Premium
Generation and characterization of a monoclonal antibody specific for the major thiol‐activated cysteine proteinase of Porphyromonas gingivalis W83
Author(s) -
Wallace A.,
Rigg G.,
Hymanf S.C.,
James R.,
Roberts I.S.
Publication year - 1992
Publication title -
letters in applied microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.698
H-Index - 110
eISSN - 1472-765X
pISSN - 0266-8254
DOI - 10.1111/j.1472-765x.1992.tb00763.x
Subject(s) - porphyromonas gingivalis , monoclonal antibody , immunogold labelling , biology , microbiology and biotechnology , antibody , bacteroidaceae , western blot , bacterial outer membrane , proteinase k , bacteria , biochemistry , enzyme , immunology , escherichia coli , genetics , gene
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.