HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Rakotoarivonina, H. Articles by Mosoni, P. Search for Related Content PubMed PubMed Citation Articles by Rakotoarivonina, H. Articles by Mosoni, P. Agricola Articles by Rakotoarivonina, H. Articles by Mosoni, P.

Adhesion to cellulose of the Gram-positive bacterium Ruminococcus albus involves type IV pili

Unité de Microbiologie¹ and Unité de Recherches sur la Viande, Equipe Microbiologie², INRA, Centre de Recherches de Clermont-Ferrand-Theix, 63122 Saint-Genès-Champanelle, France

Author for correspondence: Pascale Mosoni. Tel: +33 4 73 62 40 45. Fax: +33 4 73 62 45 81. e-mail: pmosoni{at}clermont.inra.fr

This study was aimed at characterizing a cell-surface 25 kDa glycoprotein (GP25) that was previously shown to be underproduced by a spontaneous adhesion-defective mutant D5 of Ruminococcus albus 20. An antiserum against wild-type strain 20 was adsorbed with the mutant D5 to enrich it in antibodies ‘specific’ to adhesion structures of R. albus 20. The resulting antiserum, called anti-Adh serum, blocked adhesion of R. albus 20 and reacted mainly with GP25 in bacterial and extracellular protein fractions of R. albus 20. The N-terminal sequence of purified GP25 was identical to that of CbpC, a 21 kDa cellulose-binding protein (CBP) of R. albus 8. The nucleotide sequence of the gp25 gene was determined by PCR and genomic walking procedures. The gp25 gene encoded a protein of 165 aa with a calculated molecular mass of 16940 Da that showed 72·9% identity with CbpC and presented homologies with type IV pilins of Gram-negative pathogenic bacteria. Negative-staining electron microscopy revealed fine and flexible pili surrounding R. albus 20 cells while mutant cells were not piliated. In addition, immunoelectron microscopy showed that the anti-Adh serum probing mainly GP25, completely decorated the pili surrounding R. albus 20, thereby showing that GP25 was a major pilus subunit. This study shows for the first time the presence of pili at the surface of R. albus and identifies GP25 as their major protein subunit. Though GP25 was not identified as a CBP, isolated pili were shown to bind cellulose. In conclusion, these pili, which belong to the family of type IV pili, mediate adhesion of R. albus 20 to cellulose.

Keywords: adhesion-defective mutant, cell-surface glycoprotein, cloning of type IV pilin, immunoelectron microscopy

Abbreviations: CBP, cellulose-binding protein; GP25, cell-surface 25kDa glycoprotein

The EMBL accession number for the sequence reported in this paper is AJ416469.

This article has been cited by other articles:

				J. Koo, S. Tammam, S.-Y. Ku, L. M. Sampaleanu, L. L. Burrows, and P. L. Howell PilF Is an Outer Membrane Lipoprotein Required for Multimerization and Localization of the Pseudomonas aeruginosa Type IV Pilus Secretin J. Bacteriol., November 1, 2008; 190(21): 6961 - 6969. [Abstract] [Full Text] [PDF]

				M. Mendez, I-H. Huang, K. Ohtani, R. Grau, T. Shimizu, and M. R. Sarker Carbon Catabolite Repression of Type IV Pilus-Dependent Gliding Motility in the Anaerobic Pathogen Clostridium perfringens J. Bacteriol., January 1, 2008; 190(1): 48 - 60. [Abstract] [Full Text] [PDF]

				S. Helaine, D. H. Dyer, X. Nassif, V. Pelicic, and K. T. Forest 3D structure/function analysis of PilX reveals how minor pilins can modulate the virulence properties of type IV pili PNAS, October 2, 2007; 104(40): 15888 - 15893. [Abstract] [Full Text] [PDF]

				H.-S. Jun, M. Qi, J. Gong, E. E. Egbosimba, and C. W. Forsberg Outer Membrane Proteins of Fibrobacter succinogenes with Potential Roles in Adhesion to Cellulose and in Cellulose Digestion J. Bacteriol., October 1, 2007; 189(19): 6806 - 6815. [Abstract] [Full Text] [PDF]

				P. Xu, J. M. Alves, T. Kitten, A. Brown, Z. Chen, L. S. Ozaki, P. Manque, X. Ge, M. G. Serrano, D. Puiu, et al. Genome of the Opportunistic Pathogen Streptococcus sanguinis J. Bacteriol., April 15, 2007; 189(8): 3166 - 3175. [Abstract] [Full Text] [PDF]

				P. J. Weimer, N. P. J. Price, O. Kroukamp, L.-M. Joubert, G. M. Wolfaardt, and W. H. Van Zyl Studies of the Extracellular Glycocalyx of the Anaerobic Cellulolytic Bacterium Ruminococcus albus 7 Appl. Envir. Microbiol., December 1, 2006; 72(12): 7559 - 7566. [Abstract] [Full Text] [PDF]

				C. Saarimaa, M. Peltola, M. Raulio, T. R. Neu, M. S. Salkinoja-Salonen, and P. Neubauer Characterization of Adhesion Threads of Deinococcus geothermalis as Type IV Pili. J. Bacteriol., October 1, 2006; 188(19): 7016 - 7021. [Abstract] [Full Text] [PDF]

				H. Rakotoarivonina, M. A. Larson, M. Morrison, J.-P. Girardeau, B. Gaillard-Martinie, E. Forano, and P. Mosoni The Ruminococcus albus pilA1-pilA2 locus: expression and putative role of two adjacent pil genes in pilus formation and bacterial adhesion to cellulose Microbiology, April 1, 2005; 151(4): 1291 - 1299. [Abstract] [Full Text] [PDF]

				E. Devillard, D. B. Goodheart, S. K. R. Karnati, E. A. Bayer, R. Lamed, J. Miron, K. E. Nelson, and M. Morrison Ruminococcus albus 8 Mutants Defective in Cellulose Degradation Are Deficient in Two Processive Endocellulases, Cel48A and Cel9B, Both of Which Possess a Novel Modular Architecture J. Bacteriol., January 1, 2004; 186(1): 136 - 145. [Abstract] [Full Text] [PDF]