1977
DOI: 10.1128/jb.130.1.540-541.1977
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Further characterization of the recipient ability of Escherichia coli K-12 bacteriophage-resistant mutants

Abstract: We extended the study of Escherichia coli mutants defective in conjugation and showed that the mutants with altered lipopolysaccharide, which are defective as recipients with F-like donors, are also defective with the I-like plasmid R64-11. However, the extent of reduction in recipient ability for I-like donors does not correlate either with the effect on recipient ability for F-like donors or with the degree of alteration to the lipopolysaccharide.

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Cited by 6 publications
(1 citation statement)
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“…The pilin proteins of F-like plasmids are highly conserved in sequence (26), which could imply that they interact with the same outer membrane component. However, this assumption now seems less likely, as F-like plasmids such as R100-1 transfer at normal frequencies to ompA mutant strains that prevent the transfer of F DNA (53). Additionally, studies on bacteriophage host range mutants have shown that single-amino-acid alterations in the adhesin proteins of the phages allow completely different outer membrane proteins to serve as phage receptors (79).…”
Section: Surface Exclusionmentioning
confidence: 99%
“…The pilin proteins of F-like plasmids are highly conserved in sequence (26), which could imply that they interact with the same outer membrane component. However, this assumption now seems less likely, as F-like plasmids such as R100-1 transfer at normal frequencies to ompA mutant strains that prevent the transfer of F DNA (53). Additionally, studies on bacteriophage host range mutants have shown that single-amino-acid alterations in the adhesin proteins of the phages allow completely different outer membrane proteins to serve as phage receptors (79).…”
Section: Surface Exclusionmentioning
confidence: 99%