Sep, 1995
IMMUNOLOGICAL CHARACTERIZATION AND LOCALIZATION OF A PORPHYROMONAS-GINGIVALIS BAPNA-HYDROLYZING PROTEASE POSSESSING HEMAGGLUTINATING ACTIVITY
FEMS MICROBIOLOGY LETTERS
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- Volume
- 131
- Number
- 2
- First page
- 211
- Last page
- 217
- Language
- English
- Publishing type
- DOI
- 10.1016/0378-1097(95)00261-3
- Publisher
- ELSEVIER SCIENCE BV
A monoclonal antibody (mAb-PC) was produced against a BA pNA-hydrolyzing protease possessing hemagglutinating activity (Pase-C) from Porphyromonas gingivalis. Other P. gingivalis BA pNA-hydrolyzing enzymes (Pase-B and Pase-S) did not react with this antibody. By ELISA or SDS-PAGE and Western immunoblotting analysis, mAb-PC recognized all P. gingivalis and P. endodontalis strains tested but did not recognize other members of the Porphyromonas genus nor other putative periodontopathogenic organisms. Pase-C, extracellular vesicles (ECV) and human strains of P. gingivalis showed two major immunoreactive bands (44 kDa and 40 kDa), whereas a different pattern was obtained with animal strains of P. gingivalis. Biotinylarginyl chloromethane, an irreversible inhibitor of trypsin-like proteases, did not affect the reactivity of Pase-C with mAb-PC on immunoblot. By reversed-phase electronmicroscopy following immunogold labeling, the antibody was shown to bind to the cell surface of P. gingivalis. mAb-PC inhibited the hemagglutinating activity of both P. gingivalis cells and ECV whereas a monoclonal antibody against LPS of P. gingivalis did not. These results suggest that Pase-C is located on the cell surface of P. gingivalis and may participate in erythrocyte binding.
- Link information
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- DOI
- https://doi.org/10.1016/0378-1097(95)00261-3
- CiNii Articles
- http://ci.nii.ac.jp/naid/80008490898
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/7557332
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:A1995RT10400016&DestApp=WOS_CPL
- ID information
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- DOI : 10.1016/0378-1097(95)00261-3
- ISSN : 0378-1097
- CiNii Articles ID : 80008490898
- Pubmed ID : 7557332
- Web of Science ID : WOS:A1995RT10400016