Generation and characterization of a monoclonal antibody specific for the major thiol-activated cysteine proteinase of Porphyromonas gingivalis W83

• Published in: Letters in applied microbiology Vol. 15; no. 5; p. 202
• Main Authors: Wallace, A, Rigg, G, Hyman, S C, James, R, Roberts, I S
• Format: Journal Article
• Language: English
• Published: England 01-11-1992
• Subjects: Antibodies, Bacterial - biosynthesis; Antibodies, Monoclonal - biosynthesis; Cysteine Endopeptidases - analysis; Cysteine Endopeptidases - immunology; Immunoglobulin M - biosynthesis; Microscopy, Immunoelectron; Porphyromonas gingivalis - enzymology; Porphyromonas gingivalis - immunology
• ISSN: 0266-8254
• DOI: 10.1111/j.1472-765X.1992.tb00763.x

An IgM monoclonal antibody specified for the thiol-activated proteinase of the oral pathogen Porphyromonas gingivalis W83 was generated. The antibody reacted with a single protein of approximate molecular mass 43 kDa in outer membrane preparations of P. gingivalis. Immuno-electron microscopy using the monoclonal antibody and immunogold labelling confirmed the cell surface location of the thiol-activated proteinase. The monoclonal antibody failed to detect any proteins in Western blot analysis of other closely related oral bacteria. The specificity of this monoclonal antibody to the thiol-activated proteinase of P. gingivalis should allow its use as a diagnostic tool for the rapid enumeration of P. gingivalis in clinical samples.