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) Corrigendum (v152,p2865) 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 Ulett, G. C. Articles by Schembri, M. A. Search for Related Content PubMed PubMed Citation Articles by Ulett, G. C. Articles by Schembri, M. A. Agricola Articles by Ulett, G. C. Articles by Schembri, M. A.

Antigen-43-mediated autoaggregation impairs motility in Escherichia coli

¹ School of Molecular and Microbial Sciences, University of Queensland, Brisbane, Queensland 4072, Australia
² Centre for Microscopy and Microanalysis, University of Queensland, Brisbane, Queensland 4072, Australia

Correspondence
Mark A. Schembri
m.schembri{at}uq.edu.au

Functional interaction between bacterial surface-displayed autoaggregation proteins such as antigen 43 (Ag43) of Escherichia coli and motility organelles such as flagella has not previously been described. Here, it has been demonstrated for the first time that Ag43-mediated aggregation can inhibit bacterial motility. Ag43 overexpression produces a dominant aggregation phenotype that overrides motility in the presence of low levels of flagella. In contrast, induction of an increased flagellation state prevents Ag43-mediated aggregation. This phenomenon was observed in naturally occurring subpopulations of E. coli as phase variants expressing and not expressing Ag43 revealed contrasting motility phenotypes. The effects were shown to be part of a general mechanism because other short adhesins capable of mediating autoaggregation (AIDA-I and TibA) also impaired motility. These novel insights into the function of bacterial autoaggregation proteins suggest that a balance between these two systems, i.e. autoaggregation and flagellation, influences motility.

This article has been cited by other articles:

				E. Hart, J. Yang, M. Tauschek, M. Kelly, M. J. Wakefield, G. Frankel, E. L. Hartland, and R. M. Robins-Browne RegA, an AraC-Like Protein, Is a Global Transcriptional Regulator That Controls Virulence Gene Expression in Citrobacter rodentium Infect. Immun., November 1, 2008; 76(11): 5247 - 5256. [Abstract] [Full Text] [PDF]

				J. Valle, A. N. Mabbett, G. C. Ulett, A. Toledo-Arana, K. Wecker, M. Totsika, M. A. Schembri, J.-M. Ghigo, and C. Beloin UpaG, a New Member of the Trimeric Autotransporter Family of Adhesins in Uropathogenic Escherichia coli J. Bacteriol., June 15, 2008; 190(12): 4147 - 4161. [Abstract] [Full Text] [PDF]

				R. M. Q. Shanks, N. A. Stella, E. J. Kalivoda, M. R. Doe, D. M. O'Dee, K. L. Lathrop, F. L. Guo, and G. J. Nau A Serratia marcescens OxyR Homolog Mediates Surface Attachment and Biofilm Formation J. Bacteriol., October 15, 2007; 189(20): 7262 - 7272. [Abstract] [Full Text] [PDF]

				G. C. Ulett, A. N. Mabbett, K. C. Fung, R. I. Webb, and M. A. Schembri The role of F9 fimbriae of uropathogenic Escherichia coli in biofilm formation Microbiology, July 1, 2007; 153(7): 2321 - 2331. [Abstract] [Full Text] [PDF]

				G. C. Ulett, J. Valle, C. Beloin, O. Sherlock, J.-M. Ghigo, and M. A. Schembri Functional Analysis of Antigen 43 in Uropathogenic Escherichia coli Reveals a Role in Long-Term Persistence in the Urinary Tract Infect. Immun., July 1, 2007; 75(7): 3233 - 3244. [Abstract] [Full Text] [PDF]