Copper sensitivity in an envelope mutant of Escherichia coli and its suppression by ColV, I-K94

Abstract

A phage K3-resistant isolate from Escherichia coli P678-54 was devoid of both the OmpA and OmpC proteins but had high levels of the OmpF protein. Associated with these changes, the strain showed increased sensitivity to inhibition by detergents and greatly increased sensitivity to Cu2+. Introduction of the ColV, I-K94 plasmid into this mutant produced a derivative with markedly increased resistance to Cu2+ ions but unchanged detergent sensitivity. Analysis of membranes showed that the ColV, I-K94+ derivative had essentially no OmpF protein in its outer membrane. A ca 36 K outer membrane protein was present which resembled the OmpC protein in size and failure to dissociate in SDS at low temperature. It was distinct from the OmpC protein, however, in failing to allow either tetracycline uptake or the adsorption of T4-type phages. The possible significance of OmpF porin derepression (and its reversal by ColV, I-K94) for enterobacterial survival in aquatic situations is discussed.