Abstract
Nine classes of group B colicin-resistant mutants were examined to study the role of enterochelin in colicin resistance. Four of the mutants studied (cbt, exbC, exbB, and tonB) hypersecreted enterochelin. Enterochelin hypersecretion was apparently responsible for resistance of the exbC mutant to colicins G and H and for resistance of the exbB mutant to colicins G, H, Ia, Ib, S1, and V. All four mutants scored as colicin B tolerant, even in the absence of enterochelin synthesis. The mutants produced substantially increased amounts of two high-molecular-weight outer membrane polypeptides when grown under limiting iron conditions. The presence of these polypeptides was correlated with increased colicin B-neutralizing activity in the outer membrane preparations.
MeSH Terms
2,2'-Dipyridyl/pharmacology
Bacterial Proteins/biosynthesis
Cell Membrane/metabolism
Citrates/pharmacology
Colicins/pharmacology
Deferoxamine/pharmacology
Drug Resistance, Microbial
Edetic Acid/pharmacology
Enterobactin/metabolism,pharmacology
Escherichia coli/drug effects,metabolism
Genes
Molecular Weight
Mutation
Peptide Biosynthesis
Serine/analogs & derivatives
Chemicals
Bacterial Proteins
Citrates
Colicins
Enterobactin
Serine
2,2'-Dipyridyl
Edetic Acid
Deferoxamine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Pugsley A P
Reeves P
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28 references, click to expand
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