Antigen-43-mediated autoaggregation impairs motility in Escherichia coli

Ulett, G. C., Webb, R. I. and Schembri, M. A. (2006) Antigen-43-mediated autoaggregation impairs motility in Escherichia coli. Microbiology-sgm, 152 2101-2110. doi:10.1099/mic.0.28607-0

Author Ulett, G. C.
Webb, R. I.
Schembri, M. A.
Title Antigen-43-mediated autoaggregation impairs motility in Escherichia coli
Journal name Microbiology-sgm   Check publisher's open access policy
ISSN 1350-0872
Publication date 2006-07-01
Year available 2006
Sub-type Article (original research)
DOI 10.1099/mic.0.28607-0
Open Access Status
Volume 152
Start page 2101
End page 2110
Total pages 10
Place of publication Reading
Publisher Soc General Microbiology
Language eng
Subject C1
320401 Medical Bacteriology
780105 Biological sciences
0605 Microbiology
Abstract 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.
Keyword Microbiology
Outer-membrane Protein
Antigen 43
Molecular Characterization
Autotransporter Protein
Aggregative Adherence
Colony Morphology
Phase Variation
Master Operon
Hep-2 Cells
Q-Index Code C1
Institutional Status UQ

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Created: Wed, 15 Aug 2007, 18:25:50 EST