Emergence of Biofilm-Forming Subpopulations upon Exposure of Escherichia coli to Environmental Bacteriophages

ABSTRACT Exposure of Escherichia coli MG1655 to environmental bacteriophages results in rapid selection for phage-tolerant subpopulations displaying increased biofilm formation. Analysis of one phage-tolerant strain revealed large amounts of the DNA-binding Dps protein in the outer membrane protein and production of fimbria-like structures. In dps and fimA mutant derivatives of MG1655, no selection of phage-tolerant bacteria upon exposure to bacteriophages occurred, suggesting a role for Dps and type I pili in bacteriophage tolerance.

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A new major outer membrane protein in derivatives of Escherichia coli carrying the virulence plasmid ColV-K94

Zeitschrift für allgemeine Mikrobiologie ◽

10.1002/jobm.19820220706 ◽

1982 ◽

Vol 22 (7) ◽

pp. 465-475

Author(s):

Jane C. Moores ◽

R. J. Rowbury

Keyword(s):

Escherichia Coli ◽

Membrane Protein ◽

Outer Membrane ◽

Outer Membrane Protein ◽

Major Outer Membrane Protein ◽

Virulence Plasmid ◽

Derivatives Of

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In Vivo Transfer of Plasmid-Encoded ACC-1 AmpC from Klebsiella pneumoniae to Escherichia coli in an Infant and Selection of Impermeability to Imipenem in K. pneumoniae

Antimicrobial Agents and Chemotherapy ◽

10.1128/aac.49.8.3562-3565.2005 ◽

2005 ◽

Vol 49 (8) ◽

pp. 3562-3565 ◽

Cited By ~ 40

Author(s):

Philippe Bidet ◽

Béatrice Burghoffer ◽

Valérie Gautier ◽

Naïma Brahimi ◽

Patricia Mariani-Kurkdjian ◽

...

Keyword(s):

Escherichia Coli ◽

Membrane Protein ◽

Klebsiella Pneumoniae ◽

Outer Membrane ◽

Outer Membrane Protein ◽

Major Outer Membrane Protein ◽

In Vivo Selection ◽

Selection Of

ABSTRACT We describe in vivo selection of a Klebsiella pneumoniae strain with diminished imipenem susceptibility attributable to plasmid-encoded ACC-1 β-lactamase production and loss of a 36-kDa major outer membrane protein, together with transfer of this plasmid from K. pneumoniae to Escherichia coli in a Tunisian infant.

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The Major Outer Membrane Protein MopB Is Required for Twitching Movement and Affects Biofilm Formation and Virulence in Two Xylella fastidiosa strains

Molecular Plant-Microbe Interactions ◽

10.1094/mpmi-07-17-0161-r ◽

2017 ◽

Vol 30 (11) ◽

pp. 896-905 ◽

Cited By ~ 9

Author(s):

Hongyu Chen ◽

Prem P. Kandel ◽

Luisa F. Cruz ◽

Paul A. Cobine ◽

Leonardo De La Fuente

Keyword(s):

Membrane Protein ◽

Outer Membrane ◽

Outer Membrane Protein ◽

Calcium Binding ◽

Biofilm Formation ◽

Xylella Fastidiosa ◽

Major Outer Membrane Protein ◽

Binding Motif ◽

Type I ◽

Twitching Motility

MopB is a major outer membrane protein (OMP) in Xylella fastidiosa, a bacterial plant pathogen that causes losses on many economically important crops. Based on in silico analysis, the uncharacterized MopB protein of X. fastidiosa contains a β-barrel structure with an OmpA-like domain and a predicted calcium-binding motif. Here, MopB function was studied by mutational analysis taking advantage of the natural competence of X. fastidiosa. Mutants of mopB were constructed in two different X. fastidiosa strains, the type strain Temecula and the more virulent WM1-1. Deletion of the mopB gene impaired cell-to-cell aggregation, surface attachment, and biofilm formation in both strains. Interestingly, mopB deletion completely abolished twitching motility. Electron microscopy of the bacterial cell surface revealed that mopB deletion eliminated type IV and type I pili formation, potentially caused by destabilization of the outer membrane. Both mopB mutants showed reduced virulence using tobacco (Nicotiana tabacum) as a host under greenhouse conditions. These results suggest that MopB has pleiotropic functions in biofilm formation and twitching motility and is important for virulence of X. fastidiosa.

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