Pre_GI: SWBIT SVG BLASTP

Query: NC_016610:726128 Tannerella forsythia ATCC 43037 chromosome, complete genome

Lineage: Tannerella forsythia; Tannerella; Porphyromonadaceae; Bacteroidales; Bacteroidetes; Bacteria

General Information: This organism is a key agent in the progression of periodontal disease and is involved in bone loss and loss of attachment of teeth. The pathogenic factors involved in this are poorly understood. Unlike other periodontal organism such as Porphyromonas gingivalis and Prevotella intermedia, this organism is difficult to culture and the prevalence of the organism in periodontal disease may be underestimated. This organism is synergistic with Porphyromonas gingivalis, and the presence of both accelerates progression of the disease.

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BLASTP Alignment.txt

Subject: NC_015571:1207000 Porphyromonas gingivalis TDC60, complete genome

Lineage: Porphyromonas gingivalis; Porphyromonas; Porphyromonadaceae; Bacteroidales; Bacteroidetes; Bacteria

General Information: This organism is associated with severe and chronic periodontal (tissues surrounding and supporting the tooth) diseases. Progression of the disease is caused by colonization by this organism in an anaerobic environment in host tissues and severe progression results in loss of the tissues supporting the tooth and eventually loss of the tooth itself. The black pigmentation characteristic of this bacterium comes from iron acquisition that does not use the typical siderophore system of other bacteria but accumulates hemin. Peptides appear to be the predominant carbon and energy source of this organism, perhaps in keeping with its ability to destroy host tissue. Oxygen tolerance systems play a part in establishment of the organism in the oral cavity, including a superoxide dismutase. Pathogenic factors include extracellular adhesins that mediate interactions with other bacteria as well as the extracellular matrix, and a host of degradative enzymes that are responsible for tissue degradation and spread of the organism including the gingipains, which are trypsin-like cysteine proteases.