko_KR
dc.identifier.issn0161-5890-
dc.identifier.urihttp://hdl.handle.net/10371/80470-
dc.description.abstractPorphyromonas 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.sponsorshipThis 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.isoenko_KR
dc.publisherPERGAMON-ELSEVIER SCIENCE LTDko_KR
dc.subjectPorphyromonas gingivalisko_KR
dc.subjectLipopolysaccharideko_KR
dc.subjectLipopolysaccharide-binding proteinsko_KR
dc.subjectMass spectrometryko_KR
dc.subjectSalivako_KR
dc.titleIdentification of Porphyromonas gingivalis lipopolysaccharide-binding proteins in human salivako_KR
dc.typeArticleko_KR
dc.contributor.AlternativeAuthor백정은-
dc.contributor.AlternativeAuthor전준호-
dc.contributor.AlternativeAuthor조건-
dc.contributor.AlternativeAuthor금기연-
dc.contributor.AlternativeAuthor한승현-
dc.contributor.AlternativeAuthor윤철희-
dc.contributor.AlternativeAuthor서덕규-
dc.identifier.doi10.1016/j.molimm.2011.06.434-
dc.citation.journaltitleMOLECULAR IMMUNOLOGY-
dc.description.tc1-
Appears in Collections:
College of Dentistry/School of Dentistry (치과대학/치의학대학원)Dept. of Dentistry (치의학과)Journal Papers (저널논문_치의학과)
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