|
|
||||||||
Research Paper |
Departments of Oral Infectious Diseases and Immunology1, Endodontology and Operative Dentistry2 and Pharmacology3, Faculty of Dental Science, Kyushu University, Fukuoka812-8582, Japan
Department of Microbiology, School of Dentistry, Aichi-Gakuin University, Nagoya464-8650, Japan4
Department of Medical Microbiology, Division of Molecular Pathology Infection and Immunity, St Bartholomews and the Royal London School of Medicine and Dentistry, London E1 2AA, UK5
Department of Microbiology, School of Dentistry, Nagasaki University, Nagasaki 852-8588, Japan6
Author for correspondence: Koji Nakayama. Tel: +81 95 849 7648. Fax: +81 95 849 7650. e-mail: knak{at}net.nagasaki-u.ac.jp
A nonpigmented mutant of Porphyromonas gingivalis was constructed by using transposon mutagenesis. The mutant possessed the transposon DNA at the novel gene porR. Gene targeted mutagenesis revealed that porR was responsible for pigmentation. The porR gene shared similarities with genes of the degT family, the products of which are now considered to be transaminases involved in biosynthesis of sugar portions of cell-surface polysaccharides and aminoglycosides. The porR mutant showed a pleiotropic phenotype: delayed maturation of fimbrillin, preferential presence of Rgp and Kgp proteinases in culture supernatants, and no haemagglutination. The porR mutant had altered phenol extractable polysaccharide compared to the porR+ sibling strain. A mAb, 1B5, that reacts with sugar portions of P. gingivalis cell surface polysaccharide and membrane-type Rgp proteinase showed no reaction with the cell lysates of the porR mutant. These results indicate that porR is involved in biosynthesis of cell surface polysaccharide that may function as an anchorage for Rgp, Kgp, haemagglutinins and the haemoglobin receptor protein.
Keywords: cell surface polysaccharide, cysteine proteinases, colonial pigmentation, haemagglutination, fimbrillin maturation
Abbreviations: HA, haemagglutinin; HbR, haemoglobin receptor protein; Kgp, Lys-gingipain; mt, membrane type; Rgp, Arg-gingipain; TLCK, N
-p-tosyl-L-lysine chloromethyl ketone
The GenBank/EMBL/DDBJ accession number for the sequences reported in this paper is D64132.
a M.S. and D.B.R. contributed equally to this work.
b Present address: Department of Microbiology, School of Dentistry, Nagasaki University, Nagasaki 852-8588, Japan.
This article has been cited by other articles:
![]() |
M. Rangarajan, J. Aduse-Opoku, N. Paramonov, A. Hashim, N. Bostanci, O. P. Fraser, E. Tarelli, and M. A. Curtis Identification of a Second Lipopolysaccharide in Porphyromonas gingivalis W50 J. Bacteriol., April 15, 2008; 190(8): 2920 - 2932. [Abstract] [Full Text] [PDF] |
||||
![]() |
M. J. Coyne and L. E. Comstock Niche-Specific Features of the Intestinal Bacteroidales J. Bacteriol., January 15, 2008; 190(2): 736 - 742. [Abstract] [Full Text] [PDF] |
||||
![]() |
K.-A. Nguyen, J. Travis, and J. Potempa Does the Importance of the C-Terminal Residues in the Maturation of RgpB from Porphyromonas gingivalis Reveal a Novel Mechanism for Protein Export in a Subgroup of Gram-Negative Bacteria? J. Bacteriol., February 1, 2007; 189(3): 833 - 843. [Abstract] [Full Text] [PDF] |
||||
![]() |
J. M. Slaney, A. Gallagher, J. Aduse-Opoku, K. Pell, and M. A. Curtis Mechanisms of Resistance of Porphyromonas gingivalis to Killing by Serum Complement Infect. Immun., September 1, 2006; 74(9): 5352 - 5361. [Abstract] [Full Text] [PDF] |
||||
![]() |
C. A. Seers, N. Slakeski, P. D. Veith, T. Nikolof, Y.-Y. Chen, S. G. Dashper, and E. C. Reynolds The RgpB C-Terminal Domain Has a Role in Attachment of RgpB to the Outer Membrane and Belongs to a Novel C-Terminal-Domain Family Found in Porphyromonas gingivalis. J. Bacteriol., September 1, 2006; 188(17): 6376 - 6386. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Vanterpool, F. Roy, and H. M. Fletcher Inactivation of vimF, a Putative Glycosyltransferase Gene Downstream of vimE, Alters Glycosylation and Activation of the Gingipains in Porphyromonas gingivalis W83 Infect. Immun., July 1, 2005; 73(7): 3971 - 3982. [Abstract] [Full Text] [PDF] |
||||
![]() |
K. Sato, E. Sakai, P. D. Veith, M. Shoji, Y. Kikuchi, H. Yukitake, N. Ohara, M. Naito, K. Okamoto, E. C. Reynolds, et al. Identification of a New Membrane-associated Protein That Influences Transport/Maturation of Gingipains and Adhesins of Porphyromonas gingivalis J. Biol. Chem., March 11, 2005; 280(10): 8668 - 8677. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Vanterpool, F. Roy, L. Sandberg, and H. M. Fletcher Altered Gingipain Maturation in vimA- and vimE-Defective Isogenic Mutants of Porphyromonas gingivalis Infect. Immun., March 1, 2005; 73(3): 1357 - 1366. [Abstract] [Full Text] [PDF] |
||||
![]() |
R. Takii, T. Kadowaki, A. Baba, T. Tsukuba, and K. Yamamoto A Functional Virulence Complex Composed of Gingipains, Adhesins, and Lipopolysaccharide Shows High Affinity to Host Cells and Matrix Proteins and Escapes Recognition by Host Immune Systems Infect. Immun., February 1, 2005; 73(2): 883 - 893. [Abstract] [Full Text] [PDF] |
||||
![]() |
E. Vanterpool, F. Roy, and H. M. Fletcher The vimE Gene Downstream of vimA Is Independently Expressed and Is Involved in Modulating Proteolytic Activity in Porphyromonas gingivalis W83 Infect. Immun., October 1, 2004; 72(10): 5555 - 5564. [Abstract] [Full Text] [PDF] |
||||
![]() |
D. Grenier, S. Roy, F. Chandad, P. Plamondon, M. Yoshioka, K. Nakayama, and D. Mayrand Effect of Inactivation of the Arg- and/or Lys-Gingipain Gene on Selected Virulence and Physiological Properties of Porphyromonas gingivalis Infect. Immun., August 1, 2003; 71(8): 4742 - 4748. [Abstract] [Full Text] [PDF] |
||||
![]() |
G. J. Olango, F. Roy, S. M. Sheets, M. K. Young, and H. M. Fletcher Gingipain RgpB Is Excreted as a Proenzyme in the vimA-Defective Mutant Porphyromonas gingivalis FLL92 Infect. Immun., July 1, 2003; 71(7): 3740 - 3747. [Abstract] [Full Text] [PDF] |
||||
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| INT J SYST EVOL MICROBIOL | MICROBIOLOGY | J GEN VIROL |
| J MED MICROBIOL | ALL SGM JOURNALS | |