Arginine-gingipain-specific IgG in the sera of human patients with periodontal disease is required for opsonophagocytosis of Porphyromonas gingivalis
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Abstract
Porphyromonas gingivalis is a primary etiologic agent of generalized aggressive periodontal disease (GAP), and gingipains, a group of cysteine proteinases, are critical virulence factors expressed by this organism. Gingipains are classified into two groups based on substrate specificity for arginine (Rgp A and RgpB) or lysine (Kgp) residues. In this study we characterized the levels of P. gingivalis-, and gingipain-specific IgG in sera of GAP patients, and examined the ability of gingipain-specific antibodies to facilitate opsonophagocytosis of P. gingivalis by human PMNs using a fluorescent phagocytosis assay. GAP patient sera possessed elevated levels of P. gingivalis-, arginine-gingipain (Rgp)A-, RgpB-, and lysine-gingipain (Kgp)-specific lgG (Kgp>RgpA>P. gingivalis>RgpB). Adsorption of GAP sera with P. gingivalis whole organisms, RgpA-, or RgpB-, but not Kgp-conjugated to sepharose beads significantly reduced opsonophagocytosis of P. gingivalis by PMNs. Our studies demonstrate that GAP patients possess elevated levels of P. gingivalis, and gingipain-specific IgG, demonstrate that arginine-gingipa. in antibodies promote uptake of P. gingivalis by PMNs, and establish that arginine gingipain-specific antibodies are important for control of P. gingivalis infections.
Description
Thesis (M.S.D)--Boston University, Goldman School of Dental Medicine, 2003 (Oral Biology).
Includes bibliographical references (leaves 48-59).
Includes bibliographical references (leaves 48-59).
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