Isolation and identification of the putative receptor for Porphyromonas ginivalis fimbria on human monocytes

Date
2004
DOI
Authors
Dave, Sheilesh
Version
OA Version
Citation
Abstract
It has been proposed that the first step in Porphyromonas gingivalis-induced periodontal infection is adherence to host tissues followed by invasion of host tissues and an inflammatory response. Fimbriae are involved in all of these processes. There have been several attempts to identify the receptor that is involved in binding to fimbriae on human cells. Most studies have utilized indirect methodologies and have implicated a diverse group of molecules. The purpose of this study was to determine by cross-1inking assay the molecule or molecules on human cells to which fimbriae bind most closely. Recombinant fimbriae tagged with histidine were used in a cross-linking assay involving monocytic cells. Following cross-linking, we lysed the cells, separated the proteins by SDS-PAGE, and subsequently identified the cross-linked complex using a Western blot. A 250Kd band was identified and cut out of an SDS Page gel and analyzed by Liquid Chromatography-Mass Spectroscopy-Mass Spectroscopy (LC-MS-MS). Based on LC-MS-MS results, keratin was identified as being the major cross-linked protein isolated. There is evidence in the literature to support the conclusion that fimbriae bind to keratin. However, further study will be necessary to fully establish this conclusion.
Description
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Thesis (M.S.D.)--Boston University, Goldman School of Dental Medicine 2004 (Periodontology and Oral Biology).
Includes bibliographical references (leaves 47-60).
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