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The main sources of heme for <jats:italic>P.\u00a0gingivalis in\u00a0vivo<\/jats:italic> are hemoproteins present in saliva, gingival crevicular fluid, and erythrocytes. To acquire heme, <jats:italic>P.\u00a0gingivalis<\/jats:italic> uses several mechanisms. Among them, the best characterized are those employing hemagglutinins, hemolysins, and gingipains (Kgp, RgpA, RgpB), TonB\u2010dependent outer\u2010membrane receptors (HmuR, HusB, IhtA), and hemophore\u2010like proteins (HmuY, HusA). Proteins involved in intracellular heme transport, storage, and processing are less well characterized (e.g. PgDps). Importantly, <jats:italic>P.\u00a0gingivalis<\/jats:italic> may also use the heme acquisition systems of other bacteria to fulfill its own heme requirements. <jats:italic>Porphyromonas gingivalis<\/jats:italic> displays a novel paradigm for heme acquisition from hemoglobin, whereby the Fe(<jats:styled-content style=\"fixed-case\">II<\/jats:styled-content>)\u2010containing oxyhemoglobin molecule must first be oxidized to methemoglobin to facilitate heme release. This process not only involves <jats:italic>P.\u00a0gingivalis<\/jats:italic> arginine\u2010 and lysine\u2010specific gingipains, but other proteases (e.g. interpain A from <jats:italic>Prevotella intermedia<\/jats:italic>) or pyocyanin produced by <jats:italic>Pseudomonas aeruginosa<\/jats:italic>. <jats:italic>Porphyromonas gingivalis<\/jats:italic> is then able to fully proteolyze the more susceptible methemoglobin substrate to release free heme or to wrest heme from it directly through the use of the HmuY hemophore.<\/jats:p>","DOI":"10.1111\/omi.12149","type":"journal-article","created":{"date-parts":[[2015,12,11]],"date-time":"2015-12-11T07:44:52Z","timestamp":1449819892000},"page":"1-23","source":"Crossref","is-referenced-by-count":142,"title":["Heme acquisition mechanisms of <i>Porphyromonas gingivalis<\/i> \u2013 strategies used in a polymicrobial community in a heme\u2010limited host 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