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Infect Immun. 1993 February; 61(2): 588-595

Purification and characterization of fibroblast-activating factor isolated from Porphyromonas gingivalis W50.

Department of Periodontics, University of Texas Health Science Center, San Antonio 78284-7894.

ABSTRACT

A 24-kDa polypeptide which activated the incorporation of [3H]thymidine into human fibroblasts was isolated from the outer membrane vesicles of Porphyromonas gingivalis W50. This polypeptide, named fibroblast activating factor (FAF), was isolated by 3-[(3-cholamidopropyl)-dimethyl-ammonio]-1-propane-sulfonate (CHAPS) detergent extraction and purified by DEAE ion-exchange chromatography and preparative isoelectric focusing. Purified FAF (100 ng of protein per ml) caused a 400% increase in [3H]thymidine incorporation into human gingival fibroblasts (HGFs) compared with results for controls. FAF was characterized as (i) a polypeptide with molecular masses of 24 kDa when heated at 100 degrees C for 5 min and 44 kDa when unheated, (ii) heat sensitive but not affected by selected reducing reagents, and (iii) possessing slight phosphatase activity. N'-terminal sequence analysis revealed no homology with P. gingivalis peptides or with any host-derived growth factors. These data suggest that FAF functions as a significant virulence factor which in vivo is capable of modulating homeostasis in local connective tissues.

This article has been cited by other articles:

• Kawai, T., Ito, H.-O, Sakato, N., Okada, H. (1998). A Novel Approach for Detecting an Immunodominant Antigen of Porphyromonas gingivalis in Diagnosis of Adult Periodontitis. CVI 5: 11-17 [Abstract] [Full Text]