title: Surface components of Porphyromonas gingivalis.
abstract: OBJECTIVE
  Research on Porphyromonas gingivalis, a periodontopathogen, has provided a tremendous amount of information over the last 20 years, which may exceed in part than that on other closely related members in terms of phylogenetic as well as proteomic criteria, including Bacteroides fragilis and B. thetaiotaomicron as major anaerobic, opportunistic pathogens in the medical field. In this minireview, we focused on recent research findings concerning surface components such as outer membrane proteins and fimbriae, of P. gingivalis.
  
  
  METHODS
  Elucidation of the surface components in P. gingivalis was especially difficult because outer membrane proteins are tightly bound to lipopolysaccharide and they are resistant to dissociation and separation from each other, even during sodium dodecyl sulfate-polyacrylamide gel electrophoresis, unless samples are appropriately heated. In addition, P. gingivalis is asaccharolytic and therefore a potent proteolytic bacterium, another factor causing difficulty in research. The study of the surface components was carefully carried out considering these unique features in P. gingivalis when compared with other gram-negative bacteria, including Escherichia coli and Pseudomonas aeruginosa.
  
  
  RESULTS
  Separation of outer membrane proteins, and characterization of OmpA-like proteins and RagAB as major proteins, is described herein. Our recent findings on FimA and Mfa1 fimbriae, two unique appendages in this organism, and on their regulation of expression are also described briefly.
  
  
  CONCLUSIONS
  Surface components of P. gingivalis somehow have contact with host tissues and cells because of the outermost cell elements. Therefore, such bacterial components are potentially important in the occurrence of periodontal diseases.
authors.affiliation: Department of Microbiology, School of Dentistry, Aichi-Gakuin University, Nagoya, Aichi, Japan. fuminobu@dpc.agu.ac.jp
authors.forename: F
authors.initials: F
authors.lastname: Yoshimura
authors.forename: Y
authors.initials: Y
authors.lastname: Murakami
authors.forename: K
authors.initials: K
authors.lastname: Nishikawa
authors.forename: Y
authors.initials: Y
authors.lastname: Hasegawa
authors.forename: S
authors.initials: S
authors.lastname: Kawaminami
mesh_terms: D001425:Bacterial Outer Membrane Proteins / Q000145:classification*; D001426:Bacterial Proteins / Q000145:classification; D001439:Bacteroides / Q000378:metabolism; D036781:Fimbriae Proteins / Q000145:classification; D010861:Fimbriae, Bacterial / Q000737:chemistry; D006801:Humans; D010802:Phylogeny; D018933:Pili, Sex / Q000737:chemistry; D016966:Porphyromonas gingivalis / Q000378:metabolism*; D020543:Proteome / Q000145:classification
chemical_list: D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D020543:Proteome; C484343:RagA protein, Porphyromonas gingivalis; C484346:RagB protein, bacteria; C063055:fimbrillin; D036781:Fimbriae Proteins; C078167:OMPA outer membrane proteins