Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 148 (2002), 1183-1191
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Shoji, M.
Right arrow Articles by Nakayama, K.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Shoji, M.
Right arrow Articles by Nakayama, K.
Agricola
Right arrow Articles by Shoji, M.
Right arrow Articles by Nakayama, K.
Microbiology (2002), 148, 1183-1191.
© 2002 Society for General Microbiology


Research Paper

Construction and characterization of a nonpigmented mutant of Porphyromonas gingivalis: cell surface polysaccharide as an anchorage for gingipains

Mikio Shojia,b,1,2, Dinath B. Ratnayakea,1, Yixin Shi1, Tomoko Kadowaki3, Kenji Yamamoto3, Fuminobu Yoshimura4, Akifumi Akamine2, Michael A. Curtis5 and Koji Nakayama6

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 Bartholomew’s 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{alpha}-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:


Home page
J. Bacteriol.Home page
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]


Home page
J. Bacteriol.Home page
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]


Home page
J. Bacteriol.Home page
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]


Home page
Infect. Immun.Home page
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]


Home page
J. Bacteriol.Home page
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]


Home page
Infect. Immun.Home page
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]


Home page
J. Biol. Chem.Home page
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]


Home page
Infect. Immun.Home page
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]


Home page
Infect. Immun.Home page
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]


Home page
Infect. Immun.Home page
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]


Home page
Infect. Immun.Home page
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]


Home page
Infect. Immun.Home page
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
Copyright © 2002 Society for General Microbiology.