Arginine-gingipain-specific IgG in the sera of human patients with periodontal disease is required for opsonophagocytosis of Porphyromonas gingivalis

Date
2003
DOI
Authors
Savelli, Juan E.
Version
OA Version
Citation
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).
License
This work is being made available in OpenBU by permission of its author, and is available for research purposes only. All rights are reserved to the author.