{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,26]],"date-time":"2026-09-26T00:02:59Z","timestamp":1790380979992,"version":"4.1.0"},"reference-count":35,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2017,2,1]],"date-time":"2017-02-01T00:00:00Z","timestamp":1485907200000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Journal of Periodontology"],"published-print":{"date-parts":[[2017,2]]},"abstract":"<jats:p><jats:bold>Background:<\/jats:bold> Although periodontal pathogens show a strong association with development of atherosclerosis, little is known about how a microorganism contributes to disease onset and progression. Oxidation of low\u2010density lipoprotein (LDL) is a major risk factor of atherogenesis. The principal objective of this study is to evaluate the ability of peptide 19 (Pep19) of <jats:italic>Porphyromonas gingivalis<\/jats:italic> (<jats:italic>Pg<\/jats:italic>) heat shock protein (HSP) as a potent inducer of LDL oxidation, and a secondary objective is to compare this ability with that of Pep19 from different bacteria.<\/jats:p><jats:p><jats:bold>Methods:<\/jats:bold> HSP60, Pep14, and Pep19 from <jats:italic>Pg<\/jats:italic> and THP\u20101 monocytes were cultured, and the extent of LDL oxidation induced by each peptide was evaluated by an assay for thiobarbituric acid\u2010reactive substances (TBARS). Pep19 and HSP60 from <jats:italic>Chlamydia pneumoniae<\/jats:italic> and <jats:italic>Mycobacterium tuberculosis<\/jats:italic> were also cultured with THP\u20101 monocytes and evaluated by the TBARS assay. After incubation of macrophages with LDL and peptides from <jats:italic>Pg<\/jats:italic>, Oil Red O staining was performed for examination of foam cells, macrophages that took up the oxidized LDL.<\/jats:p><jats:p><jats:bold>Results:<\/jats:bold> Monocyte\u2010mediated native\u2010LDL oxidation under the influence of Pep19 or HSP60 from <jats:italic>Pg<\/jats:italic> was significantly stronger than oxidation induced by the counterpart Pep19 or HSP60 from <jats:italic>C. pneumoniae<\/jats:italic> or <jats:italic>M. tuberculosis<\/jats:italic>. Pep19 from <jats:italic>Pg<\/jats:italic> HSP60 showed a stronger ability to induce LDL oxidation than did Pep14 from <jats:italic>Pg<\/jats:italic> HSP60.<\/jats:p><jats:p><jats:bold>Conclusion:<\/jats:bold> These results suggest Pep19 from <jats:italic>P<\/jats:italic>g HSP60 has a distinct ability to induce native\u2010LDL oxidation as a plausible mechanism by which this peptide may drive epitope spreading to the neoantigen, i.e., oxidized LDL, in the pathogenesis of atherosclerosis.<\/jats:p>","DOI":"10.1902\/jop.2016.160402","type":"journal-article","created":{"date-parts":[[2016,10,7]],"date-time":"2016-10-07T04:14:15Z","timestamp":1475813655000},"source":"Crossref","is-referenced-by-count":17,"title":["Peptide 19 of <i>Porphyromonas gingivalis<\/i> Heat Shock Protein Is a Potent Inducer of Low\u2010Density Lipoprotein 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