Source:http://linkedlifedata.com/resource/pubmed/id/13680205
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2004-4-1
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pubmed:abstractText |
Twenty six phages infected with Escherichia coli O157:H7 were screened from various sources. Among them, nine caused visible lysis of E. coli O157:H7 cells in LB liquid medium. However, prolonged incubation of E. coli cells and phage allowed the emergence of phage-resistant cells. The susceptibility of the phage-resistant cells to the nine phages was diverse. A rational procedure for selecting an effective cocktail of phage for controlling bacteria was investigated based on the mechanism of phage-resistant cell conversion. Deletion of OmpC from the E. coli cells facilitated the emergence of cells resistant to SP21 phage. After 8 h of incubation, SP21-resistant cells appeared. By contrast, alteration of the lipopolysaccharide (LPS) profile facilitated cell resistance to SP22 phage, which was observed following a 6-h incubation. When a cocktail of phages SP21 and SP22 was used to infect E. coli O157:H7 cells, 30 h was required for the emergence of cells (R-C) resistant to both phages. The R-C cells carried almost the same outer membrane and LPS components as the wild-type cells. However, the reduced binding ability of both phages to R-C cells suggested disturbance of phage adsorption to the R-C surface. Even though R-C cells resistant to both phages appeared, this work shows that rational selection of phages has the potential to at least delay the emergence of phage resistance.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Outer Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Lipopolysaccharides,
http://linkedlifedata.com/resource/pubmed/chemical/OmpC protein,
http://linkedlifedata.com/resource/pubmed/chemical/Porins,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Virus
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pubmed:status |
MEDLINE
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pubmed:month |
Apr
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pubmed:issn |
0175-7598
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
64
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
270-4
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pubmed:dateRevised |
2011-11-17
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pubmed:meshHeading |
pubmed-meshheading:13680205-Adsorption,
pubmed-meshheading:13680205-Bacterial Outer Membrane Proteins,
pubmed-meshheading:13680205-Bacterial Proteins,
pubmed-meshheading:13680205-Bacteriolysis,
pubmed-meshheading:13680205-Coliphages,
pubmed-meshheading:13680205-Escherichia coli O157,
pubmed-meshheading:13680205-Gene Deletion,
pubmed-meshheading:13680205-Genes, Bacterial,
pubmed-meshheading:13680205-Lipopolysaccharides,
pubmed-meshheading:13680205-Mutation,
pubmed-meshheading:13680205-Porins,
pubmed-meshheading:13680205-Receptors, Virus,
pubmed-meshheading:13680205-Viral Plaque Assay
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pubmed:year |
2004
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pubmed:articleTitle |
Toward rational control of Escherichia coli O157:H7 by a phage cocktail.
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pubmed:affiliation |
Department of Bioengineering, Tokyo Institute of Technology, 4259 Nagatsuta-cho, Midori-ku, 226-8501, Yokohama, Japan. ytanji@bio.titech.ac.jp
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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