Affiliation:
1. The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.
Abstract
Filamentous phage f1 exits its
Escherichia coli
host without killing the bacterial cell. It has been proposed that f1 is secreted through the outer membrane via a phage-encoded channel protein, pIV. A functional pIV mutant was isolated that allowed
E. coli
to grow on large maltodextrins and rendered
E. coli
sensitive to large hydrophilic antibiotics that normally do not penetrate the outer membrane. In planar lipid bilayers, both mutant and wild-type pIV formed highly conductive channels with similar permeability characteristics but different gating properties: the probability of the wild-type channel being open was much less than that of the mutant channel. The high conductivity of pIV channels suggests a large-diameter pore, thus implicating pIV as the outer membrane phage-conducting channel.
Publisher
American Association for the Advancement of Science (AAAS)
Reference28 articles.
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4. D. K. Marciano M. Russel S. M. Simon unpublished observations.
5. Escherichia coli containing a mutagenized population of gene IV were originally screened for sensitivity to the detergent deoxycholate [
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