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

J. Mihara, S. C. Holt

Research output: Contribution to journalArticlepeer-review

12 Scopus citations

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- propanesulfonate (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°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.

Original languageEnglish (US)
Pages (from-to)588-595
Number of pages8
JournalInfection and immunity
Volume61
Issue number2
StatePublished - Jan 1 1993

ASJC Scopus subject areas

  • Parasitology
  • Microbiology
  • Immunology
  • Infectious Diseases

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