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The cell surface protein Ag43 facilitates phage infection of Escherichia coli in the presence of bile salts and carbohydrates
KTH, Superseded Departments, Biotechnology.
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2002 (English)In: Microbiology, ISSN 1350-0872, E-ISSN 1465-2080, Vol. 148, 1533-1542 p.Article in journal (Refereed) Published
Abstract [en]

it was found that infection of Escherichia coli by bacteriophage lambda is inhibited in the presence of certain bile salts and carbohydrates when cells are in the 'OFF' state for production of the phase-variable cell surface protein antigen 43 (Ag43). The inhibition of phage growth was found to be due to a significant impairment in the process of phage adsorption. Expression of the gene encoding Ag43 (agn43) from a plasmid or inactivation of the oxyR gene (encoding an activator of genes important for defence against oxidative stress) suppressed this inhibition. A mutation, rpoA341, in the gene encoding the alpha subunit of RNA polymerase also facilitated phage adsorption in the presence of bile salts and carbohydrates. The rpoA341 mutation promoted efficient production of Ag43 in a genetic background that would otherwise be in the 'OFF' phase for expression of the agn43 gene. Analysis of a reporter gene fusion demonstrated that the promoter for the agn43 gene was more active in the rpoA341 mutant than in the otherwise isogenic rpoA(+) strain. The combined inhibitory action of bile salts and carbohydrates on phage adsorption and the abolition of this inhibition by production of Ag43 was not restricted to lambda as a similar phenomenon was observed for the coliphages P1 and T4.

Place, publisher, year, edition, pages
2002. Vol. 148, 1533-1542 p.
Keyword [en]
bacteriophage infection, MacConkey agar, antigen 43, RNA polymerase alpha subunit, phase switching, polymerase alpha-subunit, outer-membrane protein, bacteriophage-lambda, colony morphology, transcriptional activation, rpoa341 mutant, antigen-43, oxyr, cii, gene
URN: urn:nbn:se:kth:diva-21558ISI: 000175727900032OAI: diva2:340256
QC 20100525Available from: 2010-08-10 Created: 2010-08-10Bibliographically approved

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